{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P77183","secondaryAccessions":["Q2MCD9"],"uniProtkbId":"PAOD_ECOLI","entryAudit":{"firstPublicDate":"1997-11-01","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"1997-02-01","entryVersion":131,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Escherichia coli (strain K12)","taxonId":83333,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Molybdenum cofactor insertion chaperone PaoD"}}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21081498"}],"value":"paoD"},"synonyms":[{"value":"yagQ"}],"orderedLocusNames":[{"value":"b0283"},{"value":"JW0277"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19368556"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21081498"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24498065"}],"value":"Chaperone required for the production of an active PaoABC aldehyde oxidoreductase. Stabilizes the PaoC subunit and is required for the insertion of the molybdenum cofactor into this subunit (PubMed:19368556, PubMed:21081498). Binds molybdenum cofactor. Binds the molybdopterin cytosine dinucleotide (MCD) form of the cofactor after its formation by the molybdenum cofactor cytidylyltransferase MocA (PubMed:24498065)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21081498"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24498065"}],"value":"Homodimer in solution (PubMed:24498065). Interacts with MocA (PubMed:21081498)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19368556"}],"value":"Mutation results in complete impairment of cell growth in the presence of cinnamaldehyde"}],"commentType":"DISRUPTION PHENOTYPE"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"Molybdenum cofactor insertion chaperone PaoD","featureId":"PRO_0000168562"}],"keywords":[{"id":"KW-0143","category":"Molecular function","name":"Chaperone"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B1UJ6TNQ0SAS1","citationType":"submission","authors":["Chung E.","Allen E.","Araujo R.","Aparicio A.M.","Davis K.","Duncan M.","Federspiel N.","Hyman R.","Kalman S.","Komp C.","Kurdi O.","Lew H.","Lin D.","Namath A.","Oefner P.","Roberts D.","Schramm S.","Davis R.W."],"title":"Sequence of minutes 4-25 of Escherichia coli.","publicationDate":"JAN-1997","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / MG1655 / ATCC 47076","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"9278503","citationType":"journal article","authors":["Blattner F.R.","Plunkett G. III","Bloch C.A.","Perna N.T.","Burland V.","Riley M.","Collado-Vides J.","Glasner J.D.","Rode C.K.","Mayhew G.F.","Gregor J.","Davis N.W.","Kirkpatrick H.A.","Goeden M.A.","Rose D.J.","Mau B.","Shao Y."],"citationCrossReferences":[{"database":"PubMed","id":"9278503"},{"database":"DOI","id":"10.1126/science.277.5331.1453"}],"title":"The complete genome sequence of Escherichia coli K-12.","publicationDate":"1997","journal":"Science","firstPage":"1453","lastPage":"1462","volume":"277"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / MG1655 / ATCC 47076","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"16738553","citationType":"journal article","authors":["Hayashi K.","Morooka N.","Yamamoto Y.","Fujita K.","Isono K.","Choi S.","Ohtsubo E.","Baba T.","Wanner B.L.","Mori H.","Horiuchi T."],"citationCrossReferences":[{"database":"PubMed","id":"16738553"},{"database":"DOI","id":"10.1038/msb4100049"}],"title":"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.","publicationDate":"2006","journal":"Mol. Syst. Biol.","firstPage":"E1","lastPage":"E5","volume":"2"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / W3110 / ATCC 27325 / DSM 5911","type":"STRAIN"}]},{"referenceNumber":4,"citation":{"id":"19368556","citationType":"journal article","authors":["Neumann M.","Mittelstaedt G.","Iobbi-Nivol C.","Saggu M.","Lendzian F.","Hildebrandt P.","Leimkuehler S."],"citationCrossReferences":[{"database":"PubMed","id":"19368556"},{"database":"DOI","id":"10.1111/j.1742-4658.2009.07000.x"}],"title":"A periplasmic aldehyde oxidoreductase represents the first molybdopterin cytosine dinucleotide cofactor containing molybdo-flavoenzyme from Escherichia coli.","publicationDate":"2009","journal":"FEBS J.","firstPage":"2762","lastPage":"2774","volume":"276"},"referencePositions":["FUNCTION","DISRUPTION PHENOTYPE"]},{"referenceNumber":5,"citation":{"id":"21081498","citationType":"journal article","authors":["Neumann M.","Seduk F.","Iobbi-Nivol C.","Leimkuhler S."],"citationCrossReferences":[{"database":"PubMed","id":"21081498"},{"database":"DOI","id":"10.1074/jbc.m110.155671"}],"title":"Molybdopterin dinucleotide biosynthesis in Escherichia coli: identification of amino acid residues of molybdopterin dinucleotide transferases that determine specificity for binding of guanine or cytosine nucleotides.","publicationDate":"2011","journal":"J. Biol. Chem.","firstPage":"1400","lastPage":"1408","volume":"286"},"referencePositions":["FUNCTION","INTERACTION WITH MOCA","NOMENCLATURE"]},{"referenceNumber":6,"citation":{"id":"24498065","citationType":"journal article","authors":["Otrelo-Cardoso A.R.","Schwuchow V.","Rodrigues D.","Cabrita E.J.","Leimkuehler S.","Romao M.J.","Santos-Silva T."],"citationCrossReferences":[{"database":"PubMed","id":"24498065"},{"database":"DOI","id":"10.1371/journal.pone.0087295"}],"title":"Biochemical, stabilization and crystallization studies on a molecular chaperone (PaoD) involved in the maturation of molybdoenzymes.","publicationDate":"2014","journal":"PLoS ONE","firstPage":"E87295","lastPage":"E87295","volume":"9"},"referencePositions":["FUNCTION","SUBUNIT","CRYSTALLIZATION"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"U73857","properties":[{"key":"ProteinId","value":"AAB18012.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"U00096","properties":[{"key":"ProteinId","value":"AAC73386.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AP009048","properties":[{"key":"ProteinId","value":"BAE76067.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"C64754","properties":[{"key":"EntryName","value":"C64754"}]},{"database":"RefSeq","id":"NP_414817.1","properties":[{"key":"NucleotideSequenceId","value":"NC_000913.3"}]},{"database":"RefSeq","id":"WP_000121359.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP009789.1"}]},{"database":"AlphaFoldDB","id":"P77183","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P77183","properties":[{"key":"Description","value":"-"}]},{"database":"BioGRID","id":"4261499","properties":[{"key":"Interactions","value":"16"}]},{"database":"FunCoup","id":"P77183","properties":[{"key":"Number of interactors","value":"111"}]},{"database":"IntAct","id":"P77183","properties":[{"key":"Interactions","value":"4"}]},{"database":"STRING","id":"511145.b0283","properties":[{"key":"Description","value":"-"}]},{"database":"PaxDb","id":"511145-b0283","properties":[{"key":"Description","value":"-"}]},{"database":"EnsemblBacteria","id":"AAC73386","properties":[{"key":"ProteinId","value":"AAC73386"},{"key":"GeneId","value":"b0283"}]},{"database":"GeneID","id":"945010","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecj:JW0277","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"eco:b0283","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecoc:C3026_01380","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecoc:C3026_24015","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1411691.4.peg.1995","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"EchoBASE","id":"EB3326","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG1975","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"HOGENOM","id":"CLU_041115_2_1_6","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"P77183","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"EDDLSWG","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"OrthoDB","id":"9815497at2","properties":[{"key":"Description","value":"-"}]},{"database":"PhylomeDB","id":"P77183","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"EcoCyc:G6154-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:G6154-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"SABIO-RK","id":"P77183","properties":[{"key":"Description","value":"-"}]},{"database":"PRO","id":"PR:P77183","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000000625","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0043546","properties":[{"key":"GoTerm","value":"F:molybdopterin cofactor binding"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"24498065"}]},{"database":"GO","id":"GO:0042803","properties":[{"key":"GoTerm","value":"F:protein homodimerization activity"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"24498065"}]},{"database":"FunFam","id":"3.40.50.720:FF:000566","properties":[{"key":"EntryName","value":"Putative xanthine dehydrogenase accessory factor subfamily"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR052698","properties":[{"key":"EntryName","value":"MoCofactor_Util/Proc"}]},{"database":"InterPro","id":"IPR003777","properties":[{"key":"EntryName","value":"XdhC_CoxI"}]},{"database":"InterPro","id":"IPR027051","properties":[{"key":"EntryName","value":"XdhC_Rossmann_dom"}]},{"database":"PANTHER","id":"PTHR30388","properties":[{"key":"EntryName","value":"ALDEHYDE OXIDOREDUCTASE MOLYBDENUM COFACTOR ASSEMBLY PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30388:SF4","properties":[{"key":"EntryName","value":"MOLYBDENUM COFACTOR INSERTION CHAPERONE PAOD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13478","properties":[{"key":"EntryName","value":"XdhC_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02625","properties":[{"key":"EntryName","value":"XdhC_CoxI"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSYPLFDKDEHWHKPEQAFLTDDHRTILRFAVEALMSGKGAVLVTLVEIRGGAARPLGAQMVVREDGRYCGFVSGGCVEAAAAFEALEMMGSGRDREIRYGEGSPWFDIVLPCGGGITLTLHKLRSAQPLLAVLNRLEQRKPVGLRYDPQAQSLVCLPTQTRTGWNLNGFEVGFRPCVRLMIYGRSLEAQATASLAAATGYDSHIFDLFPASASAQIDTDTAVILLCHDLNRELPVLQAAREAKPFYLGALGSYRTHTLRLQKLHELGWSREETTQIRAPVGIFPKARDAHTLALSVLAEVASVRLHQEEDSCLPPSS","length":318,"molWeight":34954,"crc64":"BCE8A8A8DD78D55A","md5":"705E074B4AB5F23D1BEC82A9FD9819A0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"DISRUPTION PHENOTYPE":1},"countByFeatureType":{"Chain":1},"uniParcId":"UPI000013A0AF"}}