{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q8Z937","uniProtkbId":"FADE_SALTI","entryAudit":{"firstPublicDate":"2002-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2002-03-01","entryVersion":132,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Salmonella typhi","taxonId":90370,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8ZRJ7"}],"value":"Acyl-coenzyme A dehydrogenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8ZRJ7"}],"value":"ACDH"},{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8ZRJ7"}],"value":"Acyl-CoA dehydrogenase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8ZRJ7"}],"value":"1.3.8.7"},{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8ZRJ7"}],"value":"1.3.8.8"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8ZRJ7"}],"value":"Medium-/long-chain fatty acyl-CoA dehydrogenase"}}]},"genes":[{"geneName":{"value":"fadE"},"orderedLocusNames":[{"value":"STY0354"},{"value":"t2541"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8ZRJ7"}],"value":"Catalyzes the dehydrogenation of acyl-coenzymes A (acyl-CoAs) to 2-enoyl-CoAs, the first step of the beta-oxidation cycle of fatty acid degradation. Is required for the utilization of medium- and long-chain fatty acids as sole carbon sources for growth. Is needed for bacterial survival during carbone-source starvation"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a medium-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a medium-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14477"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:83723"},{"database":"ChEBI","id":"CHEBI:83726"}],"ecNumber":"1.3.8.7","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8ZRJ7"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a long-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17721"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:83721"},{"database":"ChEBI","id":"CHEBI:83727"}],"ecNumber":"1.3.8.8","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8ZRJ7"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P15651"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8ZRJ7"}],"value":"Lipid metabolism; fatty acid beta-oxidation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the acyl-CoA dehydrogenase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":814,"modifier":"EXACT"}},"description":"Acyl-coenzyme A dehydrogenase","featureId":"PRO_0000201202"},{"type":"Active site","location":{"start":{"value":497,"modifier":"EXACT"},"end":{"value":497,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P15651"}]}],"keywords":[{"id":"KW-0274","category":"Ligand","name":"FAD"},{"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"11677608","citationType":"journal article","authors":["Parkhill J.","Dougan G.","James K.D.","Thomson N.R.","Pickard D.","Wain J.","Churcher C.M.","Mungall K.L.","Bentley S.D.","Holden M.T.G.","Sebaihia M.","Baker S.","Basham D.","Brooks K.","Chillingworth T.","Connerton P.","Cronin A.","Davis P.","Davies R.M.","Dowd L.","White N.","Farrar J.","Feltwell T.","Hamlin N.","Haque A.","Hien T.T.","Holroyd S.","Jagels K.","Krogh A.","Larsen T.S.","Leather S.","Moule S.","O'Gaora P.","Parry C.","Quail M.A.","Rutherford K.M.","Simmonds M.","Skelton J.","Stevens K.","Whitehead S.","Barrell B.G."],"citationCrossReferences":[{"database":"PubMed","id":"11677608"},{"database":"DOI","id":"10.1038/35101607"}],"title":"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18.","publicationDate":"2001","journal":"Nature","firstPage":"848","lastPage":"852","volume":"413"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"CT18","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"12644504","citationType":"journal article","authors":["Deng W.","Liou S.-R.","Plunkett G. III","Mayhew G.F.","Rose D.J.","Burland V.","Kodoyianni V.","Schwartz D.C.","Blattner F.R."],"citationCrossReferences":[{"database":"PubMed","id":"12644504"},{"database":"DOI","id":"10.1128/jb.185.7.2330-2337.2003"}],"title":"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18.","publicationDate":"2003","journal":"J. Bacteriol.","firstPage":"2330","lastPage":"2337","volume":"185"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 700931 / Ty2","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AL513382","properties":[{"key":"ProteinId","value":"CAD08779.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AE014613","properties":[{"key":"ProteinId","value":"AAO70125.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_000973055.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CALNVT020000001.1"}]},{"database":"AlphaFoldDB","id":"Q8Z937","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q8Z937","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"220341.gene:17584383","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"stt:t2541","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"sty:STY0354","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|220341.7.peg.348","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG1960","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"HOGENOM","id":"CLU_012192_0_0_6","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"CDLANDW","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"OrthoDB","id":"9802447at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00659","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000002670","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004466","properties":[{"key":"GoTerm","value":"F:long-chain fatty acyl-CoA dehydrogenase activity"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0070991","properties":[{"key":"GoTerm","value":"F:medium-chain fatty acyl-CoA dehydrogenase activity"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0033539","properties":[{"key":"GoTerm","value":"P:fatty acid beta-oxidation using acyl-CoA dehydrogenase"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"1.10.540.10:FF:000004","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.140.10:FF:000009","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.110.10:FF:000010","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.540.10","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase/oxidase, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.110.10","properties":[{"key":"EntryName","value":"Butyryl-CoA Dehydrogenase, subunit A, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.140.10","properties":[{"key":"EntryName","value":"Butyryl-CoA Dehydrogenase, subunit A, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR046373","properties":[{"key":"EntryName","value":"Acyl-CoA_Oxase/DH_mid-dom_sf"}]},{"database":"InterPro","id":"IPR036250","properties":[{"key":"EntryName","value":"AcylCo_DH-like_C"}]},{"database":"InterPro","id":"IPR009075","properties":[{"key":"EntryName","value":"AcylCo_DH/oxidase_C"}]},{"database":"InterPro","id":"IPR006091","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_M"}]},{"database":"InterPro","id":"IPR013786","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_N"}]},{"database":"InterPro","id":"IPR037069","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_N_sf"}]},{"database":"InterPro","id":"IPR009100","properties":[{"key":"EntryName","value":"AcylCoA_DH/oxidase_NM_dom_sf"}]},{"database":"InterPro","id":"IPR047634","properties":[{"key":"EntryName","value":"FadE"}]},{"database":"InterPro","id":"IPR015396","properties":[{"key":"EntryName","value":"FadE_C"}]},{"database":"NCBIfam","id":"NF038187","properties":[{"key":"EntryName","value":"FadE_coli"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF007000","properties":[{"key":"EntryName","value":"PRK09463.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009586","properties":[{"key":"EntryName","value":"PRK13026.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48083:SF18","properties":[{"key":"EntryName","value":"ACYL-COENZYME A DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48083","properties":[{"key":"EntryName","value":"MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF09317","properties":[{"key":"EntryName","value":"ACDH_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00441","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02770","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_M"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02771","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47203","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56645","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase NM domain-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MMILSIIATVVLLGALFYHRVSLFLSSLILLAWTAALGVAGLWSIWLLVPLAIILVPFNLTPMRKSMISAPVFRGFRKVMPPMSRTEKEAIDAGTTWWEGDLFQGKPDWKKLHNYPQPQLTAEEQAFLDGPVEEACRMANDFQITHELADLPPELWAYLKEHRFFAMIIKKEYGGLEFSAYVQSRVLQKLSGVSGILAITVGVPNSLGPGELLQHYGTEEQKNHYLPRLARGQEIPCFALTSPEAGSDAGAIPDTGVVCMGEWQGQQVLGMRLTWNKRYITLAPIATVLGLAFKLSDPDRLLGGEEELGITCALIPTSTPGVEIGRRHFPLNVPFQNGPTRGNDIFVPIDYIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGVKSVALATGAYAHIRRQFKISIGKMEGIEEPLARIAGNAYVMDAAASLITYGIMLGEKPAVLSAIVKYHCTHRGQQSIIDAMDITGGKGIMLGESNFLARAYQGAPIAITVEGANILTRSMMIFGQGAIRCHPYVLEEMAAAQNNDVNAFDKLLFKHIGHVGSNTVRSFWLGLTRGLTSHTPTGDATKRYYQHLNRLSANLALLSDVSMAVLGGSLKRRERISTRLGDVLSQLYLASAVLKRYDDEGRHEADLPLVHWGVQDALYRAEQAMDDLLQNFPNRVVAGLLTAMIFPTGRHYLAPSDKLDHAVAKILQVPNATRSRIGRGQYLTPAEHNPVGLLEEALRDVIAADPIHQRICKELGKNLPFTRLDELARNALAKGLIDKDEAAILAKAEESRLRSINVDDFEPEALATKPVKLPEKVRKVEAA","length":814,"molWeight":89274,"crc64":"425C6195436B2E07","md5":"9069ABDA1CBB9792B4C5ECA32304881E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":1},"uniParcId":"UPI000005A290"}}