{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"B6V6V5","uniProtkbId":"KSHA4_RHORH","entryAudit":{"firstPublicDate":"2016-11-30","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2008-12-16","entryVersion":56,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19561185"}],"value":"3-ketosteroid-9-alpha-monooxygenase, oxygenase component"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19561185"}],"value":"3-ketosteroid-9-alpha-hydroxylase, oxygenase component"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19561185"}],"value":"KSH"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19561185"}],"value":"Androsta-1,4-diene-3,17-dione 9-alpha-hydroxylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21642460"}],"value":"1.14.15.30"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19561185"}],"value":"Rieske-type oxygenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19561185"}],"value":"RO"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"kshA"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"kshA4"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21642460"}],"value":"In vitro, catalyzes the introduction of a 9alpha-hydroxyl moiety into the ring B of 3-ketosteroid substrates such as 1,4-androstadiene-3,17-dione (ADD), 4-androstene-3,17-dione (AD), 4-androstene-17beta-ol-3-one (testosterone), 4-pregnene-3,20-dione (progesterone), 19-nor-4-androstene-3,17-dione (nordion), 1-(5alpha)-androstene-3,17-dione, 5alpha-androstane-3,17-dione and 5beta-androstane-3,17-dione (PubMed:19561185, PubMed:21642460). KSH has the highest activity with 3-keto-delta4 steroid substrates (PubMed:19561185)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"androsta-1,4-diene-3,17-dione + 2 reduced [2Fe-2S]-[ferredoxin] + O2 + 2 H(+) = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized [2Fe-2S]-[ferredoxin] + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32199"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:40799"},{"database":"ChEBI","id":"CHEBI:63641"}],"ecNumber":"1.14.15.30","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21642460"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[2Fe-2S] cluster","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:190135"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}],"value":"Binds 1 [2Fe-2S] cluster per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Fe cation","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:24875"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}],"value":"Binds 1 Fe cation."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}],"value":"KSH activity is completely inhibited by zinc ions. KshA is specifically inhibited by Fe(3+), Co(2+), Zn(2+) and Ni(2+) ions"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":10.0,"unit":"uM","substrate":"nordion","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}]},{"constant":23.0,"unit":"uM","substrate":"5alpha-androstane-3,17-dione","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}]},{"constant":33.0,"unit":"uM","substrate":"5beta-androstane-3,17-dione","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}]}]},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}],"value":"Optimum pH is 7."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}],"value":"Optimum temperature is 33 degrees Celsius."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"F1CMY8"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}],"value":"Homotrimer (By similarity). The two-component system 3-ketosteroid-9-alpha-monooxygenase is composed of an oxygenase component KshA and a reductase component KshB (PubMed:19561185)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21642460"}],"value":"By cholic acid"}],"commentType":"INDUCTION"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"3-ketosteroid-9-alpha-monooxygenase, oxygenase component","featureId":"PRO_0000438402"},{"type":"Domain","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"Rieske","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"}]},{"type":"Binding site","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":67,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":89,"modifier":"EXACT"},"end":{"value":89,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"F1CMY8"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"F1CMY8"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"F1CMY8"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"F1CMY8"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}}],"keywords":[{"id":"KW-0001","category":"Ligand","name":"2Fe-2S"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"id":"KW-0442","category":"Biological process","name":"Lipid degradation"},{"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0753","category":"Biological process","name":"Steroid metabolism"}],"references":[{"referenceNumber":1,"citation":{"id":"19561185","citationType":"journal article","authors":["Petrusma M.","Dijkhuizen L.","van der Geize R."],"citationCrossReferences":[{"database":"PubMed","id":"19561185"},{"database":"DOI","id":"10.1128/aem.00066-09"}],"title":"Rhodococcus rhodochrous DSM 43269 3-ketosteroid 9alpha-hydroxylase, a two-component iron-sulfur-containing monooxygenase with subtle steroid substrate specificity.","publicationDate":"2009","journal":"Appl. Environ. Microbiol.","firstPage":"5300","lastPage":"5307","volume":"75"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","COFACTOR","ACTIVITY REGULATION","SUBUNIT","SUBSTRATE SPECIFICITY"],"referenceComments":[{"value":"DSM 43269","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"21642460","citationType":"journal article","authors":["Petrusma M.","Hessels G.","Dijkhuizen L.","van der Geize R."],"citationCrossReferences":[{"database":"PubMed","id":"21642460"},{"database":"DOI","id":"10.1128/jb.00274-11"}],"title":"Multiplicity of 3-ketosteroid-9alpha-hydroxylase enzymes in Rhodococcus rhodochrous DSM43269 for specific degradation of different classes of steroids.","publicationDate":"2011","journal":"J. Bacteriol.","firstPage":"3931","lastPage":"3940","volume":"193"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","CATALYTIC ACTIVITY","INDUCTION","SUBSTRATE SPECIFICITY"],"referenceComments":[{"value":"DSM 43269","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"FJ238095","properties":[{"key":"ProteinId","value":"ACI62780.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"HQ425876","properties":[{"key":"ProteinId","value":"ADY18323.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_145709623.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JASIRK010000034.1"}]},{"database":"AlphaFoldDB","id":"B6V6V5","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"B6V6V5","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:MONOMER-16921","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"1.14.15.30","properties":[{"key":"OrganismId","value":"5395"}]},{"database":"GO","id":"GO:0051537","properties":[{"key":"GoTerm","value":"F:2 iron, 2 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"19561185"}]},{"database":"GO","id":"GO:0036200","properties":[{"key":"GoTerm","value":"F:3-ketosteroid 9-alpha-monooxygenase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"19561185"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"19561185"}]},{"database":"GO","id":"GO:0008203","properties":[{"key":"GoTerm","value":"P:cholesterol metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"2.102.10.10:FF:000012","properties":[{"key":"EntryName","value":"3-ketosteroid-9-alpha-hydroxylase oxygenase subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.380.10:FF:000004","properties":[{"key":"EntryName","value":"3-ketosteroid-9-alpha-hydroxylase oxygenase subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.380.10","properties":[{"key":"EntryName","value":"Naphthalene 1,2-dioxygenase Alpha Subunit, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.102.10.10","properties":[{"key":"EntryName","value":"Rieske [2Fe-2S] iron-sulphur domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050584","properties":[{"key":"EntryName","value":"Cholesterol_7-desaturase"}]},{"database":"InterPro","id":"IPR045605","properties":[{"key":"EntryName","value":"KshA-like_C"}]},{"database":"InterPro","id":"IPR017941","properties":[{"key":"EntryName","value":"Rieske_2Fe-2S"}]},{"database":"InterPro","id":"IPR036922","properties":[{"key":"EntryName","value":"Rieske_2Fe-2S_sf"}]},{"database":"PANTHER","id":"PTHR21266:SF60","properties":[{"key":"EntryName","value":"3-KETOSTEROID-9-ALPHA-MONOOXYGENASE, OXYGENASE COMPONENT"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21266","properties":[{"key":"EntryName","value":"IRON-SULFUR DOMAIN CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF19298","properties":[{"key":"EntryName","value":"KshA_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00355","properties":[{"key":"EntryName","value":"Rieske"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55961","properties":[{"key":"EntryName","value":"Bet v1-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50022","properties":[{"key":"EntryName","value":"ISP domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51296","properties":[{"key":"EntryName","value":"RIESKE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTVPQERIEIRNIDPGTNPTRFARGWHCIGLAKDFRDGKPHQVKVFGTDLVVFADTAGKLHVLDAFCRHMGGNLARGEIKGDTIACPFHDWRWNGQGRCEAVPYARRTPKLGRTKAWTTMERNGVLFVWHCPQGSEPTPELAIPEIEGYEDGQWSDWTWTTIHVEGSHCREIVDNVVDMAHFFYVHFQMPEYFKNVFDGHIAGQHMRSYGRDDIKTGVQMDLPEAQTISDAFYYGPSFMLDTIYTVSEGTTIESKLINCHYPVTNNSFVLQFGTIVKKIEGMSEEQAAEMATMFTDGLEEQFAQDIEIWKHKSRIENPLLTEEDGPVYQLRRWYNQFYVDLEDVTPDMTQRFEFEVDTSRALESWHKEVEENLAGTAE","length":378,"molWeight":43507,"crc64":"5D6201C652F417B4","md5":"ACD08BB8CA96817FC56BC3BF7D59D801"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBUNIT":1,"INDUCTION":1},"countByFeatureType":{"Chain":1,"Domain":1,"Binding site":8},"uniParcId":"UPI0001825B2B"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"B6V6V6","uniProtkbId":"KSHB_RHORH","entryAudit":{"firstPublicDate":"2016-11-30","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2008-12-16","entryVersion":63,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19561185"}],"value":"3-ketosteroid-9-alpha-monooxygenase, ferredoxin reductase component"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19561185"}],"value":"3-ketosteroid-9-alpha-hydroxylase, ferredoxin reductase component"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19561185"}],"value":"KSH"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19561185"}],"value":"Androsta-1,4-diene-3,17-dione 9-alpha-hydroxylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}],"value":"1.14.15.30"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19561185"}],"value":"Rieske-type oxygenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19561185"}],"value":"RO"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19561185"}],"value":"kshB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}],"value":"Probably involved in the degradation of cholesterol. In vitro, catalyzes the introduction of a 9alpha-hydroxyl moiety into the ring B of 3-ketosteroid substrates such as 1,4-androstadiene-3,17-dione (ADD), 4-androstene-3,17-dione (AD), 4-androstene-17beta-ol-3-one (testosterone), 4-pregnene-3,20-dione (progesterone), 19-nor-4-androstene-3,17-dione (nordion), 1-(5alpha)-androstene-3,17-dione, 5alpha-androstane-3,17-dione and 5beta-androstane-3,17-dione. KSH has the highest activity with 3-keto-Delta4 steroid substrates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"androsta-1,4-diene-3,17-dione + 2 reduced [2Fe-2S]-[ferredoxin] + O2 + 2 H(+) = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized [2Fe-2S]-[ferredoxin] + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32199"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:40799"},{"database":"ChEBI","id":"CHEBI:63641"}],"ecNumber":"1.14.15.30","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}],"value":"Binds 1 FAD per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[2Fe-2S] cluster","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00465"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:190135"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00465"}],"value":"Binds 1 2Fe-2S cluster."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}],"value":"KSH activity is completely inhibited by zinc ions. KshB is specifically inhibited by Cu(2+) ions"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":10.0,"unit":"uM","substrate":"19-nor-AD","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}]},{"constant":23.0,"unit":"uM","substrate":"5alpha-androstane-3,17-dione","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}]},{"constant":33.0,"unit":"uM","substrate":"5beta-androstane-3,17-dione","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}]}]},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}],"value":"Optimum pH is 7."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}],"value":"Optimum temperature is 33 degrees Celsius."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19561185"}],"value":"Steroid metabolism; cholesterol degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19561185"}],"value":"The two-component system 3-ketosteroid-9-alpha-monooxygenase is composed of an oxygenase component KshA and a reductase component KshB"}],"commentType":"SUBUNIT"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":351,"modifier":"EXACT"}},"description":"3-ketosteroid-9-alpha-monooxygenase, ferredoxin reductase component","featureId":"PRO_0000438404"},{"type":"Domain","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":116,"modifier":"EXACT"}},"description":"FAD-binding FR-type","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00716"}]},{"type":"Domain","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":351,"modifier":"EXACT"}},"description":"2Fe-2S ferredoxin-type","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00465"}]},{"type":"Binding site","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":300,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00465"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00465"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":308,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00465"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":338,"modifier":"EXACT"},"end":{"value":338,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00465"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}}],"keywords":[{"id":"KW-0001","category":"Ligand","name":"2Fe-2S"},{"id":"KW-0153","category":"Biological process","name":"Cholesterol metabolism"},{"id":"KW-0274","category":"Ligand","name":"FAD"},{"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"id":"KW-0442","category":"Biological process","name":"Lipid degradation"},{"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0753","category":"Biological process","name":"Steroid metabolism"},{"id":"KW-1207","category":"Biological process","name":"Sterol metabolism"}],"references":[{"referenceNumber":1,"citation":{"id":"19561185","citationType":"journal article","authors":["Petrusma M.","Dijkhuizen L.","van der Geize R."],"citationCrossReferences":[{"database":"PubMed","id":"19561185"},{"database":"DOI","id":"10.1128/aem.00066-09"}],"title":"Rhodococcus rhodochrous DSM 43269 3-ketosteroid 9alpha-hydroxylase, a two-component iron-sulfur-containing monooxygenase with subtle steroid substrate specificity.","publicationDate":"2009","journal":"Appl. Environ. Microbiol.","firstPage":"5300","lastPage":"5307","volume":"75"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","COFACTOR","ACTIVITY REGULATION","SUBUNIT","SUBSTRATE SPECIFICITY"],"referenceComments":[{"value":"DSM 43269","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"FJ238096","properties":[{"key":"ProteinId","value":"ACI62781.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_016690904.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JASIRK010000011.1"}]},{"database":"AlphaFoldDB","id":"B6V6V6","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"B6V6V6","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1829.GCA_000716895_05284","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:MONOMER-16922","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA01058","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0051537","properties":[{"key":"GoTerm","value":"F:2 iron, 2 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0036200","properties":[{"key":"GoTerm","value":"F:3-ketosteroid 9-alpha-monooxygenase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"19561185"}]},{"database":"GO","id":"GO:0071949","properties":[{"key":"GoTerm","value":"F:FAD binding"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"19561185"}]},{"database":"GO","id":"GO:0006707","properties":[{"key":"GoTerm","value":"P:cholesterol catabolic process"},{"key":"GoEvidenceType","value":"NAS:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19561185"}]},{"database":"CDD","id":"cd00207","properties":[{"key":"EntryName","value":"fer2"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd06214","properties":[{"key":"EntryName","value":"PA_degradation_oxidoreductase_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.20.30:FF:000023","properties":[{"key":"EntryName","value":"3-ketosteroid-9-alpha-hydroxylase reductase subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.20.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.80","properties":[{"key":"EntryName","value":"Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.30.10","properties":[{"key":"EntryName","value":"Translation factors"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036010","properties":[{"key":"EntryName","value":"2Fe-2S_ferredoxin-like_sf"}]},{"database":"InterPro","id":"IPR001041","properties":[{"key":"EntryName","value":"2Fe-2S_ferredoxin-type"}]},{"database":"InterPro","id":"IPR006058","properties":[{"key":"EntryName","value":"2Fe2S_fd_BS"}]},{"database":"InterPro","id":"IPR012675","properties":[{"key":"EntryName","value":"Beta-grasp_dom_sf"}]},{"database":"InterPro","id":"IPR008333","properties":[{"key":"EntryName","value":"Cbr1-like_FAD-bd_dom"}]},{"database":"InterPro","id":"IPR017927","properties":[{"key":"EntryName","value":"FAD-bd_FR_type"}]},{"database":"InterPro","id":"IPR001709","properties":[{"key":"EntryName","value":"Flavoprot_Pyr_Nucl_cyt_Rdtase"}]},{"database":"InterPro","id":"IPR039261","properties":[{"key":"EntryName","value":"FNR_nucleotide-bd"}]},{"database":"InterPro","id":"IPR050415","properties":[{"key":"EntryName","value":"MRET"}]},{"database":"InterPro","id":"IPR001433","properties":[{"key":"EntryName","value":"OxRdtase_FAD/NAD-bd"}]},{"database":"InterPro","id":"IPR017938","properties":[{"key":"EntryName","value":"Riboflavin_synthase-like_b-brl"}]},{"database":"PANTHER","id":"PTHR47354:SF8","properties":[{"key":"EntryName","value":"1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR47354","properties":[{"key":"EntryName","value":"NADH OXIDOREDUCTASE HCR"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00970","properties":[{"key":"EntryName","value":"FAD_binding_6"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00111","properties":[{"key":"EntryName","value":"Fer2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00175","properties":[{"key":"EntryName","value":"NAD_binding_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00371","properties":[{"key":"EntryName","value":"FPNCR"}]},{"database":"PRINTS","id":"PR00410","properties":[{"key":"EntryName","value":"PHEHYDRXLASE"}]},{"database":"SUPFAM","id":"SSF54292","properties":[{"key":"EntryName","value":"2Fe-2S ferredoxin-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52343","properties":[{"key":"EntryName","value":"Ferredoxin reductase-like, C-terminal NADP-linked domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF63380","properties":[{"key":"EntryName","value":"Riboflavin synthase domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00197","properties":[{"key":"EntryName","value":"2FE2S_FER_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51085","properties":[{"key":"EntryName","value":"2FE2S_FER_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51384","properties":[{"key":"EntryName","value":"FAD_FR"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTTVEVPHGSRSVILTVSAVVEETADTRSIVFAVPDELRDKFAYRPGQFLTLRIPSDRTGSVARCYSLASSPFTDDAPKVTVKRTSDGYGSNWLCDNIATGQTLEVLPPAGVFTPKSLDHDFLLFGAGSGITPVISILKSALTQGGGKVVLVYANRDEKSVIFAEELRALAEKYPTRLTVVHWLESVQGLPTADQLAAIAAPYESYEAFMCGPGPFMDTVHQALNTVGMPRARVHAEVFNSLSGDPFADQAPVEVSDEDAADAATVEVELDGEVHKLSWPRKQTLVDIMLAKGIDVPYSCQEGECGSCACTVLEGKVEMENCDVLDPEDIEAGYILGCQARPVTDHLKIEF","length":351,"molWeight":37887,"crc64":"F146084969AD4B2E","md5":"6CF0957AC001943A423E4413D2AF2AF6"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SUBUNIT":1},"countByFeatureType":{"Chain":1,"Domain":2,"Binding site":4},"uniParcId":"UPI0001825B2C"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"F1CMX0","uniProtkbId":"KSHA1_RHORH","entryAudit":{"firstPublicDate":"2016-11-30","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2011-05-03","entryVersion":54,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"3-ketosteroid-9-alpha-monooxygenase, oxygenase component"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"3-ketosteroid-9-alpha-hydroxylase, oxygenase component"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"KSH"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"25049233"}],"value":"Androsta-1,4-diene-3,17-dione 9-alpha-hydroxylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21642460"}],"value":"1.14.15.30"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"25049233"}],"value":"Rieske-type oxygenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"25049233"}],"value":"RO"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"kshA"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"kshA1"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21642460"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"value":"May be involved in the degradation of cholic acid, a steroid acid found predominantly in the bile (PubMed:21642460). In vitro, catalyzes the introduction of a 9alpha-hydroxyl moiety into the ring B of 3-ketosteroid substrates such as 1,4-androstadiene-3,17-dione (ADD), 4-androstene-3,17-dione (AD), 4-androstene-17beta-ol-3-one (testosterone), 4-pregnene-3,20-dione (progesterone), 3-oxo-23,24-bisnorcholesta-4-en-22-oate (4-BNC), 23,24-bisnorcholesta-4-ene-22-oate, 3-oxo-23,24-bisnorcholaesta-1,4-dien-22-oate (1,4-BNC), 23,24-bisnorcholesta-1,4-diene-22-oate and 3-oxo-23,24-bisnorcholesta-1,4-dien-22-oyl-coenzyme A thioester (1,4-BNC-CoA) (PubMed:21642460, PubMed:25049233). KshA1 has the highest specificity for steroids possessing an isopropionyl side chain at C17 (PubMed:25049233)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"androsta-1,4-diene-3,17-dione + 2 reduced [2Fe-2S]-[ferredoxin] + O2 + 2 H(+) = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized [2Fe-2S]-[ferredoxin] + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32199"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:40799"},{"database":"ChEBI","id":"CHEBI:63641"}],"ecNumber":"1.14.15.30","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21642460"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[2Fe-2S] cluster","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:190135"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"value":"Binds 1 [2Fe-2S] cluster per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Fe cation","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:24875"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"value":"Binds 1 Fe cation."}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":1.0,"unit":"uM","substrate":"1,4-BNC as substrate (at pH 7.0 and 22 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}]},{"constant":2.0,"unit":"uM","substrate":"1,4-BNC-CoA as substrate (at pH 7.0 and 22 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}]},{"constant":2.2,"unit":"uM","substrate":"4-BNC as substrate (at pH 7.0 and 22 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}]},{"constant":50.0,"unit":"uM","substrate":"ADD as substrate (at pH 7.0 and 22 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}]},{"constant":110.0,"unit":"uM","substrate":"testosterone as substrate (at pH 7.0 and 22 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}]},{"constant":400.0,"unit":"uM","substrate":"AD as substrate (at pH 7.0 and 22 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"value":"kcat is 2.6 sec(-1) for 4-BNC as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 1.4 sec(-1) for testosterone as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 1.3 sec(-1) for ADD as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 1.1 sec(-1) for 1,4-BNC-CoA as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 0.9 sec(-1) for 1,4-BNC as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 0.5 sec(-1) for AD as substrate (at pH 7.0 and 22 degrees Celsius)."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"value":"Homotrimer. The two-component system 3-ketosteroid-9-alpha-monooxygenase is composed of an oxygenase component KshA and a reductase component KshB"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21642460"}],"value":"By cholic acid"}],"commentType":"INDUCTION"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":394,"modifier":"EXACT"}},"description":"3-ketosteroid-9-alpha-monooxygenase, oxygenase component","featureId":"PRO_0000438399"},{"type":"Domain","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"Rieske","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"}]},{"type":"Binding site","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":68,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":70,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"F1CMY8"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"F1CMY8"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":245,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Beta strand","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Helix","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Beta strand","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Beta strand","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Beta strand","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":55,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Beta strand","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":67,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Turn","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Helix","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Beta strand","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Beta strand","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Turn","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Beta strand","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Beta strand","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Beta strand","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Helix","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Helix","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Beta strand","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Helix","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Helix","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Helix","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Beta strand","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Beta strand","location":{"start":{"value":201,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Beta strand","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Beta strand","location":{"start":{"value":251,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Beta strand","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Turn","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Helix","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":310,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Helix","location":{"start":{"value":327,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Helix","location":{"start":{"value":335,"modifier":"EXACT"},"end":{"value":338,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Helix","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Helix","location":{"start":{"value":346,"modifier":"EXACT"},"end":{"value":349,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Beta strand","location":{"start":{"value":352,"modifier":"EXACT"},"end":{"value":356,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Helix","location":{"start":{"value":359,"modifier":"EXACT"},"end":{"value":375,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Helix","location":{"start":{"value":376,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Turn","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":383,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]}],"keywords":[{"id":"KW-0001","category":"Ligand","name":"2Fe-2S"},{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"id":"KW-0442","category":"Biological process","name":"Lipid degradation"},{"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0753","category":"Biological process","name":"Steroid metabolism"}],"references":[{"referenceNumber":1,"citation":{"id":"21642460","citationType":"journal article","authors":["Petrusma M.","Hessels G.","Dijkhuizen L.","van der Geize R."],"citationCrossReferences":[{"database":"PubMed","id":"21642460"},{"database":"DOI","id":"10.1128/jb.00274-11"}],"title":"Multiplicity of 3-ketosteroid-9alpha-hydroxylase enzymes in Rhodococcus rhodochrous DSM43269 for specific degradation of different classes of steroids.","publicationDate":"2011","journal":"J. Bacteriol.","firstPage":"3931","lastPage":"3940","volume":"193"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","CATALYTIC ACTIVITY","INDUCTION","SUBSTRATE SPECIFICITY"],"referenceComments":[{"value":"DSM 43269","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"25049233","citationType":"journal article","authors":["Penfield J.S.","Worrall L.J.","Strynadka N.C.","Eltis L.D."],"citationCrossReferences":[{"database":"PubMed","id":"25049233"},{"database":"DOI","id":"10.1074/jbc.m114.575886"}],"title":"Substrate specificities and conformational flexibility of 3-ketosteroid 9alpha-hydroxylases.","publicationDate":"2014","journal":"J. Biol. Chem.","firstPage":"25523","lastPage":"25536","volume":"289"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH SUBSTRATE ANALOG; IRON ION AND IRON-SULFUR (2FE-2S)","FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","COFACTOR","SUBUNIT","SUBSTRATE SPECIFICITY"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"HQ425873","properties":[{"key":"ProteinId","value":"ADY18310.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_059382524.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JABFDW010000006.1"}]},{"database":"PDB","id":"4QDF","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.43 A"},{"key":"Chains","value":"B=1-394"}]},{"database":"AlphaFoldDB","id":"F1CMX0","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"F1CMX0","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1829.GCA_000716895_02108","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"1.14.15.30","properties":[{"key":"OrganismId","value":"5395"}]},{"database":"EvolutionaryTrace","id":"F1CMX0","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0051537","properties":[{"key":"GoTerm","value":"F:2 iron, 2 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"25049233"}]},{"database":"GO","id":"GO:0036200","properties":[{"key":"GoTerm","value":"F:3-ketosteroid 9-alpha-monooxygenase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"25049233"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"25049233"}]},{"database":"GO","id":"GO:0008203","properties":[{"key":"GoTerm","value":"P:cholesterol metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd03531","properties":[{"key":"EntryName","value":"Rieske_RO_Alpha_KSH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.102.10.10:FF:000012","properties":[{"key":"EntryName","value":"3-ketosteroid-9-alpha-hydroxylase oxygenase subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.380.10:FF:000004","properties":[{"key":"EntryName","value":"3-ketosteroid-9-alpha-hydroxylase oxygenase subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.380.10","properties":[{"key":"EntryName","value":"Naphthalene 1,2-dioxygenase Alpha Subunit, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.102.10.10","properties":[{"key":"EntryName","value":"Rieske [2Fe-2S] iron-sulphur domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050584","properties":[{"key":"EntryName","value":"Cholesterol_7-desaturase"}]},{"database":"InterPro","id":"IPR045605","properties":[{"key":"EntryName","value":"KshA-like_C"}]},{"database":"InterPro","id":"IPR017941","properties":[{"key":"EntryName","value":"Rieske_2Fe-2S"}]},{"database":"InterPro","id":"IPR036922","properties":[{"key":"EntryName","value":"Rieske_2Fe-2S_sf"}]},{"database":"PANTHER","id":"PTHR21266:SF60","properties":[{"key":"EntryName","value":"3-KETOSTEROID-9-ALPHA-MONOOXYGENASE, OXYGENASE COMPONENT"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21266","properties":[{"key":"EntryName","value":"IRON-SULFUR DOMAIN CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF19298","properties":[{"key":"EntryName","value":"KshA_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00355","properties":[{"key":"EntryName","value":"Rieske"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55961","properties":[{"key":"EntryName","value":"Bet v1-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50022","properties":[{"key":"EntryName","value":"ISP domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51296","properties":[{"key":"EntryName","value":"RIESKE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSLGTSEQSEIREIVAGSAPARFARGWHCLGLAKDFKDGKPHSVHAFGTKLVVWADSNDEIRILDAYCRHMGGDLSQGTVKGDEIACPFHDWRWGGNGRCKNIPYARRVPPIAKTRAWHTLDQDGLLFVWHDPQGNPPPADVTIPRIAGATSDEWTDWVWYTTEVDTNCREIIDNIVDMAHFFYVHYSFPVYFKNVFEGHVASQFMRGQAREDTRPHANGQPKMIGSRSDASYFGPSFMIDDLVYEYEGYDVESVLINCHYPVSQDKFVLMYGMIVKKSDRLEGEKALQTAQQFGNFIAKGFEQDIEIWRNKTRIDNPLLCEEDGPVYQLRRWYEQFYVDVEDVAPEMTDRFEFEMDTTRPVAAWMKEVEANIARKAALDTETRSAPEQSTTAG","length":394,"molWeight":45020,"crc64":"2E7CBC44AB112CFE","md5":"D148850FD69067D6D9CA6E4812B2679D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBUNIT":1,"INDUCTION":1},"countByFeatureType":{"Chain":1,"Domain":1,"Binding site":9,"Beta strand":17,"Helix":14,"Turn":4},"uniParcId":"UPI0002020DBE"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P21219","uniProtkbId":"NHA1_RHORH","entryAudit":{"firstPublicDate":"1991-05-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-01-23","entryVersion":107,"sequenceVersion":3},"annotationScore":5.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1840499"}],"value":"High-molecular weight cobalt-containing nitrile hydratase subunit alpha"},"shortNames":[{"value":"H-NHase"},{"value":"H-nitrilase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12121763"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1840499"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28644864"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35919716"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8633053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9650255"}],"value":"4.2.1.84"}]}},"genes":[{"geneName":{"value":"nhhA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12121763"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1840499"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28644864"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35919716"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8633053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9650255"}],"value":"NHase catalyzes the hydration of various nitrile compounds to the corresponding amides (PubMed:12121763, PubMed:1840499, PubMed:2013281, PubMed:28644864, PubMed:35919716, PubMed:8633053, PubMed:9650255). The alpha subunit functions as the catalytic subunit of the NHase complex while the beta subunit plays a structural/accessory role (PubMed:12121763, PubMed:28644864, PubMed:35919716, PubMed:9650255)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an aliphatic primary amide = an aliphatic nitrile + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12673"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:65285"},{"database":"ChEBI","id":"CHEBI:80291"}],"ecNumber":"4.2.1.84","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12121763"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1840499"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28644864"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35919716"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8633053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9650255"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:12675"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12121763"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1840499"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28644864"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35919716"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8633053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9650255"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Co(3+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12121763"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1840499"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28644864"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8633053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9650255"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49415"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12121763"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28644864"}],"value":"Binds 1 Co(3+) ion per heterodimer."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9650255"}],"value":"Activated by methacrylamide and crotonamide (PubMed:9650255). Inhibited by mercuric chloride and silver nitrate; competitively inhibited by potassium cyanide (PubMed:2013281)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","absorption":{"max":410,"approximate":false,"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12121763"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}],"value":"Measured for the whole complex."}]},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12121763"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},"kineticParameters":{"maximumVelocities":[{"velocity":370.0,"unit":"umol/min/mg","enzyme":"enzyme with 3-cyanopyridine as substrate (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"velocity":160.0,"unit":"umol/min/mg","enzyme":"enzyme with 2-cyanopyridine as substrate (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"velocity":256.0,"unit":"umol/min/mg","enzyme":"enzyme with 4-cyanopyridine as substrate (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"velocity":250.0,"unit":"umol/min/mg","enzyme":"enzyme with benzonitrile as substrate (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"velocity":9.6,"unit":"umol/min/mg","enzyme":"enzyme with cyanopyrazine as substrate (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"velocity":2240.0,"unit":"umol/min/mg","enzyme":"enzyme with acetonitrile as substrate (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"velocity":1600.0,"unit":"umol/min/mg","enzyme":"enzyme with propionitrile as substrate (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"velocity":1300.0,"unit":"umol/min/mg","enzyme":"enzyme with n-butylnitrile as substrate (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"velocity":4.8,"unit":"umol/min/mg","enzyme":"enzyme with isobutylnitrile as substrate (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"velocity":1760.0,"unit":"umol/min/mg","enzyme":"enzyme with acrylonitrile as substrate (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"velocity":320.0,"unit":"umol/min/mg","enzyme":"enzyme with methacrylonitrile as substrate (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"velocity":288.0,"unit":"umol/min/mg","enzyme":"enzyme with crotonitrile as substrate (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"velocity":2190.0,"unit":"umol/min/mg","enzyme":"enzyme with chloroacetonitrile as substrate (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]}],"michaelisConstants":[{"constant":200.0,"unit":"mM","substrate":"3-cyanopyridine (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"constant":21.7,"unit":"mM","substrate":"2-cyanopyridine (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"constant":18.5,"unit":"mM","substrate":"4-cyanopyridine (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"constant":28.6,"unit":"mM","substrate":"benzonitrile (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"constant":10.0,"unit":"mM","substrate":"cyanopyrazine (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"constant":1.92,"unit":"mM","substrate":"propionitrile (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"constant":21.7,"unit":"mM","substrate":"n-butylnitrile (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"constant":1.85,"unit":"mM","substrate":"isobutylnitrile (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"constant":1.89,"unit":"mM","substrate":"acrylonitrile (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"constant":6.76,"unit":"mM","substrate":"methacrylonitrile (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"constant":4.88,"unit":"mM","substrate":"crotonitrile (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"constant":12.2,"unit":"mM","substrate":"chloroacetonitrile (at pH 7.0 and 20 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]}]},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}],"value":"Optimum pH is 6.5 - 6.8 with 3-cyanopyridine as substrate (PubMed:2013281). Stable from pH 6.0 to 8.5 (PubMed:2013281)."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}],"value":"Optimum temperature is 35 degrees Celsius with 3-cyanopyridine as substrate (PubMed:2013281). Thermostable up to 50 degrees Celsius (PubMed:2013281)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12121763"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1840499"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28644864"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35919716"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8633053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9650255"}],"value":"Heteromultimer; the size of the heteromultimeric complex formed is essential for activity (PubMed:12121763, PubMed:1840499, PubMed:2013281, PubMed:28644864, PubMed:8633053, PubMed:9650255). Component of the NHase complex, composed of at least ten heterodimers of nhhA and nhhB (PubMed:12121763, PubMed:1840499, PubMed:2013281, PubMed:28644864, PubMed:35919716, PubMed:8633053, PubMed:9650255)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1840499"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8633053"}],"value":"By cobalt, urea and crotonamide"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P13448"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q7SID2"}],"value":"Oxidized (By similarity). Oxidation on Cys-105 is essential for enzymatic activity (By similarity). The cysteine-sulfenic acid formed from the oxidation of Cys-107 may be required to act as a nucleophile and initiate catalysis (By similarity)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Industrial production of acrylamide and nicotinamide is now being developed using some of these enzymes"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28644864"}],"value":"The complex exhibits higher product tolerance than the low-molecular weight NHase complex, L-NHase"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the nitrile hydratase subunit alpha family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1840499"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"High-molecular weight cobalt-containing nitrile hydratase subunit alpha","featureId":"PRO_0000186824"},{"type":"Active site","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q7SID2"}]},{"type":"Binding site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49415"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q7SID2"}],"ligand":{"name":"Co(3+)","id":"ChEBI:CHEBI:49415"}},{"type":"Binding site","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49415"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q7SID2"}],"ligand":{"name":"Co(3+)","id":"ChEBI:CHEBI:49415"}},{"type":"Binding site","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49415"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q7SID2"}],"ligand":{"name":"Co(3+)","id":"ChEBI:CHEBI:49415"}},{"type":"Binding site","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49415"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q7SID2"}],"ligand":{"name":"Co(3+)","id":"ChEBI:CHEBI:49415"}},{"type":"Modified residue","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"Cysteine sulfinic acid (-SO2H)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q7SID2"}]},{"type":"Modified residue","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"Cysteine sulfenic acid (-SOH)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q7SID2"}]},{"type":"Disulfide bond","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q7SID2"}]},{"type":"Mutagenesis","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"Abolishes the binding of cobalt ion and consequently the activity of the complex; when associated with A-105.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12121763"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"Abolishes the binding of cobalt ion and consequently the activity of the complex; alone and when associated with either A-102 or A-107.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12121763"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"Abolishes the binding of cobalt ion and consequently the activity of the complex; alone and when associated with A-105.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12121763"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["A"]}}],"keywords":[{"id":"KW-0170","category":"Ligand","name":"Cobalt"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0558","category":"PTM","name":"Oxidation"}],"references":[{"referenceNumber":1,"citation":{"id":"1840499","citationType":"journal article","authors":["Kobayashi M.","Nishiyama M.","Nagasawa T.","Horinouchi S.","Beppu T.","Yamada H."],"citationCrossReferences":[{"database":"PubMed","id":"1840499"},{"database":"DOI","id":"10.1016/0167-4781(91)90208-4"}],"title":"Cloning, nucleotide sequence and expression in Escherichia coli of two cobalt-containing nitrile hydratase genes from Rhodococcus rhodochrous J1.","publicationDate":"1991","journal":"Biochim. Biophys. Acta","firstPage":"23","lastPage":"33","volume":"1129"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 2-27 AND 162-173","FUNCTION","CATALYTIC ACTIVITY","COFACTOR","SUBUNIT","INDUCTION BY COBALT; UREA AND CROTONAMIDE"],"referenceComments":[{"value":"J1","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"8633053","citationType":"journal article","authors":["Komeda H.","Kobayashi M.","Shimizu S."],"citationCrossReferences":[{"database":"PubMed","id":"8633053"},{"database":"DOI","id":"10.1073/pnas.93.9.4267"}],"title":"Characterization of the gene cluster of high-molecular-mass nitrile hydratase (H-NHase) induced by its reaction product in Rhodococcus rhodochrous J1.","publicationDate":"1996","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"4267","lastPage":"4272","volume":"93"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","CATALYTIC ACTIVITY","COFACTOR","SUBUNIT","INDUCTION BY UREA"],"referenceComments":[{"value":"J1","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"2013281","citationType":"journal article","authors":["Nagasawa T.","Takeuchi K.","Yamada H."],"citationCrossReferences":[{"database":"PubMed","id":"2013281"},{"database":"DOI","id":"10.1111/j.1432-1033.1991.tb15853.x"}],"title":"Characterization of a new cobalt-containing nitrile hydratase purified from urea-induced cells of Rhodococcus rhodochrous J1.","publicationDate":"1991","journal":"Eur. J. Biochem.","firstPage":"581","lastPage":"589","volume":"196"},"referencePositions":["PROTEIN SEQUENCE OF 2-29","FUNCTION","CATALYTIC ACTIVITY","COFACTOR","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT","INDUCTION BY UREA"],"referenceComments":[{"value":"J1","type":"STRAIN"}]},{"referenceNumber":4,"citation":{"id":"9650255","citationType":"journal article","authors":["Mizunashi W.","Nishiyama M.","Horinouchi S.","Beppu T."],"citationCrossReferences":[{"database":"PubMed","id":"9650255"},{"database":"DOI","id":"10.1007/s002530051214"}],"title":"Overexpression of high-molecular-mass nitrile hydratase from Rhodococcus rhodochrous J1 in recombinant Rhodococcus cells.","publicationDate":"1998","journal":"Appl. Microbiol. Biotechnol.","firstPage":"568","lastPage":"572","volume":"49"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","COFACTOR","ACTIVITY REGULATION","SUBUNIT"]},{"referenceNumber":5,"citation":{"id":"12121763","citationType":"journal article","authors":["Hashimoto Y.","Sasaki S.","Herai S.","Oinuma K.","Shimizu S.","Kobayashi M."],"citationCrossReferences":[{"database":"PubMed","id":"12121763"},{"database":"DOI","id":"10.1016/s0162-0134(02)00373-2"}],"title":"Site-directed mutagenesis for cysteine residues of cobalt-containing nitrile hydratase.","publicationDate":"2002","journal":"J. Inorg. Biochem.","firstPage":"70","lastPage":"77","volume":"91"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","COFACTOR","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT","MUTAGENESIS OF CYS-102; CYS-105 AND CYS-107"]},{"referenceNumber":6,"citation":{"id":"28644864","citationType":"journal article","authors":["Lan Y.","Zhang X.","Liu Z.","Zhou L.","Shen R.","Zhong X.","Cui W.","Zhou Z."],"citationCrossReferences":[{"database":"PubMed","id":"28644864"},{"database":"DOI","id":"10.1371/journal.pone.0179833"}],"title":"Overexpression and characterization of two types of nitrile hydratases from Rhodococcus rhodochrous J1.","publicationDate":"2017","journal":"PLoS ONE","firstPage":"e0179833","lastPage":"e0179833","volume":"12"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","COFACTOR","SUBUNIT"]},{"referenceNumber":7,"citation":{"id":"35919716","citationType":"journal article","authors":["Ma D.","Cheng Z.","Peplowski L.","Han L.","Xia Y.","Hou X.","Guo J.","Yin D.","Rao Y.","Zhou Z."],"citationCrossReferences":[{"database":"PubMed","id":"35919716"},{"database":"DOI","id":"10.1039/d2sc02319a"}],"title":"Insight into the broadened substrate scope of nitrile hydratase by static and dynamic structure analysis.","publicationDate":"2022","journal":"Chem. Sci.","firstPage":"8417","lastPage":"8428","volume":"13"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","SUBUNIT"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X64359","properties":[{"key":"ProteinId","value":"CAA45710.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"D67027","properties":[{"key":"ProteinId","value":"BAA11044.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"S19714","properties":[{"key":"EntryName","value":"S19714"}]},{"database":"AlphaFoldDB","id":"P21219","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P21219","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:MONOMER-2283","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"4.2.1.84","properties":[{"key":"OrganismId","value":"22537"}]},{"database":"GO","id":"GO:0018822","properties":[{"key":"GoTerm","value":"F:nitrile hydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046914","properties":[{"key":"GoTerm","value":"F:transition metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.90.330.10","properties":[{"key":"EntryName","value":"Nitrile hydratase alpha /Thiocyanate hydrolase gamma"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036648","properties":[{"key":"EntryName","value":"CN_Hdrase_a/SCN_Hdrase_g_sf"}]},{"database":"InterPro","id":"IPR004232","properties":[{"key":"EntryName","value":"CN_Hdrtase_a/SCN_Hdrlase_g"}]},{"database":"InterPro","id":"IPR023900","properties":[{"key":"EntryName","value":"CN_Hdrtase_asu/SCN_Hdrlase_gsu"}]},{"database":"InterPro","id":"IPR018141","properties":[{"key":"EntryName","value":"Nitrile_hydratase_asu"}]},{"database":"NCBIfam","id":"TIGR01323","properties":[{"key":"EntryName","value":"nitrile_alph"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02979","properties":[{"key":"EntryName","value":"NHase_alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001426","properties":[{"key":"EntryName","value":"NHase_alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56209","properties":[{"key":"EntryName","value":"Nitrile hydratase alpha chain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSEHVNKYTEYEARTKAIETLLYERGLITPAAVDRVVSYYENEIGPMGGAKVVAKSWVDPEYRKWLEEDATAAMASLGYAGEQAHQISAVFNDSQTHHVVVCTLCSCYPWPVLGLPPAWYKSMEYRSRVVADPRGVLKRDFGFDIPDEVEVRVWDSSSEIRYIVIPERPAGTDGWSEEELTKLVSRDSMIGVSNALTPQEVIV","length":203,"molWeight":22835,"crc64":"515ED2A4863E6C98","md5":"C4879CF83E47D5531AF1D24902514EB8"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBUNIT":1,"INDUCTION":1,"PTM":1,"BIOTECHNOLOGY":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Active site":1,"Binding site":4,"Modified residue":2,"Disulfide bond":1,"Mutagenesis":3},"uniParcId":"UPI000000D661"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"F1CMY8","uniProtkbId":"KSHA5_RHORH","entryAudit":{"firstPublicDate":"2016-11-30","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2011-05-03","entryVersion":50,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"3-ketosteroid-9-alpha-monooxygenase, oxygenase component"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"3-ketosteroid-9-alpha-hydroxylase, oxygenase component"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"KSH"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"25049233"}],"value":"Androsta-1,4-diene-3,17-dione 9-alpha-hydroxylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21642460"}],"value":"1.14.15.30"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"25049233"}],"value":"Rieske-type oxygenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"25049233"}],"value":"RO"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"kshA"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"kshA5"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21642460"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"value":"Probably involved in the degradation of cholesterol (PubMed:21642460). In vitro, catalyzes the introduction of a 9alpha-hydroxyl moiety into the ring B of 3-ketosteroid substrates such as 1,4-androstadiene-3,17-dione (ADD), 4-androstene-3,17-dione (AD), 4-androstene-17beta-ol-3-one (testosterone), 4-pregnene-3,20-dione (progesterone), 19-nor-4-androstene-3,17-dione, 1-(5alpha)-androstene-3,17-dione, 5alpha-androstane-3,17-dione, 5beta-androstane-3,17-dione, 5alpha-androstane-17beta-ol-3-one (stanolon), 11beta-hydrocortisone, 3-oxo-23,24-bisnorcholesta-4-en-22-oate (4-BNC), 23,24-bisnorcholesta-4-ene-22-oate, 3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate (1,4-BNC) and 3-oxo-23,24-bisnorcholesta-1,4-dien-22-oyl-coenzyme A thioester (1,4-BNC-CoA) (PubMed:21642460, PubMed:25049233). KshA5 has the broadest substrate range without a clear substrate preference and is active with Delta-4, Delta-1,4, 5alpha-H and 5beta-H steroids, as well as with steroids having bulky aliphatic side chains and an isopropionyl side chain at C17"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"androsta-1,4-diene-3,17-dione + 2 reduced [2Fe-2S]-[ferredoxin] + O2 + 2 H(+) = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized [2Fe-2S]-[ferredoxin] + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32199"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:40799"},{"database":"ChEBI","id":"CHEBI:63641"}],"ecNumber":"1.14.15.30","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21642460"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[2Fe-2S] cluster","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:190135"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"value":"Binds 1 [2Fe-2S] cluster per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Fe cation","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:24875"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"value":"Binds 1 Fe cation."}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":0.5,"unit":"uM","substrate":"1,4-BNC as substrate (at pH 7.0 and 22 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}]},{"constant":0.5,"unit":"uM","substrate":"testosterone as substrate (at pH 7.0 and 22 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}]},{"constant":0.8,"unit":"uM","substrate":"AD as substrate (at pH 7.0 and 22 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}]},{"constant":1.2,"unit":"uM","substrate":"4-BNC as substrate (at pH 7.0 and 22 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}]},{"constant":6.1,"unit":"uM","substrate":"5alpha-androstan-3,17-dione as substrate (at pH 7.0 and 22 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}]},{"constant":500.0,"unit":"uM","substrate":"1,4-BNC-CoA as substrate (at pH 7.0 and 22 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"value":"kcat is 1.7 sec(-1) for 1,4-BNC-CoA as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 0.8 sec(-1) for 5alpha-androstan-3,17-dione, AD and testosterone as substrates (at pH 7.0 and 22 degrees Celsius). kcat is 0.7 sec(-1) for ADD as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 0.6 sec(-1) for 4-BNC as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 0.5 sec(-1) for 1,4-BNC as substrate (at pH 7.0 and 22 degrees Celsius)."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"25049233"}],"value":"Steroid metabolism; cholesterol degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"value":"Homotrimer. The two-component system 3-ketosteroid-9-alpha-monooxygenase is composed of an oxygenase component KshA and a reductase component KshB"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21642460"}],"value":"By cholesterol, progesterone, AD and cholic acid"}],"commentType":"INDUCTION"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"3-ketosteroid-9-alpha-monooxygenase, oxygenase component","featureId":"PRO_0000438403"},{"type":"Domain","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"Rieske","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"}]},{"type":"Binding site","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":75,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":311,"modifier":"EXACT"},"end":{"value":311,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25049233"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Helix","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDD"}]},{"type":"Helix","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Helix","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Beta strand","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Helix","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Beta strand","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Beta strand","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":51,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Beta strand","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Beta strand","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDD"}]},{"type":"Beta strand","location":{"start":{"value":66,"modifier":"EXACT"},"end":{"value":72,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Turn","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Helix","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Beta strand","location":{"start":{"value":83,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Beta strand","location":{"start":{"value":89,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Turn","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Beta strand","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Beta strand","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Beta strand","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":113,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Beta strand","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Beta strand","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":136,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Helix","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Turn","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Beta strand","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Helix","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Helix","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Helix","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Beta strand","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Beta strand","location":{"start":{"value":207,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Helix","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Beta strand","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":253,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Beta strand","location":{"start":{"value":256,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Beta strand","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":283,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Beta strand","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDF"}]},{"type":"Helix","location":{"start":{"value":290,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Helix","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Helix","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":344,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Helix","location":{"start":{"value":347,"modifier":"EXACT"},"end":{"value":349,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Helix","location":{"start":{"value":352,"modifier":"EXACT"},"end":{"value":355,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Beta strand","location":{"start":{"value":358,"modifier":"EXACT"},"end":{"value":362,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Helix","location":{"start":{"value":365,"modifier":"EXACT"},"end":{"value":377,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]},{"type":"Helix","location":{"start":{"value":380,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4QDC"}]}],"keywords":[{"id":"KW-0001","category":"Ligand","name":"2Fe-2S"},{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0153","category":"Biological process","name":"Cholesterol metabolism"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"id":"KW-0442","category":"Biological process","name":"Lipid degradation"},{"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0753","category":"Biological process","name":"Steroid metabolism"},{"id":"KW-1207","category":"Biological process","name":"Sterol metabolism"}],"references":[{"referenceNumber":1,"citation":{"id":"21642460","citationType":"journal article","authors":["Petrusma M.","Hessels G.","Dijkhuizen L.","van der Geize R."],"citationCrossReferences":[{"database":"PubMed","id":"21642460"},{"database":"DOI","id":"10.1128/jb.00274-11"}],"title":"Multiplicity of 3-ketosteroid-9alpha-hydroxylase enzymes in Rhodococcus rhodochrous DSM43269 for specific degradation of different classes of steroids.","publicationDate":"2011","journal":"J. Bacteriol.","firstPage":"3931","lastPage":"3940","volume":"193"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","CATALYTIC ACTIVITY","INDUCTION","SUBSTRATE SPECIFICITY"],"referenceComments":[{"value":"DSM 43269","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"25049233","citationType":"journal article","authors":["Penfield J.S.","Worrall L.J.","Strynadka N.C.","Eltis L.D."],"citationCrossReferences":[{"database":"PubMed","id":"25049233"},{"database":"DOI","id":"10.1074/jbc.m114.575886"}],"title":"Substrate specificities and conformational flexibility of 3-ketosteroid 9alpha-hydroxylases.","publicationDate":"2014","journal":"J. Biol. Chem.","firstPage":"25523","lastPage":"25536","volume":"289"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH IRON ION AND IRON-SULFUR (2FE-2S)","FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","COFACTOR","PATHWAY","SUBUNIT","SUBSTRATE SPECIFICITY"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"HQ425877","properties":[{"key":"ProteinId","value":"ADY18328.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_145709578.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JASIRK010000006.1"}]},{"database":"PDB","id":"4QDC","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.90 A"},{"key":"Chains","value":"A=1-390"}]},{"database":"PDB","id":"4QDD","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.60 A"},{"key":"Chains","value":"A=1-390"}]},{"database":"PDB","id":"4QDF","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.43 A"},{"key":"Chains","value":"A=1-390"}]},{"database":"AlphaFoldDB","id":"F1CMY8","properties":[{"key":"Description","value":"-"}]},{"database":"MDposit","id":"F1CMY8","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"F1CMY8","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1829.GCA_000716895_04572","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"1.14.15.30","properties":[{"key":"OrganismId","value":"5395"}]},{"database":"UniPathway","id":"UPA01058","properties":[{"key":"RectionId","value":"-"}]},{"database":"EvolutionaryTrace","id":"F1CMY8","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0051537","properties":[{"key":"GoTerm","value":"F:2 iron, 2 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"25049233"}]},{"database":"GO","id":"GO:0036200","properties":[{"key":"GoTerm","value":"F:3-ketosteroid 9-alpha-monooxygenase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"25049233"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"25049233"}]},{"database":"GO","id":"GO:0006707","properties":[{"key":"GoTerm","value":"P:cholesterol catabolic process"},{"key":"GoEvidenceType","value":"NAS:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"25049233"}]},{"database":"CDD","id":"cd03531","properties":[{"key":"EntryName","value":"Rieske_RO_Alpha_KSH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.102.10.10:FF:000012","properties":[{"key":"EntryName","value":"3-ketosteroid-9-alpha-hydroxylase oxygenase subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.380.10:FF:000004","properties":[{"key":"EntryName","value":"3-ketosteroid-9-alpha-hydroxylase oxygenase subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.380.10","properties":[{"key":"EntryName","value":"Naphthalene 1,2-dioxygenase Alpha Subunit, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.102.10.10","properties":[{"key":"EntryName","value":"Rieske [2Fe-2S] iron-sulphur domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050584","properties":[{"key":"EntryName","value":"Cholesterol_7-desaturase"}]},{"database":"InterPro","id":"IPR045605","properties":[{"key":"EntryName","value":"KshA-like_C"}]},{"database":"InterPro","id":"IPR017941","properties":[{"key":"EntryName","value":"Rieske_2Fe-2S"}]},{"database":"InterPro","id":"IPR036922","properties":[{"key":"EntryName","value":"Rieske_2Fe-2S_sf"}]},{"database":"PANTHER","id":"PTHR21266:SF60","properties":[{"key":"EntryName","value":"3-KETOSTEROID-9-ALPHA-MONOOXYGENASE, OXYGENASE COMPONENT"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21266","properties":[{"key":"EntryName","value":"IRON-SULFUR DOMAIN CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF19298","properties":[{"key":"EntryName","value":"KshA_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00355","properties":[{"key":"EntryName","value":"Rieske"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55961","properties":[{"key":"EntryName","value":"Bet v1-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50022","properties":[{"key":"EntryName","value":"ISP domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51296","properties":[{"key":"EntryName","value":"RIESKE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSIDTARSGSDDDVEIREIQAAAAPTRFARGWHCLGLLRDFQDGKPHSIEAFGTKLVVFADSKGQLNVLDAYCRHMGGDLSRGEVKGDSIACPFHDWRWNGKGKCTDIPYARRVPPIAKTRAWTTLERNGQLYVWNDPQGNPPPEDVTIPEIAGYGTDEWTDWSWKSLRIKGSHCREIVDNVVDMAHFFYIHYSFPRYFKNVFEGHTATQYMHSTGREDVISGTNYDDPNAELRSEATYFGPSYMIDWLESDANGQTIETILINCHYPVSNNEFVLQYGAIVKKLPGVSDEIAAGMAEQFAEGVQLGFEQDVEIWKNKAPIDNPLLSEEDGPVYQLRRWYQQFYVDVEDITEDMTKRFEFEIDTTRAVASWQKEVAENLAKQAEGSTATP","length":390,"molWeight":44249,"crc64":"46E13D2C9B6F7025","md5":"0513825A6FAE8A49386FEF436741A346"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SUBUNIT":1,"INDUCTION":1},"countByFeatureType":{"Chain":1,"Domain":1,"Binding site":8,"Helix":17,"Beta strand":21,"Turn":3},"uniParcId":"UPI0002020EA5"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P29378","uniProtkbId":"NHA2_RHORH","entryAudit":{"firstPublicDate":"1992-12-01","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2007-01-23","entryVersion":98,"sequenceVersion":3},"annotationScore":4.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"28644864"}],"value":"Low-molecular weight cobalt-containing nitrile hydratase subunit alpha"},"shortNames":[{"value":"L-NHase"},{"value":"L-nitrilase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1840499"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28644864"}],"value":"4.2.1.84"}]}},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1840499"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28644864"}],"value":"NHase catalyzes the hydration of various nitrile compounds to the corresponding amides (PubMed:1840499, PubMed:28644864). The alpha subunit functions as the catalytic subunit of the NHase complex while the beta subunit plays a structural/accessory role (PubMed:28644864)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an aliphatic primary amide = an aliphatic nitrile + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12673"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:65285"},{"database":"ChEBI","id":"CHEBI:80291"}],"ecNumber":"4.2.1.84","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1840499"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28644864"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:12675"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1840499"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28644864"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Co(3+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1840499"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28644864"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49415"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q7SID2"}],"value":"Binds 1 Co(3+) ion per heterodimer."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1840499"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28644864"}],"value":"Component of the NHase complex, composed of two heterodimers of alpha and beta subunits"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P29378","intActId":"EBI-15729943"},"interactantTwo":{"uniProtKBAccession":"P96453","geneName":"nhlE","intActId":"EBI-15729982"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P29378","intActId":"EBI-15729943"},"interactantTwo":{"uniProtKBAccession":"P29379","intActId":"EBI-15729954"},"numberOfExperiments":2,"organismDiffer":false}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1840499"}],"value":"By cobalt, cyclohexanecarboxamide and crotonamide"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P13448"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q7SID2"}],"value":"Oxidized (By similarity). Oxidation on Cys-112 is essential for enzymatic activity (By similarity). The cysteine-sulfenic acid formed from the oxidation of Cys-114 may be required to act as a nucleophile and initiate catalysis (By similarity)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Industrial production of acrylamide and nicotinamide is now being developed using some of these enzymes"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28644864"}],"value":"The complex exhibits higher thermostability than the high-molecular weight NHase complex, H-NHase"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the nitrile hydratase subunit alpha family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed"},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":207,"modifier":"EXACT"}},"description":"Low-molecular weight cobalt-containing nitrile hydratase subunit alpha","featureId":"PRO_0000186825"},{"type":"Active site","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q7SID2"}]},{"type":"Binding site","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49415"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q7SID2"}],"ligand":{"name":"Co(3+)","id":"ChEBI:CHEBI:49415"}},{"type":"Binding site","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49415"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q7SID2"}],"ligand":{"name":"Co(3+)","id":"ChEBI:CHEBI:49415"}},{"type":"Binding site","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":113,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49415"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q7SID2"}],"ligand":{"name":"Co(3+)","id":"ChEBI:CHEBI:49415"}},{"type":"Binding site","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49415"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q7SID2"}],"ligand":{"name":"Co(3+)","id":"ChEBI:CHEBI:49415"}},{"type":"Modified residue","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"Cysteine sulfinic acid (-SO2H)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q7SID2"}]},{"type":"Modified residue","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"Cysteine sulfenic acid (-SOH)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q7SID2"}]},{"type":"Disulfide bond","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q7SID2"}]}],"keywords":[{"id":"KW-0170","category":"Ligand","name":"Cobalt"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0558","category":"PTM","name":"Oxidation"}],"references":[{"referenceNumber":1,"citation":{"id":"1840499","citationType":"journal article","authors":["Kobayashi M.","Nishiyama M.","Nagasawa T.","Horinouchi S.","Beppu T.","Yamada H."],"citationCrossReferences":[{"database":"PubMed","id":"1840499"},{"database":"DOI","id":"10.1016/0167-4781(91)90208-4"}],"title":"Cloning, nucleotide sequence and expression in Escherichia coli of two cobalt-containing nitrile hydratase genes from Rhodococcus rhodochrous J1.","publicationDate":"1991","journal":"Biochim. Biophys. Acta","firstPage":"23","lastPage":"33","volume":"1129"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 2-16; 33-58; 63-70; 83-104; 129-133 AND 142-192","FUNCTION","CATALYTIC ACTIVITY","COFACTOR","SUBUNIT","INDUCTION BY COBALT; CYCLOHEXANECARBOXAMIDE AND CROTONAMIDE"],"referenceComments":[{"value":"J1","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"28644864","citationType":"journal article","authors":["Lan Y.","Zhang X.","Liu Z.","Zhou L.","Shen R.","Zhong X.","Cui W.","Zhou Z."],"citationCrossReferences":[{"database":"PubMed","id":"28644864"},{"database":"DOI","id":"10.1371/journal.pone.0179833"}],"title":"Overexpression and characterization of two types of nitrile hydratases from Rhodococcus rhodochrous J1.","publicationDate":"2017","journal":"PLoS ONE","firstPage":"e0179833","lastPage":"e0179833","volume":"12"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","COFACTOR","SUBUNIT"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X64360","properties":[{"key":"ProteinId","value":"CAA45712.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"S19716","properties":[{"key":"EntryName","value":"S19716"}]},{"database":"RefSeq","id":"WP_088899668.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP027558.1"}]},{"database":"AlphaFoldDB","id":"P29378","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P29378","properties":[{"key":"Description","value":"-"}]},{"database":"DIP","id":"DIP-46299N","properties":[{"key":"Description","value":"-"}]},{"database":"IntAct","id":"P29378","properties":[{"key":"Interactions","value":"2"}]},{"database":"BRENDA","id":"4.2.1.84","properties":[{"key":"OrganismId","value":"5395"}]},{"database":"GO","id":"GO:0018822","properties":[{"key":"GoTerm","value":"F:nitrile hydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046914","properties":[{"key":"GoTerm","value":"F:transition metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.90.330.10","properties":[{"key":"EntryName","value":"Nitrile hydratase alpha /Thiocyanate hydrolase gamma"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036648","properties":[{"key":"EntryName","value":"CN_Hdrase_a/SCN_Hdrase_g_sf"}]},{"database":"InterPro","id":"IPR004232","properties":[{"key":"EntryName","value":"CN_Hdrtase_a/SCN_Hdrlase_g"}]},{"database":"InterPro","id":"IPR023900","properties":[{"key":"EntryName","value":"CN_Hdrtase_asu/SCN_Hdrlase_gsu"}]},{"database":"InterPro","id":"IPR018141","properties":[{"key":"EntryName","value":"Nitrile_hydratase_asu"}]},{"database":"NCBIfam","id":"TIGR01323","properties":[{"key":"EntryName","value":"nitrile_alph"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02979","properties":[{"key":"EntryName","value":"NHase_alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001426","properties":[{"key":"EntryName","value":"NHase_alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56209","properties":[{"key":"EntryName","value":"Nitrile hydratase alpha chain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTAHNPVQGTLPRSNEEIAARVKAMEAILVDKGLISTDAIDHMSSVYENEVGPQLGAKIVARAWVDPEFKQRLLTDATSACREMGVGGMQGEEMVVLENTGTVHNMVVCTLCSCYPWPVLGLPPNWYKYPAYRARAVRDPRGVLAEFGYTPDPDVEIRIWDSSAELRYWVLPQRPAGTENFTEEQLADLVTRDSLIGVSVPTTPSKA","length":207,"molWeight":22848,"crc64":"B8E2BBFFF15B3D95","md5":"770B6F44780624C233EC7E7C3C642756"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"INTERACTION":2,"INDUCTION":1,"PTM":1,"BIOTECHNOLOGY":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Active site":1,"Binding site":4,"Modified residue":2,"Disulfide bond":1},"uniParcId":"UPI000004FA96"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"F1CMX6","uniProtkbId":"KSHA2_RHORH","entryAudit":{"firstPublicDate":"2016-11-30","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2011-05-03","entryVersion":38,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"Probable 3-ketosteroid-9-alpha-monooxygenase, oxygenase component"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"Probable 3-ketosteroid-9-alpha-hydroxylase, oxygenase component"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"KSH"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21642460"}],"value":"1.14.13.-"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21642460"}],"value":"Rieske-type oxygenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21642460"}],"value":"RO"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"kshA"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"kshA2"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21642460"}],"value":"Could catalyze the introduction of a 9alpha-hydroxyl moiety into the ring B of 3-ketosteroid substrates"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"[2Fe-2S] cluster","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:190135"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"}],"value":"Binds 1 [2Fe-2S] cluster per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Fe cation","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"F1CMY8"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:24875"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"F1CMY8"}],"value":"Binds 1 Fe cation."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"F1CMY8"}],"value":"Homotrimer. The two-component system 3-ketosteroid-9-alpha-monooxygenase is composed of an oxygenase component KshA and a reductase component KshB"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21642460"}],"value":"By cholic acid"}],"commentType":"INDUCTION"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"Probable 3-ketosteroid-9-alpha-monooxygenase, oxygenase component","featureId":"PRO_0000438400"},{"type":"Domain","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"Rieske","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"}]},{"type":"Binding site","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":67,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":89,"modifier":"EXACT"},"end":{"value":89,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"F1CMY8"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"F1CMY8"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"F1CMY8"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":307,"modifier":"EXACT"},"end":{"value":307,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"F1CMY8"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}}],"keywords":[{"id":"KW-0001","category":"Ligand","name":"2Fe-2S"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"id":"KW-0442","category":"Biological process","name":"Lipid degradation"},{"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0520","category":"Ligand","name":"NAD"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0753","category":"Biological process","name":"Steroid metabolism"}],"references":[{"referenceNumber":1,"citation":{"id":"21642460","citationType":"journal article","authors":["Petrusma M.","Hessels G.","Dijkhuizen L.","van der Geize R."],"citationCrossReferences":[{"database":"PubMed","id":"21642460"},{"database":"DOI","id":"10.1128/jb.00274-11"}],"title":"Multiplicity of 3-ketosteroid-9alpha-hydroxylase enzymes in Rhodococcus rhodochrous DSM43269 for specific degradation of different classes of steroids.","publicationDate":"2011","journal":"J. Bacteriol.","firstPage":"3931","lastPage":"3940","volume":"193"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","INDUCTION"],"referenceComments":[{"value":"DSM 43269","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"HQ425874","properties":[{"key":"ProteinId","value":"ADY18316.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_283479672.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JASIRK010000006.1"}]},{"database":"AlphaFoldDB","id":"F1CMX6","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"F1CMX6","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"1.14.15.30","properties":[{"key":"OrganismId","value":"5395"}]},{"database":"GO","id":"GO:0051537","properties":[{"key":"GoTerm","value":"F:2 iron, 2 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0004497","properties":[{"key":"GoTerm","value":"F:monooxygenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0016705","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0008203","properties":[{"key":"GoTerm","value":"P:cholesterol metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd03531","properties":[{"key":"EntryName","value":"Rieske_RO_Alpha_KSH"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.380.10","properties":[{"key":"EntryName","value":"Naphthalene 1,2-dioxygenase Alpha Subunit, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.102.10.10","properties":[{"key":"EntryName","value":"Rieske [2Fe-2S] iron-sulphur domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050584","properties":[{"key":"EntryName","value":"Cholesterol_7-desaturase"}]},{"database":"InterPro","id":"IPR045605","properties":[{"key":"EntryName","value":"KshA-like_C"}]},{"database":"InterPro","id":"IPR017941","properties":[{"key":"EntryName","value":"Rieske_2Fe-2S"}]},{"database":"InterPro","id":"IPR036922","properties":[{"key":"EntryName","value":"Rieske_2Fe-2S_sf"}]},{"database":"PANTHER","id":"PTHR21266:SF60","properties":[{"key":"EntryName","value":"3-KETOSTEROID-9-ALPHA-MONOOXYGENASE, OXYGENASE COMPONENT"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21266","properties":[{"key":"EntryName","value":"IRON-SULFUR DOMAIN CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF19298","properties":[{"key":"EntryName","value":"KshA_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00355","properties":[{"key":"EntryName","value":"Rieske"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55961","properties":[{"key":"EntryName","value":"Bet v1-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50022","properties":[{"key":"EntryName","value":"ISP domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51296","properties":[{"key":"EntryName","value":"RIESKE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGSTDTEDQVRTIDVGTPPERYARGWHCLGLVRDFADGKPHQVDAFGTSLVVFAGEDGKLNVLDAYCRHMGGNLAQGSVKGNTIACPFHDWRWRGDGKCAEIPYARRVPPLARTRTWPVAEVSGQLFVWHDPQGSKPPAELAVPEVPTYGDPGWTDWVWNSIEVTGSHCREIVDNVVDMAHFFYVHYGMPTYFRNVFEGHTATQVMRSLPRADAVGVSQATNYSAESRSDATYYGPSYMIDKLWSAGRDPESTPNIYLINCHYPISPTSFRLQYGVMVERPEGVPPEQAEQIAQAVAQGVAIGFEQDVEIWKNKSRIDNPLLCEEDGPVYQLRRWYEQFYVDVEDIRPEMVNRFEYEIDTTRALTSWQAEVDENVAAGRSAFAPNLTRAREAASAESGS","length":399,"molWeight":44753,"crc64":"6777F0704FB53D2E","md5":"74C8438646E8524C26BBC02FDABC0D08"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":2,"SUBUNIT":1,"INDUCTION":1},"countByFeatureType":{"Chain":1,"Domain":1,"Binding site":8},"uniParcId":"UPI0002020DC4"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P0A3G2","secondaryAccessions":["Q53042"],"uniProtkbId":"DHAA_RHORH","entryAudit":{"firstPublicDate":"2005-03-15","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2005-03-15","entryVersion":77,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Haloalkane dehalogenase"},"ecNumbers":[{"value":"3.8.1.5"}]}},"genes":[{"geneName":{"value":"dhaA"}}],"comments":[{"texts":[{"value":"Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Expresses halogenase activity against 1-chloroalkanes of chain length C3 to C10, and also shows a very weak activity with 1,2-dichloroethane"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1-haloalkane + H2O = a halide anion + a primary alcohol + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19081"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15734"},{"database":"ChEBI","id":"CHEBI:16042"},{"database":"ChEBI","id":"CHEBI:18060"}],"ecNumber":"3.8.1.5"}},{"texts":[{"value":"Xenobiotic degradation; haloalkane degradation"}],"commentType":"PATHWAY"},{"texts":[{"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"value":"By 1-haloalkanes"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the haloalkane dehalogenase family. Type 2 subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"Haloalkane dehalogenase","featureId":"PRO_0000216775"},{"type":"Domain","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"AB hydrolase-1","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Active site","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Active site","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Active site","location":{"start":{"value":272,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Beta strand","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Beta strand","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Beta strand","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Beta strand","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Helix","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Turn","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":51,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Helix","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":55,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Turn","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Beta strand","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Helix","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Beta strand","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Helix","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Helix","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Beta strand","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Beta strand","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3RK4"}]},{"type":"Helix","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Helix","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Helix","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Beta strand","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Helix","location":{"start":{"value":160,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Helix","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Helix","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9HKF"}]},{"type":"Beta strand","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Helix","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Helix","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Helix","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Helix","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Helix","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Beta strand","location":{"start":{"value":236,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Beta strand","location":{"start":{"value":245,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Helix","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":258,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Beta strand","location":{"start":{"value":262,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Helix","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Helix","location":{"start":{"value":279,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]},{"type":"Helix","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FLK"}]}],"geneLocations":[{"value":"pRTL1","geneEncodingType":"Plasmid"}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0216","category":"Biological process","name":"Detoxification"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0614","category":"Technical term","name":"Plasmid"}],"references":[{"referenceNumber":1,"citation":{"id":"9025284","citationType":"journal article","authors":["Kulakova A.N.","Larkin M.J.","Kulakov L.A."],"citationCrossReferences":[{"database":"PubMed","id":"9025284"},{"database":"DOI","id":"10.1099/00221287-143-1-109"}],"title":"The plasmid-located haloalkane dehalogenase gene from Rhodococcus rhodochrous NCIMB 13064.","publicationDate":"1997","journal":"Microbiology","firstPage":"109","lastPage":"115","volume":"143"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"NCIMB 13064","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AF060871","properties":[{"key":"ProteinId","value":"AAC15838.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PDB","id":"2V9Z","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.00 A"},{"key":"Chains","value":"A=1-293"}]},{"database":"PDB","id":"3FBW","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.23 A"},{"key":"Chains","value":"A=1-293"}]},{"database":"PDB","id":"3RK4","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.31 A"},{"key":"Chains","value":"A=1-293"}]},{"database":"PDB","id":"3SK0","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.78 A"},{"key":"Chains","value":"A=1-293"}]},{"database":"PDB","id":"4E46","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.26 A"},{"key":"Chains","value":"A=1-293"}]},{"database":"PDB","id":"4F5Z","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.20 A"},{"key":"Chains","value":"A=1-293"}]},{"database":"PDB","id":"4F60","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.45 A"},{"key":"Chains","value":"A=1-293"}]},{"database":"PDB","id":"4FWB","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.26 A"},{"key":"Chains","value":"A=4-293"}]},{"database":"PDB","id":"4WCV","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.69 A"},{"key":"Chains","value":"A=1-293"}]},{"database":"PDB","id":"5FLK","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"0.99 A"},{"key":"Chains","value":"A=1-293"}]},{"database":"PDB","id":"5UXZ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.92 A"},{"key":"Chains","value":"A/B=4-290"}]},{"database":"PDB","id":"5UY1","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.35 A"},{"key":"Chains","value":"A/B=4-290"}]},{"database":"PDB","id":"5VNP","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.23 A"},{"key":"Chains","value":"A/B=4-293"}]},{"database":"PDB","id":"6SP5","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.60 A"},{"key":"Chains","value":"A/B=3-293"}]},{"database":"PDB","id":"6SP8","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.55 A"},{"key":"Chains","value":"A/B=3-293"}]},{"database":"PDB","id":"6TY7","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.50 A"},{"key":"Chains","value":"A/B=1-293"}]},{"database":"PDB","id":"6XT8","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.70 A"},{"key":"Chains","value":"A/B/C/D=1-293"}]},{"database":"PDB","id":"6XTC","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.54 A"},{"key":"Chains","value":"A/B/C/D=1-293"}]},{"database":"PDB","id":"7O3O","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.25 A"},{"key":"Chains","value":"A=1-293"}]},{"database":"PDB","id":"7O8B","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.75 A"},{"key":"Chains","value":"A=4-293"}]},{"database":"PDB","id":"9HKF","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.40 A"},{"key":"Chains","value":"A/B=3-256, A/B=258-272, A/B=275-290"}]},{"database":"AlphaFoldDB","id":"P0A3G2","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P0A3G2","properties":[{"key":"Description","value":"-"}]},{"database":"ESTHER","id":"rhoso-halo1","properties":[{"key":"FamilyName","value":"Haloalkane_dehalogenase-HLD2"}]},{"database":"BRENDA","id":"3.8.1.5","properties":[{"key":"OrganismId","value":"5395"}]},{"database":"SABIO-RK","id":"P0A3G2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00007","properties":[{"key":"RectionId","value":"-"}]},{"database":"EvolutionaryTrace","id":"P0A3G2","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0016020","properties":[{"key":"GoTerm","value":"C:membrane"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0018786","properties":[{"key":"GoTerm","value":"F:haloalkane dehalogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.40.50.1820","properties":[{"key":"EntryName","value":"alpha/beta hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01231","properties":[{"key":"EntryName","value":"Haloalk_dehal_type2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000073","properties":[{"key":"EntryName","value":"AB_hydrolase_1"}]},{"database":"InterPro","id":"IPR029058","properties":[{"key":"EntryName","value":"AB_hydrolase_fold"}]},{"database":"InterPro","id":"IPR050266","properties":[{"key":"EntryName","value":"AB_hydrolase_sf"}]},{"database":"InterPro","id":"IPR000639","properties":[{"key":"EntryName","value":"Epox_hydrolase-like"}]},{"database":"InterPro","id":"IPR023594","properties":[{"key":"EntryName","value":"Haloalkane_dehalogenase_2"}]},{"database":"NCBIfam","id":"NF002938","properties":[{"key":"EntryName","value":"PRK03592.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43798:SF24","properties":[{"key":"EntryName","value":"CIS-3-ALKYL-4-ALKYLOXETAN-2-ONE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43798","properties":[{"key":"EntryName","value":"MONOACYLGLYCEROL LIPASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00561","properties":[{"key":"EntryName","value":"Abhydrolase_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00412","properties":[{"key":"EntryName","value":"EPOXHYDRLASE"}]},{"database":"SUPFAM","id":"SSF53474","properties":[{"key":"EntryName","value":"alpha/beta-Hydrolases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSEIGTGFPFDPHYVEVLGERMHYVDVGPRDGTPVLFLHGNPTSSYLWRNIIPHVAPSHRCIAPDLIGMGKSDKPDLDYFFDDHVRYLDAFIEALGLEEVVLVIHDWGSALGFHWAKRNPERVKGIACMEFIRPIPTWDEWPEFARETFQAFRTADVGRELIIDQNAFIEGALPKCVVRPLTEVEMDHYREPFLKPVDREPLWRFPNELPIAGEPANIVALVEAYMNWLHQSPVPKLLFWGTPGVLIPPAEAARLAESLPNCKTVDIGPGLHYLQEDNPDLIGSEIARWLPAL","length":293,"molWeight":33246,"crc64":"2B637C53E36BE9F3","md5":"51448B993B58BBB29F790AA6F263D657"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"INDUCTION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":1,"Active site":3,"Beta strand":13,"Helix":20,"Turn":2},"uniParcId":"UPI000012926F"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q03217","uniProtkbId":"NRL2_RHORH","entryAudit":{"firstPublicDate":"1993-10-01","lastAnnotationUpdateDate":"2025-02-05","lastSequenceUpdateDate":"2007-01-23","entryVersion":75,"sequenceVersion":2},"annotationScore":3.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Aliphatic nitrilase"},"ecNumbers":[{"value":"3.5.5.7"}]}},"genes":[{"geneName":{"value":"nitA"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an aliphatic nitrile + 2 H2O = a carboxylate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46188"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29067"},{"database":"ChEBI","id":"CHEBI:80291"}],"ecNumber":"3.5.5.7"}},{"texts":[{"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the carbon-nitrogen hydrolase superfamily. Nitrilase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed"},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":366,"modifier":"EXACT"}},"description":"Aliphatic nitrilase","featureId":"PRO_0000204046"},{"type":"Domain","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":282,"modifier":"EXACT"}},"description":"CN hydrolase","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00054"}]},{"type":"Region","location":{"start":{"value":346,"modifier":"EXACT"},"end":{"value":366,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":355,"modifier":"EXACT"},"end":{"value":366,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":48,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00054"}]},{"type":"Active site","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00054"}]},{"type":"Active site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00054"},{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU10105"}]},{"type":"Mutagenesis","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"100% loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1400390"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["S","A"]}}],"keywords":[{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"}],"references":[{"referenceNumber":1,"citation":{"id":"1400390","citationType":"journal article","authors":["Kobayashi M.","Komeda H.","Yanaka N.","Nagasawa T.","Yamada H."],"citationCrossReferences":[{"database":"PubMed","id":"1400390"},{"database":"DOI","id":"10.1016/s0021-9258(19)36749-3"}],"title":"Nitrilase from Rhodococcus rhodochrous J1. Sequencing and overexpression of the gene and identification of an essential cysteine residue.","publicationDate":"1992","journal":"J. Biol. Chem.","firstPage":"20746","lastPage":"20751","volume":"267"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PARTIAL PROTEIN SEQUENCE","MUTAGENESIS OF CYS-165"],"referenceComments":[{"value":"J1","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D11425","properties":[{"key":"ProteinId","value":"BAA01994.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"D67026","properties":[{"key":"ProteinId","value":"BAA11037.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"A45070","properties":[{"key":"EntryName","value":"A45070"}]},{"database":"AlphaFoldDB","id":"Q03217","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q03217","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"3.5.5.7","properties":[{"key":"OrganismId","value":"5395"}]},{"database":"GO","id":"GO:0018762","properties":[{"key":"GoTerm","value":"F:aliphatic nitrilase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"CDD","id":"cd07564","properties":[{"key":"EntryName","value":"nitrilases_CHs"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.60.110.10","properties":[{"key":"EntryName","value":"Carbon-nitrogen hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003010","properties":[{"key":"EntryName","value":"C-N_Hydrolase"}]},{"database":"InterPro","id":"IPR036526","properties":[{"key":"EntryName","value":"C-N_Hydrolase_sf"}]},{"database":"InterPro","id":"IPR000132","properties":[{"key":"EntryName","value":"Nitrilase/CN_hydratase_CS"}]},{"database":"InterPro","id":"IPR044149","properties":[{"key":"EntryName","value":"Nitrilases_CHs"}]},{"database":"PANTHER","id":"PTHR46044:SF14","properties":[{"key":"EntryName","value":"ARYLACETONITRILASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46044","properties":[{"key":"EntryName","value":"NITRILASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00795","properties":[{"key":"EntryName","value":"CN_hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56317","properties":[{"key":"EntryName","value":"Carbon-nitrogen hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50263","properties":[{"key":"EntryName","value":"CN_HYDROLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00920","properties":[{"key":"EntryName","value":"NITRIL_CHT_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00921","properties":[{"key":"EntryName","value":"NITRIL_CHT_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVEYTNTFKVAAVQAQPVWFDAAKTVDKTVSIIAEAARNGCELVAFPEVFIPGYPYHIWVDSPLAGMAKFAVRYHENSLTMDSPHVQRLLDAARDHNIAVVVGISERDGGSLYMTQLVIDADGQLVARRRKLKPTHVERSVYGEGNGSDISVYDMPFARLGALNCWEHFQTLTKYAMYSMHEQVHVASWPGMSLYQPEVPAFGVDAQLTATRMYALEGQTFVVCTTQVVTPEAHEFFCDNDEQRKLIGRGGGFARIIGPDGRDLATPLAEDEEGILYADIDLSAITLAKQAADPVGHYSRPDVLSLNFNQRHTTPVNTAISTIHATHTLVPQSGALDGVRELNGADEQRALPSTHSDETDRATASI","length":366,"molWeight":40189,"crc64":"3B8E1274AE5EC287","md5":"E6EDAF2F893086AE5EC7572E7FC9627B"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Domain":1,"Region":1,"Compositional bias":1,"Active site":3,"Mutagenesis":1},"uniParcId":"UPI000016FF36"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P21220","uniProtkbId":"NHB1_RHORH","entryAudit":{"firstPublicDate":"1991-05-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1992-12-01","entryVersion":96,"sequenceVersion":2},"annotationScore":3.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1840499"}],"value":"High-molecular weight cobalt-containing nitrile hydratase subunit beta"},"shortNames":[{"value":"H-NHase"},{"value":"H-nitrilase"}]}},"genes":[{"geneName":{"value":"nhhB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12121763"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28644864"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35919716"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9650255"}],"value":"NHase catalyzes the hydration of various nitrile compounds to the corresponding amides (PubMed:12121763, PubMed:2013281, PubMed:28644864, PubMed:35919716, PubMed:9650255). The alpha subunit functions as the catalytic subunit of the NHase complex while the beta subunit plays a structural/accessory role (PubMed:12121763, PubMed:2013281, PubMed:28644864, PubMed:35919716, PubMed:9650255)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12121763"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1840499"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28644864"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35919716"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8633053"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9650255"}],"value":"Heteromultimer; the size of the heteromultimeric complex formed is essential for activity (PubMed:12121763, PubMed:1840499, PubMed:2013281, PubMed:28644864, PubMed:8633053, PubMed:9650255). Component of the NHase complex, composed of at least ten heterodimers of nhhA and nhhB (PubMed:12121763, PubMed:1840499, PubMed:2013281, PubMed:28644864, PubMed:35919716, PubMed:8633053, PubMed:9650255)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1840499"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2013281"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8633053"}],"value":"By cobalt, urea and crotonamide"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Industrial production of acrylamide and nicotinamide is now being developed using some of these enzymes"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28644864"}],"value":"The complex exhibits higher product tolerance than the low-molecular weight NHase complex, L-NHase"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the nitrile hydratase subunit beta family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"High-molecular weight cobalt-containing nitrile hydratase subunit beta","featureId":"PRO_0000186832"},{"type":"Mutagenesis","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"Increases the enzyme activity for bulkier substrates including cinnamonitrile compared to the wild-type.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35919716"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["F","H","L"]}},{"type":"Mutagenesis","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"Increases the enzyme activity for bulkier substrates including cinnamonitrile compared to the wild-type.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35919716"}],"alternativeSequence":{"originalSequence":"L","alternativeSequences":["H","K","Q","Y"]}},{"type":"Sequence conflict","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":7,"modifier":"EXACT"}},"description":"in Ref. 3; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["I"]}},{"type":"Sequence conflict","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"in Ref. 3; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{}}],"keywords":[{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"}],"references":[{"referenceNumber":1,"citation":{"id":"1840499","citationType":"journal article","authors":["Kobayashi M.","Nishiyama M.","Nagasawa T.","Horinouchi S.","Beppu T.","Yamada H."],"citationCrossReferences":[{"database":"PubMed","id":"1840499"},{"database":"DOI","id":"10.1016/0167-4781(91)90208-4"}],"title":"Cloning, nucleotide sequence and expression in Escherichia coli of two cobalt-containing nitrile hydratase genes from Rhodococcus rhodochrous J1.","publicationDate":"1991","journal":"Biochim. Biophys. Acta","firstPage":"23","lastPage":"33","volume":"1129"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 1-28 AND 69-78","SUBUNIT","INDUCTION BY COBALT; UREA AND CROTONAMIDE"],"referenceComments":[{"value":"J1","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"8633053","citationType":"journal article","authors":["Komeda H.","Kobayashi M.","Shimizu S."],"citationCrossReferences":[{"database":"PubMed","id":"8633053"},{"database":"DOI","id":"10.1073/pnas.93.9.4267"}],"title":"Characterization of the gene cluster of high-molecular-mass nitrile hydratase (H-NHase) induced by its reaction product in Rhodococcus rhodochrous J1.","publicationDate":"1996","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"4267","lastPage":"4272","volume":"93"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","SUBUNIT","INDUCTION BY UREA"],"referenceComments":[{"value":"J1","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"2013281","citationType":"journal article","authors":["Nagasawa T.","Takeuchi K.","Yamada H."],"citationCrossReferences":[{"database":"PubMed","id":"2013281"},{"database":"DOI","id":"10.1111/j.1432-1033.1991.tb15853.x"}],"title":"Characterization of a new cobalt-containing nitrile hydratase purified from urea-induced cells of Rhodococcus rhodochrous J1.","publicationDate":"1991","journal":"Eur. J. Biochem.","firstPage":"581","lastPage":"589","volume":"196"},"referencePositions":["PROTEIN SEQUENCE OF 1-28","FUNCTION","SUBUNIT","INDUCTION BY UREA"],"referenceComments":[{"value":"J1","type":"STRAIN"}]},{"referenceNumber":4,"citation":{"id":"9650255","citationType":"journal article","authors":["Mizunashi W.","Nishiyama M.","Horinouchi S.","Beppu T."],"citationCrossReferences":[{"database":"PubMed","id":"9650255"},{"database":"DOI","id":"10.1007/s002530051214"}],"title":"Overexpression of high-molecular-mass nitrile hydratase from Rhodococcus rhodochrous J1 in recombinant Rhodococcus cells.","publicationDate":"1998","journal":"Appl. Microbiol. Biotechnol.","firstPage":"568","lastPage":"572","volume":"49"},"referencePositions":["FUNCTION","SUBUNIT"]},{"referenceNumber":5,"citation":{"id":"12121763","citationType":"journal article","authors":["Hashimoto Y.","Sasaki S.","Herai S.","Oinuma K.","Shimizu S.","Kobayashi M."],"citationCrossReferences":[{"database":"PubMed","id":"12121763"},{"database":"DOI","id":"10.1016/s0162-0134(02)00373-2"}],"title":"Site-directed mutagenesis for cysteine residues of cobalt-containing nitrile hydratase.","publicationDate":"2002","journal":"J. Inorg. Biochem.","firstPage":"70","lastPage":"77","volume":"91"},"referencePositions":["FUNCTION","SUBUNIT"]},{"referenceNumber":6,"citation":{"id":"28644864","citationType":"journal article","authors":["Lan Y.","Zhang X.","Liu Z.","Zhou L.","Shen R.","Zhong X.","Cui W.","Zhou Z."],"citationCrossReferences":[{"database":"PubMed","id":"28644864"},{"database":"DOI","id":"10.1371/journal.pone.0179833"}],"title":"Overexpression and characterization of two types of nitrile hydratases from Rhodococcus rhodochrous J1.","publicationDate":"2017","journal":"PLoS ONE","firstPage":"e0179833","lastPage":"e0179833","volume":"12"},"referencePositions":["FUNCTION","SUBUNIT"]},{"referenceNumber":7,"citation":{"id":"35919716","citationType":"journal article","authors":["Ma D.","Cheng Z.","Peplowski L.","Han L.","Xia Y.","Hou X.","Guo J.","Yin D.","Rao Y.","Zhou Z."],"citationCrossReferences":[{"database":"PubMed","id":"35919716"},{"database":"DOI","id":"10.1039/d2sc02319a"}],"title":"Insight into the broadened substrate scope of nitrile hydratase by static and dynamic structure analysis.","publicationDate":"2022","journal":"Chem. Sci.","firstPage":"8417","lastPage":"8428","volume":"13"},"referencePositions":["FUNCTION","SUBUNIT","MUTAGENESIS OF SER-46 AND LEU-133"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X64359","properties":[{"key":"ProteinId","value":"CAA45709.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"D67027","properties":[{"key":"ProteinId","value":"BAA11043.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"S19713","properties":[{"key":"EntryName","value":"S19713"}]},{"database":"AlphaFoldDB","id":"P21220","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P21220","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:MONOMER-2284","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"4.2.1.84","properties":[{"key":"OrganismId","value":"22537"}]},{"database":"GO","id":"GO:0018822","properties":[{"key":"GoTerm","value":"F:nitrile hydratase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0046914","properties":[{"key":"GoTerm","value":"F:transition metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"2.30.30.50","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.472.20","properties":[{"key":"EntryName","value":"Nitrile hydratase, beta subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR049054","properties":[{"key":"EntryName","value":"CN_hydtase_beta-like_N"}]},{"database":"InterPro","id":"IPR042262","properties":[{"key":"EntryName","value":"CN_hydtase_beta_C"}]},{"database":"InterPro","id":"IPR024690","properties":[{"key":"EntryName","value":"CN_hydtase_beta_dom_C"}]},{"database":"InterPro","id":"IPR008990","properties":[{"key":"EntryName","value":"Elect_transpt_acc-like_dom_sf"}]},{"database":"InterPro","id":"IPR003168","properties":[{"key":"EntryName","value":"Nitrile_hydratase_bsu"}]},{"database":"NCBIfam","id":"TIGR03888","properties":[{"key":"EntryName","value":"nitrile_beta"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02211","properties":[{"key":"EntryName","value":"NHase_beta_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21006","properties":[{"key":"EntryName","value":"NHase_beta_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001427","properties":[{"key":"EntryName","value":"NHase_beta"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50090","properties":[{"key":"EntryName","value":"Electron transport accessory proteins"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDGIHDTGGMTGYGPVPYQKDEPFFHYEWEGRTLSILTWMHLKGISWWDKSRFFRESMGNENYVNEIRNSYYTHWLSAAERILVADKIITEEERKHRVQEILEGRYTDRKPSRKFDPAQIEKAIERLHEPHSLALPGAEPSFSLGDKIKVKSMNPLGHTRCPKYVRNKIGEIVAYHGCQIYPESSSAGLGDDPRPLYTVAFSAQELWGDDGNGKDVVCVDLWEPYLISA","length":229,"molWeight":26322,"crc64":"73270C13358D4671","md5":"4F849703CB6676B86364B7A497B96565"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"INDUCTION":1,"BIOTECHNOLOGY":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Mutagenesis":2,"Sequence conflict":2},"uniParcId":"UPI0000130030"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"E3UUE6","uniProtkbId":"FAC19_RHORH","entryAudit":{"firstPublicDate":"2014-10-29","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2011-01-11","entryVersion":35,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21602385"}],"value":"3-oxocholest-4-en-26-oate--CoA ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21602385"}],"value":"6.2.1.42"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21602385"}],"value":"Steroid-CoA ligase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21602385"}],"value":"Steroid-coenzyme A ligase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21602385"}],"value":"fadD19"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21602385"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24244004"}],"value":"Involved in the degradation of the side chains of C-24 branched-chain sterols. Catalyzes the ATP-dependent CoA thioesterification of the sterol 3-oxocholest-4-en-26-oate to yield 3-oxocholest-4-en-26-oyl-CoA. It can also use beta-sitosterol, campesterol and 3beta-hydroxy-5-cholesten-26-oate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(25S)-3-oxocholest-4-en-26-oate + ATP + CoA = (25S)-3-oxocholest-4-en-26-oyl-CoA + AMP + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:29291"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:71541"},{"database":"ChEBI","id":"CHEBI:83819"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.2.1.42","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21602385"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21602385"}],"value":"Steroid metabolism; cholesterol metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21602385"}],"value":"Cells lacking this gene are unable to degrade the side chain of C-24 branched sterols such as beta-sitosterol and campesterol"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the ATP-dependent AMP-binding enzyme family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":555,"modifier":"EXACT"}},"description":"3-oxocholest-4-en-26-oate--CoA ligase","featureId":"PRO_0000430658"},{"type":"Region","location":{"start":{"value":525,"modifier":"EXACT"},"end":{"value":555,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":544,"modifier":"EXACT"},"end":{"value":555,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":418,"modifier":"EXACT"},"end":{"value":418,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":433,"modifier":"EXACT"},"end":{"value":433,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":524,"modifier":"EXACT"},"end":{"value":524,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0153","category":"Biological process","name":"Cholesterol metabolism"},{"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0753","category":"Biological process","name":"Steroid metabolism"},{"id":"KW-1207","category":"Biological process","name":"Sterol metabolism"}],"references":[{"referenceNumber":1,"citation":{"id":"21602385","citationType":"journal article","authors":["Wilbrink M.H.","Petrusma M.","Dijkhuizen L.","van der Geize R."],"citationCrossReferences":[{"database":"PubMed","id":"21602385"},{"database":"DOI","id":"10.1128/aem.00380-11"}],"title":"FadD19 of Rhodococcus rhodochrous DSM43269, a steroid-coenzyme A ligase essential for degradation of C-24 branched sterol side chains.","publicationDate":"2011","journal":"Appl. Environ. Microbiol.","firstPage":"4455","lastPage":"4464","volume":"77"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","CATALYTIC ACTIVITY","DISRUPTION PHENOTYPE","SUBSTRATE SPECIFICITY"],"referenceComments":[{"value":"DSM43269","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"24244004","citationType":"journal article","authors":["Casabon I.","Swain K.","Crowe A.M.","Eltis L.D.","Mohn W.W."],"citationCrossReferences":[{"database":"PubMed","id":"24244004"},{"database":"DOI","id":"10.1128/jb.01012-13"}],"title":"Actinobacterial acyl coenzyme A synthetases involved in steroid side-chain catabolism.","publicationDate":"2014","journal":"J. Bacteriol.","firstPage":"579","lastPage":"587","volume":"196"},"referencePositions":["FUNCTION"],"referenceComments":[{"value":"DSM43269","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"HM588719","properties":[{"key":"ProteinId","value":"ADP09625.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_283479969.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JASIRK010000008.1"}]},{"database":"AlphaFoldDB","id":"E3UUE6","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"E3UUE6","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1829.GCA_000716895_01595","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ag:ADP09625","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:MONOMER-16899","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00296","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0016878","properties":[{"key":"GoTerm","value":"F:acid-thiol ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0008203","properties":[{"key":"GoTerm","value":"P:cholesterol metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd05924","properties":[{"key":"EntryName","value":"FACL_like_5"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.300.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.12780","properties":[{"key":"EntryName","value":"N-terminal domain of ligase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR045851","properties":[{"key":"EntryName","value":"AMP-b_sf"}]},{"database":"InterPro","id":"IPR025110","properties":[{"key":"EntryName","value":"AMP-bd_C"}]},{"database":"InterPro","id":"IPR020845","properties":[{"key":"EntryName","value":"AMP-binding_CS"}]},{"database":"InterPro","id":"IPR000873","properties":[{"key":"EntryName","value":"AMP-dep_synth/lig_dom"}]},{"database":"InterPro","id":"IPR042099","properties":[{"key":"EntryName","value":"ANL_N_sf"}]},{"database":"InterPro","id":"IPR050237","properties":[{"key":"EntryName","value":"ATP-dep_AMP-bd_enzyme"}]},{"database":"NCBIfam","id":"NF005863","properties":[{"key":"EntryName","value":"PRK07798.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43767","properties":[{"key":"EntryName","value":"LONG-CHAIN-FATTY-ACID--COA LIGASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43767:SF1","properties":[{"key":"EntryName","value":"NONRIBOSOMAL PEPTIDE SYNTHASE PES1 (EUROFUNG)-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00501","properties":[{"key":"EntryName","value":"AMP-binding"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13193","properties":[{"key":"EntryName","value":"AMP-binding_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56801","properties":[{"key":"EntryName","value":"Acetyl-CoA synthetase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00455","properties":[{"key":"EntryName","value":"AMP_BINDING"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MALNIADLVEHAIDLVPERVALASDGREVTYAQLEERANRLAHYLREQGVEPGDKVGIYSRNTIEAVEAMIAVFKIRAIMINVNYRYVENELQYIFDNSDMVALIHERRYSDKVANVLPSTPLVKTVVVVEDGTDVDFSAYGGIEYEAALAQSSPERDFEDRSADDIYILYTGGTTGHPKGVMWRHEDVWRVLGGGINFMTGEWVKDEWQLAKEGAENPGLVRYPIPPMIHGGAQWALFQSLFSGGKVIMHPEFSGHEVWRIIDDHKVNVIFITGDAMARPMLDALEEGNPKTGKPYDLSTLFAMASSAALFSPSIKDRFLDLLPGKIITDSIGSSETGFGGIGIAEKGKTLGGGPTVKIDESTTVLDDDGNPIEPGSGKVGMVARTGNIPLGYYKDEAKTKATFREYNGIRYSIPGDYARVEADGTVTMLGRGSVSINSGGEKVYPEEVEGALKQHPAVFDALVVGVPDERFGERVSAVVALRDGEQVTLDELMTTARSKIAGYKVPRAVWFVDEIKRSPAGKPDYRWAKDQTGLRPADEVYNNGDGNGAAATG","length":555,"molWeight":60602,"crc64":"0C884C255591F0E3","md5":"6645FE916B94DCA7C46D15C0062C647A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"DISRUPTION PHENOTYPE":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Region":1,"Compositional bias":1,"Binding site":4},"uniParcId":"UPI0001ECFC19"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"F1CMX8","uniProtkbId":"KSHA3_RHORH","entryAudit":{"firstPublicDate":"2016-11-30","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2011-05-03","entryVersion":50,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"3-ketosteroid-9-alpha-monooxygenase, oxygenase component"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"3-ketosteroid-9-alpha-hydroxylase, oxygenase component"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"KSH"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"Androsta-1,4-diene-3,17-dione 9-alpha-hydroxylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21642460"}],"value":"1.14.15.30"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21642460"}],"value":"Rieske-type oxygenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21642460"}],"value":"RO"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"kshA"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21642460"}],"value":"kshA3"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21642460"}],"value":"In vitro, catalyzes the introduction of a 9alpha-hydroxyl moiety into the ring B of 3-ketosteroid substrates such as 1,4-androstadiene-3,17-dione (ADD), 4-androstene-3,17-dione (AD), 4-androstene-17beta-ol-3-one (testosterone), 4-pregnene-3,20-dione (progesterone), 23,24-bisnorcholesta-4-ene-22-oate and 23,24-bisnorcholesta-1,4-diene-22-oate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"androsta-1,4-diene-3,17-dione + 2 reduced [2Fe-2S]-[ferredoxin] + O2 + 2 H(+) = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized [2Fe-2S]-[ferredoxin] + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32199"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:40799"},{"database":"ChEBI","id":"CHEBI:63641"}],"ecNumber":"1.14.15.30","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21642460"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[2Fe-2S] cluster","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:190135"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"}],"value":"Binds 1 [2Fe-2S] cluster per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Fe cation","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"F1CMY8"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:24875"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"F1CMY8"}],"value":"Binds 1 Fe cation."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"F1CMY8"}],"value":"Homotrimer. The two-component system 3-ketosteroid-9-alpha-monooxygenase is composed of an oxygenase component KshA and a reductase component KshB"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21642460"}],"value":"By 4-androstene-3,17-dione (AD)"}],"commentType":"INDUCTION"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"3-ketosteroid-9-alpha-monooxygenase, oxygenase component","featureId":"PRO_0000438401"},{"type":"Domain","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"Rieske","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"}]},{"type":"Binding site","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":83,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00628"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"F1CMY8"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"F1CMY8"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"F1CMY8"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"F1CMY8"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}}],"keywords":[{"id":"KW-0001","category":"Ligand","name":"2Fe-2S"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"id":"KW-0442","category":"Biological process","name":"Lipid degradation"},{"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0753","category":"Biological process","name":"Steroid metabolism"}],"references":[{"referenceNumber":1,"citation":{"id":"21642460","citationType":"journal article","authors":["Petrusma M.","Hessels G.","Dijkhuizen L.","van der Geize R."],"citationCrossReferences":[{"database":"PubMed","id":"21642460"},{"database":"DOI","id":"10.1128/jb.00274-11"}],"title":"Multiplicity of 3-ketosteroid-9alpha-hydroxylase enzymes in Rhodococcus rhodochrous DSM43269 for specific degradation of different classes of steroids.","publicationDate":"2011","journal":"J. Bacteriol.","firstPage":"3931","lastPage":"3940","volume":"193"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","CATALYTIC ACTIVITY","INDUCTION","SUBSTRATE SPECIFICITY"],"referenceComments":[{"value":"DSM 43269","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"HQ425875","properties":[{"key":"ProteinId","value":"ADY18318.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_059382556.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP032221.1"}]},{"database":"AlphaFoldDB","id":"F1CMX8","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"F1CMX8","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1829.GCA_000716895_01734","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"1.14.15.30","properties":[{"key":"OrganismId","value":"5395"}]},{"database":"GO","id":"GO:0051537","properties":[{"key":"GoTerm","value":"F:2 iron, 2 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0036200","properties":[{"key":"GoTerm","value":"F:3-ketosteroid 9-alpha-monooxygenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0008203","properties":[{"key":"GoTerm","value":"P:cholesterol metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd03531","properties":[{"key":"EntryName","value":"Rieske_RO_Alpha_KSH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.102.10.10:FF:000012","properties":[{"key":"EntryName","value":"3-ketosteroid-9-alpha-hydroxylase oxygenase subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.380.10:FF:000004","properties":[{"key":"EntryName","value":"3-ketosteroid-9-alpha-hydroxylase oxygenase subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.380.10","properties":[{"key":"EntryName","value":"Naphthalene 1,2-dioxygenase Alpha Subunit, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.102.10.10","properties":[{"key":"EntryName","value":"Rieske [2Fe-2S] iron-sulphur domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050584","properties":[{"key":"EntryName","value":"Cholesterol_7-desaturase"}]},{"database":"InterPro","id":"IPR045605","properties":[{"key":"EntryName","value":"KshA-like_C"}]},{"database":"InterPro","id":"IPR017941","properties":[{"key":"EntryName","value":"Rieske_2Fe-2S"}]},{"database":"InterPro","id":"IPR036922","properties":[{"key":"EntryName","value":"Rieske_2Fe-2S_sf"}]},{"database":"PANTHER","id":"PTHR21266:SF60","properties":[{"key":"EntryName","value":"3-KETOSTEROID-9-ALPHA-MONOOXYGENASE, OXYGENASE COMPONENT"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21266","properties":[{"key":"EntryName","value":"IRON-SULFUR DOMAIN CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF19298","properties":[{"key":"EntryName","value":"KshA_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00355","properties":[{"key":"EntryName","value":"Rieske"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55961","properties":[{"key":"EntryName","value":"Bet v1-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50022","properties":[{"key":"EntryName","value":"ISP domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51296","properties":[{"key":"EntryName","value":"RIESKE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAQIREIDVGEVRTRFARGWHCLGLSRTFKDGKPHAVEAFGTKLVVWADSNGEPKVLDAYCRHMGGDLSQGEIKGDSVACPFHDWRWGGNGKCTDIPYARRVPPLARTRSWITMEKHGQLFVWNDPEGNTPPPEVTIPEIEQYGSDEWTDWTWNQIRIEGSNCREIIDNVVDMAHFFYIHYAFPTFFKNVFEGHIAEQYLNTRGRPDKGMATQYGLESTLESYAAYYGPSYMINPLKNNYGGYQTESVLINCHYPITHDSFMLQYGIIVKKPQGMSPEQSDVLAAKLTEGVGEGFLQDVEIWKNKTKIENPLLCEEDGPVYQLRRWYEQFYVDVADVTEKMTGRFEFEVDTAKANEAWEKEVAENLERKKREEEQGKQEAEV","length":382,"molWeight":43954,"crc64":"79F3CF17B5675600","md5":"DBACE8012A4B228822433C53E38CEFA4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"SUBUNIT":1,"INDUCTION":1},"countByFeatureType":{"Chain":1,"Domain":1,"Binding site":8},"uniParcId":"UPI0002020DC6"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q762H5","uniProtkbId":"MHPB_RHORH","entryAudit":{"firstPublicDate":"2008-05-20","lastAnnotationUpdateDate":"2025-06-18","lastSequenceUpdateDate":"2004-07-05","entryVersion":61,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01653"}],"value":"2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01653"}],"value":"1.13.11.16"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01653"}],"value":"3-carboxyethylcatechol 2,3-dioxygenase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01653"}],"value":"mhpB"},"synonyms":[{"value":"bphC3"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01653"}],"value":"Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-ketononatrienedioate, respectively"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-hydroxy-6-oxonona-2,4-dienedioate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23840"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:46951"},{"database":"ChEBI","id":"CHEBI:66887"}],"ecNumber":"1.13.11.16","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01653"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + O2 = (2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-trienedioate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:25054"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:58642"},{"database":"ChEBI","id":"CHEBI:66888"}],"ecNumber":"1.13.11.16","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01653"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Fe(2+)","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01653"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29033"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01653"}],"value":"Aromatic compound metabolism; 3-phenylpropanoate degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01653"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01653"}],"value":"Belongs to the LigB/MhpB extradiol dioxygenase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":316,"modifier":"EXACT"}},"description":"2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase","featureId":"PRO_0000337666"},{"type":"Active site","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01653"}]},{"type":"Active site","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01653"}]}],"keywords":[{"id":"KW-0058","category":"Biological process","name":"Aromatic hydrocarbons catabolism"},{"id":"KW-0223","category":"Molecular function","name":"Dioxygenase"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"}],"references":[{"referenceNumber":1,"citation":{"id":"15118304","citationType":"journal article","authors":["Taguchi K.","Motoyama M.","Kudo T."],"citationCrossReferences":[{"database":"PubMed","id":"15118304"},{"database":"DOI","id":"10.1271/bbb.68.787"}],"title":"Multiplicity of 2,3-dihydroxybiphenyl dioxygenase genes in the Gram-positive polychlorinated biphenyl degrading bacterium Rhodococcus rhodochrous K37.","publicationDate":"2004","journal":"Biosci. Biotechnol. Biochem.","firstPage":"787","lastPage":"795","volume":"68"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"K37","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB117721","properties":[{"key":"ProteinId","value":"BAD10895.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q762H5","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q762H5","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00714","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0047070","properties":[{"key":"GoTerm","value":"F:3-carboxyethylcatechol 2,3-dioxygenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008198","properties":[{"key":"GoTerm","value":"F:ferrous iron binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0019380","properties":[{"key":"GoTerm","value":"P:3-phenylpropionate catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd07365","properties":[{"key":"EntryName","value":"MhpB_like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.830.10","properties":[{"key":"EntryName","value":"LigB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01653","properties":[{"key":"EntryName","value":"MhpB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023789","properties":[{"key":"EntryName","value":"DHPP/DHXA_dioxygenase"}]},{"database":"InterPro","id":"IPR004183","properties":[{"key":"EntryName","value":"Xdiol_dOase_suB"}]},{"database":"NCBIfam","id":"NF009910","properties":[{"key":"EntryName","value":"PRK13370.1-4"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02900","properties":[{"key":"EntryName","value":"LigB"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53213","properties":[{"key":"EntryName","value":"LigB-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTQALLCMSHSPLLDHATPPAEVKSAVDDAFARARDFVEAFDPELVVNFGPDHFNGFFYDLMPPFCIGYRAHGTGDYDSFAGDLDVPEDVAADLAQFVLDHGSDVAISRHMEVDHGAVQPMEILHGGDAGARPILPVFVNSIARPFVPMSRVRAFGHAVGDFFAGTDKRVLFLGSGGLSHDPPVPQFATATASQREFLTSGRNPPPEARPARQARTIETARRFAAGEAEIMDLNPEWDRAFLDVCRSGRVEDFDRYTADEMDAAAGHSSHEVRTWVAAYSALRACGEYDVTYEFYRPIKEYIAGFAVTTAQLAGEA","length":316,"molWeight":34533,"crc64":"E3CD5EEABC8A294E","md5":"A455FC1F8D4E6CC6A9DA1BE0B9C80506"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":2},"uniParcId":"UPI000023BD58"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P29379","uniProtkbId":"NHB2_RHORH","entryAudit":{"firstPublicDate":"1992-12-01","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"1992-12-01","entryVersion":87,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"28644864"}],"value":"Low-molecular weight cobalt-containing nitrile hydratase subunit beta"},"shortNames":[{"value":"L-NHase"},{"value":"L-nitrilase"}]}},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1840499"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28644864"}],"value":"NHase catalyzes the hydration of various nitrile compounds to the corresponding amides (PubMed:1840499, PubMed:28644864). The alpha subunit functions as the catalytic subunit of the NHase complex while the beta subunit plays a structural/accessory role (PubMed:28644864)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1840499"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28644864"}],"value":"Component of the NHase complex, composed of two heterodimers of alpha and beta subunits"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P29379","intActId":"EBI-15729954"},"interactantTwo":{"uniProtKBAccession":"P29378","intActId":"EBI-15729943"},"numberOfExperiments":2,"organismDiffer":false}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1840499"}],"value":"By cobalt, cyclohexanecarboxamide and crotonamide"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Industrial production of acrylamide and nicotinamide is now being developed using some of these enzymes"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28644864"}],"value":"The complex exhibits higher thermostability than the high-molecular weight NHase complex, H-NHase"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the nitrile hydratase subunit beta family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"Low-molecular weight cobalt-containing nitrile hydratase subunit beta","featureId":"PRO_0000186833"},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"}],"references":[{"referenceNumber":1,"citation":{"id":"1840499","citationType":"journal article","authors":["Kobayashi M.","Nishiyama M.","Nagasawa T.","Horinouchi S.","Beppu T.","Yamada H."],"citationCrossReferences":[{"database":"PubMed","id":"1840499"},{"database":"DOI","id":"10.1016/0167-4781(91)90208-4"}],"title":"Cloning, nucleotide sequence and expression in Escherichia coli of two cobalt-containing nitrile hydratase genes from Rhodococcus rhodochrous J1.","publicationDate":"1991","journal":"Biochim. Biophys. Acta","firstPage":"23","lastPage":"33","volume":"1129"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 1-31; 95-129 AND 166-224","FUNCTION","SUBUNIT","INDUCTION BY COBALT; CYCLOHEXANECARBOXAMIDE AND CROTONAMIDE"],"referenceComments":[{"value":"J1","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"28644864","citationType":"journal article","authors":["Lan Y.","Zhang X.","Liu Z.","Zhou L.","Shen R.","Zhong X.","Cui W.","Zhou Z."],"citationCrossReferences":[{"database":"PubMed","id":"28644864"},{"database":"DOI","id":"10.1371/journal.pone.0179833"}],"title":"Overexpression and characterization of two types of nitrile hydratases from Rhodococcus rhodochrous J1.","publicationDate":"2017","journal":"PLoS ONE","firstPage":"e0179833","lastPage":"e0179833","volume":"12"},"referencePositions":["FUNCTION","SUBUNIT"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X64360","properties":[{"key":"ProteinId","value":"CAA45711.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"S19715","properties":[{"key":"EntryName","value":"S19715"}]},{"database":"RefSeq","id":"WP_088899669.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP027558.1"}]},{"database":"AlphaFoldDB","id":"P29379","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P29379","properties":[{"key":"Description","value":"-"}]},{"database":"DIP","id":"DIP-46300N","properties":[{"key":"Description","value":"-"}]},{"database":"IntAct","id":"P29379","properties":[{"key":"Interactions","value":"1"}]},{"database":"BRENDA","id":"4.2.1.84","properties":[{"key":"OrganismId","value":"5395"}]},{"database":"GO","id":"GO:0018822","properties":[{"key":"GoTerm","value":"F:nitrile hydratase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0046914","properties":[{"key":"GoTerm","value":"F:transition metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"2.30.30.50","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.472.20","properties":[{"key":"EntryName","value":"Nitrile hydratase, beta subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR049054","properties":[{"key":"EntryName","value":"CN_hydtase_beta-like_N"}]},{"database":"InterPro","id":"IPR042262","properties":[{"key":"EntryName","value":"CN_hydtase_beta_C"}]},{"database":"InterPro","id":"IPR024690","properties":[{"key":"EntryName","value":"CN_hydtase_beta_dom_C"}]},{"database":"InterPro","id":"IPR008990","properties":[{"key":"EntryName","value":"Elect_transpt_acc-like_dom_sf"}]},{"database":"InterPro","id":"IPR003168","properties":[{"key":"EntryName","value":"Nitrile_hydratase_bsu"}]},{"database":"NCBIfam","id":"TIGR03888","properties":[{"key":"EntryName","value":"nitrile_beta"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02211","properties":[{"key":"EntryName","value":"NHase_beta_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21006","properties":[{"key":"EntryName","value":"NHase_beta_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001427","properties":[{"key":"EntryName","value":"NHase_beta"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50090","properties":[{"key":"EntryName","value":"Electron transport accessory proteins"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDGIHDLGGRAGLGPIKPESDEPVFHSDWERSVLTMFPAMALAGAFNLDQFRGAMEQIPPHDYLTSQYYEHWMHAMIHHGIEAGIFDSDELDRRTQYYMDHPDDTTPTRQDPQLVETISQLITHGADYRRPTDTEAAFAVGDKVIVRSDASPNTHTRRAGYVRGRVGEVVATHGAYVFPDTNALGAGESPEHLYTVRFSATELWGEPAAPNVVNHIDVFEPYLLPA","length":226,"molWeight":25201,"crc64":"A790BCC67B319654","md5":"EF7CB54E72CD7A273473D5145AC416FB"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"INTERACTION":1,"INDUCTION":1,"BIOTECHNOLOGY":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Region":1},"uniParcId":"UPI000004FA97"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P84650","uniProtkbId":"AMID_RHORH","entryAudit":{"firstPublicDate":"2005-09-27","lastAnnotationUpdateDate":"2025-06-18","lastSequenceUpdateDate":"2005-09-27","entryVersion":46,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Enantioselective amidase"},"ecNumbers":[{"value":"3.5.1.4"}]}},"genes":[{"geneName":{"value":"amdA"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a monocarboxylic acid amide + H2O = a monocarboxylate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12020"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:35757"},{"database":"ChEBI","id":"CHEBI:83628"}],"ecNumber":"3.5.1.4","evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.1"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.1"}],"value":"Homooctamer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.1"}],"value":"By aromatic and aliphatic amides"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Belongs to the amidase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":517,"modifier":"EXACT"}},"description":"Enantioselective amidase","featureId":"PRO_0000105127"},{"type":"Active site","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P97612"}]},{"type":"Active site","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P97612"}]},{"type":"Active site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"Acyl-ester intermediate","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P97612"}]}],"keywords":[{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-ATICU1NV7ANQ","citationType":"submission","authors":["Pertsovich S.I.","Guranda D.T.","Svedas V.K."],"title":"New amidase from Rhodococcus rhodochrous possesses unusual substrate specificity.","publicationDate":"SEP-2005","submissionDatabase":"UniProtKB"},"referencePositions":["PROTEIN SEQUENCE","CATALYTIC ACTIVITY","SUBUNIT","INDUCTION"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.1"}],"value":"M8","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"AlphaFoldDB","id":"P84650","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P84650","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0004040","properties":[{"key":"GoTerm","value":"F:amidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"Gene3D","id":"3.90.1300.10","properties":[{"key":"EntryName","value":"Amidase signature (AS) domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000120","properties":[{"key":"EntryName","value":"Amidase"}]},{"database":"InterPro","id":"IPR020556","properties":[{"key":"EntryName","value":"Amidase_CS"}]},{"database":"InterPro","id":"IPR023631","properties":[{"key":"EntryName","value":"Amidase_dom"}]},{"database":"InterPro","id":"IPR036928","properties":[{"key":"EntryName","value":"AS_sf"}]},{"database":"NCBIfam","id":"NF005565","properties":[{"key":"EntryName","value":"PRK07235.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11895:SF170","properties":[{"key":"EntryName","value":"AMIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11895","properties":[{"key":"EntryName","value":"TRANSAMIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01425","properties":[{"key":"EntryName","value":"Amidase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF75304","properties":[{"key":"EntryName","value":"Amidase signature (AS) enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00571","properties":[{"key":"EntryName","value":"AMIDASES"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSSLTPPNSNQMSALNNHFFFGLTTPKLEEFAPALEATLAYAVTDERVYERTAPEPPDRSWTTPTAAENPLSAWYVTTSISYTDGGPLAGRTVAIKDNVTVAGVPMMNGSRVVEGFTPRYDATVLRRLLDAGATKAGKAVCEDLCFSGSSVTSHPQPVRNPWDESHGYKAGGSSSGSEALVASGHVDCAVGGDGGGSIRIPLACCGIVGCKPTHGLKPYTFPIERTIDHLGPMTRTVGDAAMMLTVLAGTDGLDPRQADHRIEPVDYLAALAEPAGLRVVVVTEGFDTPVQDAAVDDAVRAAILVLRSGCLTVEIVSIPIHLDAFAVWNVIATEGAAYQMLDGNYYGMNTGGFYDPELIIHFSRRRLEHGHQLSKTVKLVGMGGRYTSETGGGKYAAAARQLVREVRAAYDLALARYDVLVMPTLPYTATKIPITDIPLADYLDTALSMIINTAPFDVTGHPALCPVAGAVHGLPVGMMIIGKAHDDDATVLRVAAFEHAVGNYPVPPEAASTLATL","length":517,"molWeight":54735,"crc64":"10F75F7AF1AA40F5","md5":"AA4B0AD2A10A277E575E91F48ADF455E"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"INDUCTION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":3},"uniParcId":"UPI00005B2E14"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P96454","uniProtkbId":"NHLF_RHORH","entryAudit":{"firstPublicDate":"2014-10-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1997-05-01","entryVersion":58,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Cobalt transport protein NhlF"}}},"genes":[{"geneName":{"value":"nhlF"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10201093"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8990157"}],"value":"Mediates energy-dependent uptake of cobalt ions into the cell. Can also transport nickel ions, but cobalt is the preferred substrate"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8990157"}],"value":"Cobalt uptake is inhibited by uncouplers (CCCP and 3,5-di-tert-butyl-4-hydroxybenzylidenemalononitrile) and by the addition of excess nickel"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the NiCoT transporter (TC 2.A.52) family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":352,"modifier":"EXACT"}},"description":"Cobalt transport protein NhlF","featureId":"PRO_0000430351"},{"type":"Transmembrane","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":43,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":290,"modifier":"EXACT"},"end":{"value":310,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":323,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}],"keywords":[{"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"id":"KW-0170","category":"Ligand","name":"Cobalt"},{"id":"KW-0171","category":"Biological process","name":"Cobalt transport"},{"id":"KW-0406","category":"Biological process","name":"Ion transport"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0533","category":"Ligand","name":"Nickel"},{"id":"KW-0921","category":"Biological process","name":"Nickel transport"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"8990157","citationType":"journal article","authors":["Komeda H.","Kobayashi M.","Shimizu S."],"citationCrossReferences":[{"database":"PubMed","id":"8990157"},{"database":"DOI","id":"10.1073/pnas.94.1.36"}],"title":"A novel transporter involved in cobalt uptake.","publicationDate":"1997","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"36","lastPage":"41","volume":"94"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","ACTIVITY REGULATION"],"referenceComments":[{"value":"J1","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"10201093","citationType":"journal article","authors":["Degen O.","Kobayashi M.","Shimizu S.","Eitinger T."],"citationCrossReferences":[{"database":"PubMed","id":"10201093"},{"database":"DOI","id":"10.1007/s002030050691"}],"title":"Selective transport of divalent cations by transition metal permeases: the Alcaligenes eutrophus HoxN and the Rhodococcus rhodochrous NhlF.","publicationDate":"1999","journal":"Arch. Microbiol.","firstPage":"139","lastPage":"145","volume":"171"},"referencePositions":["FUNCTION AS A COBALT AND NICKEL IONS TRANSPORTER"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D83695","properties":[{"key":"ProteinId","value":"BAA12063.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"P96454","properties":[{"key":"Description","value":"-"}]},{"database":"TCDB","id":"2.A.52.1.2","properties":[{"key":"FamilyName","value":"the ni(2+)-co(2+) transporter (nicot) family"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0015099","properties":[{"key":"GoTerm","value":"F:nickel cation transmembrane transporter activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"InterPro","id":"IPR004688","properties":[{"key":"EntryName","value":"Ni/Co_transpt"}]},{"database":"InterPro","id":"IPR011541","properties":[{"key":"EntryName","value":"Ni/Co_transpt_high_affinity"}]},{"database":"NCBIfam","id":"TIGR00802","properties":[{"key":"EntryName","value":"nico"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31611","properties":[{"key":"EntryName","value":"HIGH-AFFINITY NICKEL TRANSPORT PROTEIN NIC1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31611:SF0","properties":[{"key":"EntryName","value":"HIGH-AFFINITY NICKEL TRANSPORT PROTEIN NIC1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03824","properties":[{"key":"EntryName","value":"NicO"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTSTTITPHHIGGAWTRTERRRLASVVGAIVILHVLGVALYLGYSGNPAAAGGLAGSGVLAYVLGVRHAFDADHIAAIDDTTRLMLLRGRRPVGVGFFFAMGHSTVVVVLALVVALGASALTTTELEGVQEIGGLVATVVAVTFLSIVAGLNSVVLRNLLCLSRQVRAGSDITGDLESRLSERGLFTRLLGNRWRGLVRSSWHMYPVGLLMGLGLETASEVTLLTLTASAATGGTLSIAAVLSLPLLFAAGMSTFDTADSLFMTRAYSWSYQDPQRRLNFNIATTGATVVIGLFVAGIYVCALLAHLPMFAALSPIGDISENFEFLGYAVAAAFILTWTGALLFNHLKPQRN","length":352,"molWeight":37187,"crc64":"5512BAEA15C6F979","md5":"892B564139F455E68B6557F0C8C1DF26"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"ACTIVITY REGULATION":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Transmembrane":8},"uniParcId":"UPI00000B4660"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P31718","uniProtkbId":"CPXX_RHORH","entryAudit":{"firstPublicDate":"1993-07-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1993-07-01","entryVersion":51,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Cytochrome P450-RR1"},"shortNames":[{"value":"Cytochrome P450RR1"}],"ecNumbers":[{"value":"1.14.-.-"}]},"alternativeNames":[{"fullName":{"value":"Cytochrome P450-RRI"}}],"flag":"Fragment"},"comments":[{"texts":[{"value":"P450-RRI catalyzes the O-dealkylation of 2-ethoxyphenol and 2-methoxyphenol to produce catechol. The cytochrome binds other ortho-substituted phenols, including 2-ethoxyphenol, 2-methylphenol and 2-chlorophenol"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"heme","evidences":[{"evidenceCode":"ECO:0000250"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}]},{"texts":[{"value":"By 2-ethoxyphenol"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the cytochrome P450 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":20,"modifier":"OUTSIDE"}},"description":"Cytochrome P450-RR1","featureId":"PRO_0000052232"},{"type":"Non-terminal residue","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":""}],"keywords":[{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0349","category":"Ligand","name":"Heme"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0503","category":"Molecular function","name":"Monooxygenase"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"}],"references":[{"referenceNumber":1,"citation":{"id":"8477696","citationType":"journal article","authors":["Eltis L.D.","Karlson U.","Timmis K.N."],"citationCrossReferences":[{"database":"PubMed","id":"8477696"},{"database":"DOI","id":"10.1111/j.1432-1033.1993.tb17750.x"}],"title":"Purification and characterization of cytochrome P450RR1 from Rhodococcus rhodochrous.","publicationDate":"1993","journal":"Eur. J. Biochem.","firstPage":"211","lastPage":"216","volume":"213"},"referencePositions":["PROTEIN SEQUENCE"],"referenceComments":[{"value":"116","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"AlphaFoldDB","id":"P31718","properties":[{"key":"Description","value":"-"}]}],"sequence":{"value":"TSTLSWLDEITMEELERNPY","length":20,"molWeight":2428,"crc64":"BCA81586D8DD1496","md5":"B7FBDC598F5D9E3C57F7A3E3F324A3D6"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"INDUCTION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Non-terminal residue":1},"uniParcId":"UPI0000128343"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q53034","uniProtkbId":"CATA_RHORH","entryAudit":{"firstPublicDate":"1998-12-15","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1996-11-01","entryVersion":83,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"Metapyrocatechase"},"shortNames":[{"value":"MPC"}],"ecNumbers":[{"value":"1.13.11.2"}]},"alternativeNames":[{"fullName":{"value":"CatO2ase"}},{"fullName":{"value":"Catechol 2,3-dioxygenase"}}]},"genes":[{"geneName":{"value":"catA"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"catechol + O2 = (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17337"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:18135"},{"database":"ChEBI","id":"CHEBI:71198"}],"ecNumber":"1.13.11.2"}},{"commentType":"COFACTOR","cofactors":[{"name":"Fe(2+)","evidences":[{"evidenceCode":"ECO:0000250"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29033"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the extradiol ring-cleavage dioxygenase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"Metapyrocatechase","featureId":"PRO_0000085031"},{"type":"Domain","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"VOC 1","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01163"}]},{"type":"Domain","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":263,"modifier":"EXACT"}},"description":"VOC 2","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01163"}]},{"type":"Binding site","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":209,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":259,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}}],"keywords":[{"id":"KW-0058","category":"Biological process","name":"Aromatic hydrocarbons catabolism"},{"id":"KW-0223","category":"Molecular function","name":"Dioxygenase"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0677","category":"Domain","name":"Repeat"}],"references":[{"referenceNumber":1,"citation":{"id":"9579069","citationType":"journal article","authors":["Kulakov L.A.","Delcroix V.A.","Larkin M.J.","Ksenzenko V.N.","Kulakova A.N."],"citationCrossReferences":[{"database":"PubMed","id":"9579069"},{"database":"DOI","id":"10.1099/00221287-144-4-955"}],"title":"Cloning of new Rhodococcus extradiol dioxygenase genes and study of their distribution in different Rhodococcus strains.","publicationDate":"1998","journal":"Microbiology","firstPage":"955","lastPage":"963","volume":"144"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"NCIMB 13064 / Isolate P200","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"L77225","properties":[{"key":"ProteinId","value":"AAC18907.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q53034","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q53034","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0018577","properties":[{"key":"GoTerm","value":"F:catechol 2,3-dioxygenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0008198","properties":[{"key":"GoTerm","value":"F:ferrous iron binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0042178","properties":[{"key":"GoTerm","value":"P:xenobiotic catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd07237","properties":[{"key":"EntryName","value":"BphC1-RGP6_C_like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd07252","properties":[{"key":"EntryName","value":"BphC1-RGP6_N_like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.180.10","properties":[{"key":"EntryName","value":"2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR017626","properties":[{"key":"EntryName","value":"DiOHbiphenyl_dOase"}]},{"database":"InterPro","id":"IPR029068","properties":[{"key":"EntryName","value":"Glyas_Bleomycin-R_OHBP_Dase"}]},{"database":"InterPro","id":"IPR004360","properties":[{"key":"EntryName","value":"Glyas_Fos-R_dOase_dom"}]},{"database":"InterPro","id":"IPR037523","properties":[{"key":"EntryName","value":"VOC_core"}]},{"database":"InterPro","id":"IPR000486","properties":[{"key":"EntryName","value":"Xdiol_ring_cleave_dOase_1/2"}]},{"database":"NCBIfam","id":"TIGR03213","properties":[{"key":"EntryName","value":"23dbph12diox"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21366:SF14","properties":[{"key":"EntryName","value":"GLYOXALASE DOMAIN-CONTAINING PROTEIN 5"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21366","properties":[{"key":"EntryName","value":"GLYOXALASE FAMILY PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22632","properties":[{"key":"EntryName","value":"BphC_D1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00903","properties":[{"key":"EntryName","value":"Glyoxalase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54593","properties":[{"key":"EntryName","value":"Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00082","properties":[{"key":"EntryName","value":"EXTRADIOL_DIOXYGENAS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51819","properties":[{"key":"EntryName","value":"VOC"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MALVTGIGYIGIGVSDLPAWEEFAETIGFQIRERGEDGTLYLRMDKAHHRVAVHPTGEDDLTYVGWQVADENGFDELERTLRAAGVPVEMAGEDDAELRGVARLMRFEDPSGIKSEAYYGLVSEPEVPYVSPYAVDFVTEDQGFGHIVVMVDDYDETMRFYREVLGLQTSDLVKVGAGGVQTRMAFMRCNPRQHSLAFWAGDSTTRLNHFMLQTQTLDQTGMTLDRCFHGGIPATNLGRHVNDYAVSFYITTPSGFMIEYGWGVREVVSDYPVDKYRSVSIWGHRNLDGIHYTQALPPEAAESPAEQHLVEEPVAAAV","length":318,"molWeight":35438,"crc64":"ED9EB5EAA9659058","md5":"C26E3394D2CF828642A18442D82C2EFF"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":2,"Binding site":3},"uniParcId":"UPI000012707D"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q02068","uniProtkbId":"NRL1_RHORH","entryAudit":{"firstPublicDate":"1993-10-01","lastAnnotationUpdateDate":"2025-02-05","lastSequenceUpdateDate":"1993-10-01","entryVersion":82,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Aliphatic nitrilase"},"ecNumbers":[{"value":"3.5.5.7"}]}},"comments":[{"texts":[{"value":"Acts on aliphatic nitriles such as acrylonitrile, crotononitrile and glutaronitrile"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an aliphatic nitrile + 2 H2O = a carboxylate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46188"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29067"},{"database":"ChEBI","id":"CHEBI:80291"}],"ecNumber":"3.5.5.7"}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the carbon-nitrogen hydrolase superfamily. Nitrilase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":383,"modifier":"EXACT"}},"description":"Aliphatic nitrilase","featureId":"PRO_0000204045"},{"type":"Domain","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"CN hydrolase","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00054"}]},{"type":"Region","location":{"start":{"value":359,"modifier":"EXACT"},"end":{"value":383,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":53,"modifier":"EXACT"},"end":{"value":53,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00054"}]},{"type":"Active site","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":136,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00054"}]},{"type":"Active site","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00054"},{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU10105"}]},{"type":"Mutagenesis","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"100% loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1390687"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["S","A"]}}],"keywords":[{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"}],"references":[{"referenceNumber":1,"citation":{"id":"1390687","citationType":"journal article","authors":["Kobayashi M.","Yanaka N.","Nagasawa T.","Yamada H."],"citationCrossReferences":[{"database":"PubMed","id":"1390687"},{"database":"DOI","id":"10.1021/bi00152a042"}],"title":"Primary structure of an aliphatic nitrile-degrading enzyme, aliphatic nitrilase, from Rhodococcus rhodochrous K22 and expression of its gene and identification of its active site residue.","publicationDate":"1992","journal":"Biochemistry","firstPage":"9000","lastPage":"9007","volume":"31"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PARTIAL PROTEIN SEQUENCE","MUTAGENESIS OF CYS-170"],"referenceComments":[{"value":"K22","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D12583","properties":[{"key":"ProteinId","value":"BAA02127.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"A43470","properties":[{"key":"EntryName","value":"A43470"}]},{"database":"AlphaFoldDB","id":"Q02068","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q02068","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ag:BAA02127","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"3.5.5.7","properties":[{"key":"OrganismId","value":"5395"}]},{"database":"GO","id":"GO:0018762","properties":[{"key":"GoTerm","value":"F:aliphatic nitrilase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"CDD","id":"cd07564","properties":[{"key":"EntryName","value":"nitrilases_CHs"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.60.110.10","properties":[{"key":"EntryName","value":"Carbon-nitrogen hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003010","properties":[{"key":"EntryName","value":"C-N_Hydrolase"}]},{"database":"InterPro","id":"IPR036526","properties":[{"key":"EntryName","value":"C-N_Hydrolase_sf"}]},{"database":"InterPro","id":"IPR000132","properties":[{"key":"EntryName","value":"Nitrilase/CN_hydratase_CS"}]},{"database":"InterPro","id":"IPR044149","properties":[{"key":"EntryName","value":"Nitrilases_CHs"}]},{"database":"PANTHER","id":"PTHR46044:SF14","properties":[{"key":"EntryName","value":"ARYLACETONITRILASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46044","properties":[{"key":"EntryName","value":"NITRILASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00795","properties":[{"key":"EntryName","value":"CN_hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56317","properties":[{"key":"EntryName","value":"Carbon-nitrogen hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50263","properties":[{"key":"EntryName","value":"CN_HYDROLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00920","properties":[{"key":"EntryName","value":"NITRIL_CHT_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00921","properties":[{"key":"EntryName","value":"NITRIL_CHT_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSSNPELKYTGKVKVATVQAEPVILDADATIDKAIGFIEEAAKNGAEFLAFPEVWIPGYPYWAWIGDVKWAVSDFIPKYHENSLTLGDDRMRRLQLAARQNNIALVMGYSEKDGASRYLSQVFIDQNGDIVANRRKLKPTHVERTIYGEGNGTDFLTHDFGFGRVGGLNCWEHFQPLSKYMMYSLNEQIHVASWPAMFALTPDVHQLSVEANDTVTRSYAIEGQTFVLASTHVIGKATQDLFAGDDDAKRALLPLGQGWARIYGPDGKSLAEPLPEDAEGLLYAELDLEQIILAKAAADPAGHYSRPDVLSLKIDTRNHTPVQYITADGRTSLNSNSRVENYRLHQLADIEKYENAEAATLPLDAPAPAPAPEQKSGRAKAEA","length":383,"molWeight":42276,"crc64":"BA8EE5572B8DA17B","md5":"1843A1CD4C6BED89B27B9EDF6C359B43"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":1,"Region":1,"Active site":3,"Mutagenesis":1},"uniParcId":"UPI0000130516"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0AA46WYF7","uniProtkbId":"A0AA46WYF7_RHORH","entryAudit":{"firstPublicDate":"2024-01-24","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2024-01-24","entryVersion":13,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UZF45676.1"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00021623"}],"value":"Phosphoenolpyruvate synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011996"}],"value":"2.7.9.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00033470"}],"value":"Pyruvate, water dikinase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UZF45676.1"}],"value":"KUM34_002985"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002988"}],"value":"Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"pyruvate + ATP + H2O = phosphoenolpyruvate + AMP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11364"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58702"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"2.7.9.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047700"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004742"}],"value":"Carbohydrate biosynthesis; gluconeogenesis"}],"commentType":"PATHWAY"}],"features":[{"type":"Domain","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"Pyruvate phosphate dikinase AMP/ATP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01326"}]},{"type":"Region","location":{"start":{"value":335,"modifier":"EXACT"},"end":{"value":367,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":335,"modifier":"EXACT"},"end":{"value":345,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9GOJ"}],"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"34566938","citationType":"journal article","authors":["Navas L.E.","Dexter G.","Liu J.","Levy-Booth D.","Cho M.","Jang S.K.","Mansfield S.D.","Renneckar S.","Mohn W.W.","Eltis L.D."],"citationCrossReferences":[{"database":"PubMed","id":"34566938"}],"title":"Bacterial Transformation of Aromatic Monomers in Softwood Black Liquor.","publicationDate":"2021","journal":"Front. Microbiol.","firstPage":"735000","lastPage":"735000","volume":"12"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UZF45676.1"}],"value":"GD02","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UZF45676.1"}]},{"referenceNumber":2,"citation":{"id":"40345584","citationType":"journal article","authors":["Dexter G.N.","Grigg J.C.","Zahn M.","Wheatley E.J.","Lian J.","Mohn W.W.","Eltis L.D."],"citationCrossReferences":[{"database":"PubMed","id":"40345584"},{"database":"DOI","id":"10.1016/j.jbc.2025.110210"}],"title":"Characterization of a two-component kinase that initiates the bacterial catabolism of hydroxyphenylethanones.","publicationDate":"2025","journal":"J. Biol. Chem.","firstPage":"110210","lastPage":"110210","volume":"301"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS)"],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"9GOJ"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP083974","properties":[{"key":"ProteinId","value":"UZF45676.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_229581529.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP083974.1"}]},{"database":"PDB","id":"9GOJ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.80 A"},{"key":"Chains","value":"A=1-367"}]},{"database":"AlphaFoldDB","id":"A0AA46WYF7","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"A0AA46WYF7","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008986","properties":[{"key":"GoTerm","value":"F:pyruvate, water dikinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"Gene3D","id":"3.30.1490.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, A domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013815","properties":[{"key":"EntryName","value":"ATP_grasp_subdomain_1"}]},{"database":"InterPro","id":"IPR006319","properties":[{"key":"EntryName","value":"PEP_synth"}]},{"database":"InterPro","id":"IPR002192","properties":[{"key":"EntryName","value":"PPDK_AMP/ATP-bd"}]},{"database":"PANTHER","id":"PTHR43030","properties":[{"key":"EntryName","value":"PHOSPHOENOLPYRUVATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43030:SF1","properties":[{"key":"EntryName","value":"PHOSPHOENOLPYRUVATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01326","properties":[{"key":"EntryName","value":"PPDK_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGKYTKKFNEVRSTDRPLVGGKCASLGEMVQAGLPVPDGFAVTIDAYEDFRDDSDLRAELRSLVFGVDPDSSKSLQDAHDQAVALVLGRNLPAAIEDEIREAYLTLSRETARRRGTGDTDRIPVAVRSSSVDEDGDAASFAGQQETYLWVVGADDVIAKVRECWASLYTPQAIAYRAGMSETDAAEASKISVAVQLMADADVAGVMFTVSPRTGDRSVIAINASWGLGQSVVSGEVTPDEYWLSKIGPTLTSSRIASKEHEYVPAPDGTGVIFREVEQARREVSCLSDSELMQLAEIGLRVEEHYGCPQDIEWALEHDSDGTSRVMLLQSRPETNWKKRKEEKSKRTSSATSNLLGFVSAAAKGQTR","length":367,"molWeight":39932,"crc64":"A819533BBBE8547A","md5":"683DEAF2D567A28DE4592CCE6D998ADB"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1},"uniParcId":"UPI001E44DA29"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A3KCV0","uniProtkbId":"A3KCV0_RHORH","entryAudit":{"firstPublicDate":"2007-04-03","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-04-03","entryVersion":36,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48118.1"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003567"}],"value":"ATP-dependent Clp protease proteolytic subunit"}},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48118.1"}],"value":"orf18"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007039"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003567"}],"value":"Belongs to the peptidase S14 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48118.1"}]}],"references":[{"referenceNumber":1,"citation":{"id":"15118304","citationType":"journal article","authors":["Taguchi K.","Motoyama M.","Kudo T."],"citationCrossReferences":[{"database":"PubMed","id":"15118304"},{"database":"DOI","id":"10.1271/bbb.68.787"}],"title":"Multiplicity of 2,3-dihydroxybiphenyl dioxygenase genes in the Gram-positive polychlorinated biphenyl degrading bacterium Rhodococcus rhodochrous K37.","publicationDate":"2004","journal":"Biosci. Biotechnol. Biochem.","firstPage":"787","lastPage":"795","volume":"68"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48118.1"}],"value":"K37","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48118.1"}]},{"referenceNumber":2,"citation":{"id":"CI-CNEU8KQIIUBOQ","citationType":"submission","authors":["Taguchi K.","Motoyama M.","Kudo T."],"title":"Several meta-cleavage enzyme genes induced by steroid from Gram-positive bacterium Rhodococcus rhodochrous K37.","publicationDate":"SEP-2006","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48118.1"}],"value":"K37","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48118.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB271915","properties":[{"key":"ProteinId","value":"BAF48118.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A3KCV0","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009368","properties":[{"key":"GoTerm","value":"C:endopeptidase Clp complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004176","properties":[{"key":"GoTerm","value":"F:ATP-dependent peptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0051117","properties":[{"key":"GoTerm","value":"F:ATPase binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006515","properties":[{"key":"GoTerm","value":"P:protein quality control for misfolded or incompletely synthesized proteins"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.90.226.10","properties":[{"key":"EntryName","value":"2-enoyl-CoA Hydratase, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001907","properties":[{"key":"EntryName","value":"ClpP"}]},{"database":"InterPro","id":"IPR029045","properties":[{"key":"EntryName","value":"ClpP/crotonase-like_dom_sf"}]},{"database":"InterPro","id":"IPR023562","properties":[{"key":"EntryName","value":"ClpP/TepA"}]},{"database":"PANTHER","id":"PTHR10381","properties":[{"key":"EntryName","value":"ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10381:SF11","properties":[{"key":"EntryName","value":"ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00574","properties":[{"key":"EntryName","value":"CLP_protease"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00127","properties":[{"key":"EntryName","value":"CLPPROTEASEP"}]},{"database":"SUPFAM","id":"SSF52096","properties":[{"key":"EntryName","value":"ClpP/crotonase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"LWLCDVDADLEVTLTLLDVLDLMGVEIHAICLGELVGAGVALLTAADRRDSGVHTVFHLREPRTRYSGYAADAAAYTERQQRHLQTLHERLAHICGRSVDEIAADMRNQRILTAEQARDYGLIDTVTESTPGP","length":133,"molWeight":14681,"crc64":"FE3CC1FB71BB1872","md5":"F004F9021B6671D80CA66A9F92E2809F"},"extraAttributes":{"countByCommentType":{"SIMILARITY":1},"countByFeatureType":{"Non-terminal residue":1},"uniParcId":"UPI0000F35438"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A3KCV1","uniProtkbId":"A3KCV1_RHORH","entryAudit":{"firstPublicDate":"2007-04-03","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2007-04-03","entryVersion":90,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48119.1"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"4: Predicted","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48119.1"}],"value":"Uncharacterized protein orf17"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48119.1"}],"value":"orf17"}}],"features":[{"type":"Domain","location":{"start":{"value":25,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"Response regulatory","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50110"}]},{"type":"Domain","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"OmpR/PhoB-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51755"}]},{"type":"DNA binding","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"OmpR/PhoB-type","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01091"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Modified residue","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"4-aspartylphosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00169"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01091"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00169"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023163"}],"id":"KW-0804","category":"Biological process","name":"Transcription"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023015"}],"id":"KW-0805","category":"Biological process","name":"Transcription regulation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023012"}],"id":"KW-0902","category":"Biological process","name":"Two-component regulatory system"}],"references":[{"referenceNumber":1,"citation":{"id":"15118304","citationType":"journal article","authors":["Taguchi K.","Motoyama M.","Kudo T."],"citationCrossReferences":[{"database":"PubMed","id":"15118304"},{"database":"DOI","id":"10.1271/bbb.68.787"}],"title":"Multiplicity of 2,3-dihydroxybiphenyl dioxygenase genes in the Gram-positive polychlorinated biphenyl degrading bacterium Rhodococcus rhodochrous K37.","publicationDate":"2004","journal":"Biosci. Biotechnol. Biochem.","firstPage":"787","lastPage":"795","volume":"68"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48119.1"}],"value":"K37","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48119.1"}]},{"referenceNumber":2,"citation":{"id":"CI-CNEU8KQIIUBOQ","citationType":"submission","authors":["Taguchi K.","Motoyama M.","Kudo T."],"title":"Several meta-cleavage enzyme genes induced by steroid from Gram-positive bacterium Rhodococcus rhodochrous K37.","publicationDate":"SEP-2006","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48119.1"}],"value":"K37","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48119.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB271915","properties":[{"key":"ProteinId","value":"BAF48119.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A3KCV1","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0032993","properties":[{"key":"GoTerm","value":"C:protein-DNA complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000156","properties":[{"key":"GoTerm","value":"F:phosphorelay response regulator activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000976","properties":[{"key":"GoTerm","value":"F:transcription cis-regulatory region binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006355","properties":[{"key":"GoTerm","value":"P:regulation of DNA-templated transcription"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00383","properties":[{"key":"EntryName","value":"trans_reg_C"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.10.10:FF:000018","properties":[{"key":"EntryName","value":"DNA-binding response regulator ResD"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2300","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.250.690","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.10","properties":[{"key":"EntryName","value":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011006","properties":[{"key":"EntryName","value":"CheY-like_sf"}]},{"database":"InterPro","id":"IPR001867","properties":[{"key":"EntryName","value":"OmpR/PhoB-type_DNA-bd"}]},{"database":"InterPro","id":"IPR016032","properties":[{"key":"EntryName","value":"Sig_transdc_resp-reg_C-effctor"}]},{"database":"InterPro","id":"IPR001789","properties":[{"key":"EntryName","value":"Sig_transdc_resp-reg_receiver"}]},{"database":"InterPro","id":"IPR039420","properties":[{"key":"EntryName","value":"WalR-like"}]},{"database":"InterPro","id":"IPR036388","properties":[{"key":"EntryName","value":"WH-like_DNA-bd_sf"}]},{"database":"PANTHER","id":"PTHR48111:SF4","properties":[{"key":"EntryName","value":"DNA-BINDING DUAL TRANSCRIPTIONAL REGULATOR OMPR"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48111","properties":[{"key":"EntryName","value":"REGULATOR OF RPOS"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00072","properties":[{"key":"EntryName","value":"Response_reg"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00486","properties":[{"key":"EntryName","value":"Trans_reg_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00448","properties":[{"key":"EntryName","value":"REC"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00862","properties":[{"key":"EntryName","value":"Trans_reg_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF46894","properties":[{"key":"EntryName","value":"C-terminal effector domain of the bipartite response regulators"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52172","properties":[{"key":"EntryName","value":"CheY-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51755","properties":[{"key":"EntryName","value":"OMPR_PHOB"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50110","properties":[{"key":"EntryName","value":"RESPONSE_REGULATORY"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MASTSHTSVPNSDASPGSRPPAGLRAMVVEDEAALANLIGSYLERDGFEATITGDGAEAIALARRIDPDVLVLDLGLPSLDGVEVCRQLRTFSDAYVVMLTARTEELDTLIGLSVGADDYMTKPFGPRELIARIQAMMRRPRTTDTARSRQIRTFGDLSIDVEGREVTVDGVPVSLTRTEFDVLAALSQDPGIVITRAQLIGAVWGPNWVGDEHLVDVHIGHLRRKLGDDATRGRYVRTVRGVGYRMGTGR","length":251,"molWeight":27213,"crc64":"3D5F1B09BF3A974A","md5":"FA67FB2A23A39788ACB22BD25D8B4113"},"extraAttributes":{"countByFeatureType":{"Domain":2,"DNA binding":1,"Region":1,"Compositional bias":1,"Modified residue":1},"uniParcId":"UPI0000F35439"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A3KCV2","uniProtkbId":"A3KCV2_RHORH","entryAudit":{"firstPublicDate":"2007-04-03","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-04-03","entryVersion":86,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48120.1"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"4: Predicted","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012438"}],"value":"histidine kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012438"}],"value":"2.7.13.3"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48120.1"}],"value":"orf16"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.","ecNumber":"2.7.13.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000085"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004236"}],"value":"Cell membrane","id":"SL-0039"}}]}],"features":[{"type":"Transmembrane","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"HAMP","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50885"}]},{"type":"Domain","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"Histidine kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50109"}]},{"type":"Coiled coil","location":{"start":{"value":137,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Modified residue","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"Phosphohistidine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00107"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00107"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00107"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00107"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023012"}],"id":"KW-0902","category":"Biological process","name":"Two-component regulatory system"}],"references":[{"referenceNumber":1,"citation":{"id":"15118304","citationType":"journal article","authors":["Taguchi K.","Motoyama M.","Kudo T."],"citationCrossReferences":[{"database":"PubMed","id":"15118304"},{"database":"DOI","id":"10.1271/bbb.68.787"}],"title":"Multiplicity of 2,3-dihydroxybiphenyl dioxygenase genes in the Gram-positive polychlorinated biphenyl degrading bacterium Rhodococcus rhodochrous K37.","publicationDate":"2004","journal":"Biosci. Biotechnol. Biochem.","firstPage":"787","lastPage":"795","volume":"68"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48120.1"}],"value":"K37","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48120.1"}]},{"referenceNumber":2,"citation":{"id":"CI-CNEU8KQIIUBOQ","citationType":"submission","authors":["Taguchi K.","Motoyama M.","Kudo T."],"title":"Several meta-cleavage enzyme genes induced by steroid from Gram-positive bacterium Rhodococcus rhodochrous K37.","publicationDate":"SEP-2006","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48120.1"}],"value":"K37","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48120.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB271915","properties":[{"key":"ProteinId","value":"BAF48120.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A3KCV2","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000155","properties":[{"key":"GoTerm","value":"F:phosphorelay sensor kinase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd06225","properties":[{"key":"EntryName","value":"HAMP"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00082","properties":[{"key":"EntryName","value":"HisKA"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.565.10:FF:000006","properties":[{"key":"EntryName","value":"Sensor histidine kinase WalK"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.287.130","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.340.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.565.10","properties":[{"key":"EntryName","value":"Histidine kinase-like ATPase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003660","properties":[{"key":"EntryName","value":"HAMP_dom"}]},{"database":"InterPro","id":"IPR036890","properties":[{"key":"EntryName","value":"HATPase_C_sf"}]},{"database":"InterPro","id":"IPR003594","properties":[{"key":"EntryName","value":"HATPase_dom"}]},{"database":"InterPro","id":"IPR005467","properties":[{"key":"EntryName","value":"His_kinase_dom"}]},{"database":"InterPro","id":"IPR003661","properties":[{"key":"EntryName","value":"HisK_dim/P_dom"}]},{"database":"InterPro","id":"IPR036097","properties":[{"key":"EntryName","value":"HisK_dim/P_sf"}]},{"database":"InterPro","id":"IPR004358","properties":[{"key":"EntryName","value":"Sig_transdc_His_kin-like_C"}]},{"database":"InterPro","id":"IPR050428","properties":[{"key":"EntryName","value":"TCS_sensor_his_kinase"}]},{"database":"PANTHER","id":"PTHR45436:SF5","properties":[{"key":"EntryName","value":"SENSOR HISTIDINE KINASE TRCS"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45436","properties":[{"key":"EntryName","value":"SENSOR HISTIDINE KINASE YKOH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00672","properties":[{"key":"EntryName","value":"HAMP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02518","properties":[{"key":"EntryName","value":"HATPase_c"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00512","properties":[{"key":"EntryName","value":"HisKA"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00344","properties":[{"key":"EntryName","value":"BCTRLSENSOR"}]},{"database":"SMART","id":"SM00304","properties":[{"key":"EntryName","value":"HAMP"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00387","properties":[{"key":"EntryName","value":"HATPase_c"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00388","properties":[{"key":"EntryName","value":"HisKA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55874","properties":[{"key":"EntryName","value":"ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF158472","properties":[{"key":"EntryName","value":"HAMP domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47384","properties":[{"key":"EntryName","value":"Homodimeric domain of signal transducing histidine kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50885","properties":[{"key":"EntryName","value":"HAMP"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50109","properties":[{"key":"EntryName","value":"HIS_KIN"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNTARAEHESRPKRGLAGFSFGTRLLVALSVVVVGCAVSAWLVASALAPSIFRDHLGQAGIDHDSNEAAHVEEAFTWAIVLAWGLAVAIAVLLALVVSWYLTRRVQRSITAVTTSAAQIADGHYDTRVHSHGLGREFDELAVSVNELARRLEATENTRSRMLADLGHEMRTPVTTLDSYLEALDDGVRTFDDDTRQVLRDATNRLERLAQDITAVSHAEEHLTRIRPTSTATGALVTSAVHAAREQFENKGVTLDARLEDSAAVTVDPDRLGQVLGNLLDNALRHTPAGGAVTVTSRSGEHGHAQIIIADTGDGLAHDELDHLFDRFYRVDTARDRGHGGSGIGLTIARALVTAHGGRISAYSDGPGRGARFTVELPADRA","length":381,"molWeight":40943,"crc64":"9A571EC50F13D0F8","md5":"9231FB2558C3D5B988B2258923DE8D02"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"SUBCELLULAR LOCATION":1},"countByFeatureType":{"Transmembrane":2,"Domain":2,"Coiled coil":1,"Modified residue":1},"uniParcId":"UPI0000F3543A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A3KCY0","uniProtkbId":"A3KCY0_RHORH","entryAudit":{"firstPublicDate":"2007-04-03","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2007-04-03","entryVersion":58,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48487.1"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00039316"}],"value":"UvrABC system protein A"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00042156"}],"value":"Excinuclease ABC subunit A"}}],"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48487.1"}],"value":"orf812"}}],"comments":[{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00038000"}],"value":"Belongs to the ABC transporter superfamily. UvrA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00434"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"ABC transporter","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50893"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48487.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00434"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022769"}],"id":"KW-0228","category":"Biological process","name":"DNA excision"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022881"}],"id":"KW-0267","category":"Molecular function","name":"Excision nuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00434"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"}],"id":"KW-0677","category":"Domain","name":"Repeat"}],"references":[{"referenceNumber":1,"citation":{"id":"15118304","citationType":"journal article","authors":["Taguchi K.","Motoyama M.","Kudo T."],"citationCrossReferences":[{"database":"PubMed","id":"15118304"},{"database":"DOI","id":"10.1271/bbb.68.787"}],"title":"Multiplicity of 2,3-dihydroxybiphenyl dioxygenase genes in the Gram-positive polychlorinated biphenyl degrading bacterium Rhodococcus rhodochrous K37.","publicationDate":"2004","journal":"Biosci. Biotechnol. Biochem.","firstPage":"787","lastPage":"795","volume":"68"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48487.1"}],"value":"K37","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48487.1"}]},{"referenceNumber":2,"citation":{"id":"17485846","citationType":"journal article","authors":["Taguchi K.","Motoyama M.","Iida T.","Kudo T."],"citationCrossReferences":[{"database":"PubMed","id":"17485846"},{"database":"DOI","id":"10.1271/bbb.60551"}],"title":"Polychlorinated biphenyl/biphenyl degrading gene clusters in Rhodococcus sp. K37, HA99, and TA431 are different from well-known bph gene clusters of Rhodococci.","publicationDate":"2007","journal":"Biosci. Biotechnol. Biochem.","firstPage":"1136","lastPage":"1144","volume":"71"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48487.1"}],"value":"K37","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48487.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB272984","properties":[{"key":"ProteinId","value":"BAF48487.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A3KCY0","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"1.20.1580.10","properties":[{"key":"EntryName","value":"ABC transporter ATPase like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003439","properties":[{"key":"EntryName","value":"ABC_transporter-like_ATP-bd"}]},{"database":"InterPro","id":"IPR017871","properties":[{"key":"EntryName","value":"ABC_transporter-like_CS"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"PANTHER","id":"PTHR43152:SF1","properties":[{"key":"EntryName","value":"UVRA PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43152","properties":[{"key":"EntryName","value":"UVRABC SYSTEM PROTEIN A"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00211","properties":[{"key":"EntryName","value":"ABC_TRANSPORTER_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50893","properties":[{"key":"EntryName","value":"ABC_TRANSPORTER_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"GRIEGTLGGLRRVVAIDQRPIGRTPRSNVATYTGMFDHIRKLFAATPAAKKRNYKPGRFSFNVAGGRCPTCEGEGFVMIELLFLPSVYSPCPDCNGTRYTQSTLEITWRDRNIADVLAMSIDEAHAFFTSENDVLRSLTVLREVGLGYLRLGQPATELSGGEAQRVKLASELQRAQRGDTLYILDEPTAGLHPSDSDRLLAHAQGLVDADNTVVMVELDMRVVAQADHVIDLGPGAGADGGRIVATGSPEQVAATADSATAPYLRAALENTGAGTTQH","length":278,"molWeight":29809,"crc64":"24575331E7CFAFFB","md5":"27A0E95C246D0FDD1A6E7B48EBE82FD7"},"extraAttributes":{"countByCommentType":{"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Non-terminal residue":1},"uniParcId":"UPI0000F535ED"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A3KCY4","uniProtkbId":"A3KCY4_RHORH","entryAudit":{"firstPublicDate":"2007-04-03","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2007-04-03","entryVersion":73,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Rhodococcus rhodochrous","taxonId":1829,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48491.1"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Rhodococcus"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48491.1"}],"value":"Biphenyl dioxygenase large subunit"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48491.1"}],"value":"bphA1"}}],"comments":[{"commentType":"COFACTOR","cofactors":[{"name":"Fe cation","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001962"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:24875"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"[2Fe-2S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00628"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:190135"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00628"}],"value":"Binds 1 [2Fe-2S] cluster per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008751"}],"value":"Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00628"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"Rieske","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51296"}]},{"type":"Binding site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00628"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00628"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00628"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}},{"type":"Binding site","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00628"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022714"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00628"}],"id":"KW-0001","category":"Ligand","name":"2Fe-2S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022797"}],"id":"KW-0058","category":"Biological process","name":"Aromatic hydrocarbons catabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022964"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48491.1"}],"id":"KW-0223","category":"Molecular function","name":"Dioxygenase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00628"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00628"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00628"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"}],"references":[{"referenceNumber":1,"citation":{"id":"15118304","citationType":"journal article","authors":["Taguchi K.","Motoyama M.","Kudo T."],"citationCrossReferences":[{"database":"PubMed","id":"15118304"},{"database":"DOI","id":"10.1271/bbb.68.787"}],"title":"Multiplicity of 2,3-dihydroxybiphenyl dioxygenase genes in the Gram-positive polychlorinated biphenyl degrading bacterium Rhodococcus rhodochrous K37.","publicationDate":"2004","journal":"Biosci. Biotechnol. Biochem.","firstPage":"787","lastPage":"795","volume":"68"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48491.1"}],"value":"K37","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48491.1"}]},{"referenceNumber":2,"citation":{"id":"17485846","citationType":"journal article","authors":["Taguchi K.","Motoyama M.","Iida T.","Kudo T."],"citationCrossReferences":[{"database":"PubMed","id":"17485846"},{"database":"DOI","id":"10.1271/bbb.60551"}],"title":"Polychlorinated biphenyl/biphenyl degrading gene clusters in Rhodococcus sp. K37, HA99, and TA431 are different from well-known bph gene clusters of Rhodococci.","publicationDate":"2007","journal":"Biosci. Biotechnol. Biochem.","firstPage":"1136","lastPage":"1144","volume":"71"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48491.1"}],"value":"K37","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF48491.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB272984","properties":[{"key":"ProteinId","value":"BAF48491.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A3KCY4","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"A3KCY4","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0051537","properties":[{"key":"GoTerm","value":"F:2 iron, 2 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004497","properties":[{"key":"GoTerm","value":"F:monooxygenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0016705","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd08881","properties":[{"key":"EntryName","value":"RHO_alpha_C_NDO-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.380.10","properties":[{"key":"EntryName","value":"Naphthalene 1,2-dioxygenase Alpha Subunit, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.102.10.10","properties":[{"key":"EntryName","value":"Rieske [2Fe-2S] iron-sulphur domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR015881","properties":[{"key":"EntryName","value":"ARHD_Rieske_2Fe_2S"}]},{"database":"InterPro","id":"IPR043266","properties":[{"key":"EntryName","value":"RHO_NdoB-like_C"}]},{"database":"InterPro","id":"IPR017941","properties":[{"key":"EntryName","value":"Rieske_2Fe-2S"}]},{"database":"InterPro","id":"IPR036922","properties":[{"key":"EntryName","value":"Rieske_2Fe-2S_sf"}]},{"database":"InterPro","id":"IPR015879","properties":[{"key":"EntryName","value":"Ring_hydroxy_dOase_asu_C_dom"}]},{"database":"InterPro","id":"IPR001663","properties":[{"key":"EntryName","value":"Rng_hydr_dOase-A"}]},{"database":"PANTHER","id":"PTHR43756:SF1","properties":[{"key":"EntryName","value":"3-PHENYLPROPIONATE_CINNAMIC ACID DIOXYGENASE SUBUNIT ALPHA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43756","properties":[{"key":"EntryName","value":"CHOLINE MONOOXYGENASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00355","properties":[{"key":"EntryName","value":"Rieske"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00848","properties":[{"key":"EntryName","value":"Ring_hydroxyl_A"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00090","properties":[{"key":"EntryName","value":"RNGDIOXGNASE"}]},{"database":"SUPFAM","id":"SSF55961","properties":[{"key":"EntryName","value":"Bet v1-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50022","properties":[{"key":"EntryName","value":"ISP domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51296","properties":[{"key":"EntryName","value":"RIESKE"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00570","properties":[{"key":"EntryName","value":"RING_HYDROXYL_ALPHA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTVDSRINDLIDAVQYDKGLINRSIFVDRDVYELELERLFANTWLFLGHVSQVAEPGDFITTYMGEDSVIVSRGHDGRVRALLNSCRHRGMRVCRSDEGNTSFFKCPYHAWTYSSAGELEGVPKFRLGYAGVLDKKEWGLREVTRVEEYRGFLFGNWAPEGPSLDEWLGELKTYFDLLFARDPAGVEVVPGAHRWTVDTNWKIAAENFAADMYHVEHSHARPAELGLMQAVPDQGYQISAGMGFIGHAFTRPVSEDVGGEEPLHSYWTLPNIQTEFLAEQRKRIAEEKGAELARLIPLGHGALFPTFAWLDLEQFRLMRVHHPQGPDRTLIHQWCVLDKSLPEDVKDAVRKQYELTFGPAGLLEQDDGENWRECQNGMRGFIGRQLDSNMMLGLGSDRTAAEVVGDDDVPGIAGGIYSEINQRRFYELWKTYMQAASPESISKIPPTRI","length":449,"molWeight":50874,"crc64":"D74A2B0E918EA66C","md5":"B20C0439B4A715CC016622E6943101E4"},"extraAttributes":{"countByCommentType":{"COFACTOR":2,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":4},"uniParcId":"UPI00006E0DF7"}}]}