ID PAOC_ECOLI Reviewed; 732 AA. AC P77489; Q2MCD8; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 02-SEP-2026, entry version 171. DE RecName: Full=Aldehyde oxidoreductase molybdenum-binding subunit PaoC {ECO:0000305}; DE EC=1.2.99.6 {ECO:0000269|PubMed:19368556, ECO:0000269|PubMed:21081498}; GN Name=paoC {ECO:0000303|PubMed:21081498}; Synonyms=yagR; GN OrderedLocusNames=b0284, JW0278; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; RT "Sequence of minutes 4-25 of Escherichia coli."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION RP PHENOTYPE, ACTIVE SITE, AND MUTAGENESIS OF GLU-692. RX PubMed=19368556; DOI=10.1111/j.1742-4658.2009.07000.x; RA Neumann M., Mittelstaedt G., Iobbi-Nivol C., Saggu M., Lendzian F., RA Hildebrandt P., Leimkuehler S.; RT "A periplasmic aldehyde oxidoreductase represents the first molybdopterin RT cytosine dinucleotide cofactor containing molybdo-flavoenzyme from RT Escherichia coli."; RL FEBS J. 276:2762-2774(2009). RN [5] RP CATALYTIC ACTIVITY, AND NOMENCLATURE. RX PubMed=21081498; DOI=10.1074/jbc.m110.155671; RA Neumann M., Seduk F., Iobbi-Nivol C., Leimkuhler S.; RT "Molybdopterin dinucleotide biosynthesis in Escherichia coli: RT identification of amino acid residues of molybdopterin dinucleotide RT transferases that determine specificity for binding of guanine or cytosine RT nucleotides."; RL J. Biol. Chem. 286:1400-1408(2011). RN [6] RP CRYSTALLIZATION, AND SUBUNIT. RX PubMed=24492481; DOI=10.3390/ijms15022223; RA Otrelo-Cardoso A.R., da Silva Correia M.A., Schwuchow V., Svergun D.I., RA Romao M.J., Leimkuehler S., Santos-Silva T.; RT "Structural data on the periplasmic aldehyde oxidoreductase PaoABC from RT Escherichia coli: SAXS and preliminary X-ray crystallography analysis."; RL Int. J. Mol. Sci. 15:2223-2236(2014). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND RP SUBUNIT. RX PubMed=30945846; DOI=10.1021/acs.biochem.9b00078; RA Reschke S., Duffus B.R., Schrapers P., Mebs S., Teutloff C., Dau H., RA Haumann M., Leimkuehler S.; RT "Identification of YdhV as the First Molybdoenzyme Binding a Bis-Mo-MPT RT Cofactor in Escherichia coli."; RL Biochemistry 58:2228-2242(2019). RN [8] {ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH MOLYBDOPTERIN RP CYTOSINE DINUCLEOTIDE, COFACTOR, SUBUNIT, AND MUTAGENESIS OF ARG-440. RX PubMed=27622978; DOI=10.1021/acschembio.6b00572; RA Correia M.A., Otrelo-Cardoso A.R., Schwuchow V., Sigfridsson Clauss K.G., RA Haumann M., Romao M.J., Leimkuhler S., Santos-Silva T.; RT "The Escherichia coli periplasmic aldehyde oxidoreductase is an exceptional RT member of the xanthine oxidase family of molybdoenzymes."; RL ACS Chem. Biol. 11:2923-2935(2016). CC -!- FUNCTION: Oxidizes aldehydes to the corresponding carboxylic acids with CC a preference for aromatic aldehydes (PubMed:19368556, PubMed:30945846). CC It might play a role in the detoxification of aldehydes to avoid cell CC damage (PubMed:19368556). {ECO:0000269|PubMed:19368556, CC ECO:0000269|PubMed:30945846}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an aldehyde + A + H2O = a carboxylate + AH2 + H(+); CC Xref=Rhea:RHEA:56856, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:17499, CC ChEBI:CHEBI:29067; EC=1.2.99.6; CC Evidence={ECO:0000269|PubMed:19368556, ECO:0000269|PubMed:21081498, CC ECO:0000269|PubMed:30945846}; CC -!- COFACTOR: CC Name=Mo-molybdopterin cytosine dinucleotide; Xref=ChEBI:CHEBI:71308; CC Evidence={ECO:0000269|PubMed:19368556, ECO:0000269|PubMed:27622978, CC ECO:0000269|PubMed:30945846}; CC -!- ACTIVITY REGULATION: The complex requires PaoD for activity. CC {ECO:0000269|PubMed:19368556}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=63 uM for cinnamaldehyde {ECO:0000269|PubMed:19368556}; CC KM=70 uM for benzaldehyde {ECO:0000269|PubMed:19368556}; CC KM=132 uM for vanillin {ECO:0000269|PubMed:19368556}; CC Note=kcat is 84 sec(-1) with cinnamaldehyde as substrate CC (PubMed:19368556). kcat is 97 sec(-1) with benzaldehyde as substrate CC (PubMed:19368556). kcat is 125 sec(-1) with vanillin as substrate CC (PubMed:19368556). kcat is 36.64 sec(-1) with vanillin as substrate CC (at pH 6.8) (PubMed:30945846). {ECO:0000269|PubMed:19368556, CC ECO:0000269|PubMed:30945846}; CC pH dependence: CC Stable up to a pH of 4. {ECO:0000269|PubMed:19368556}; CC -!- SUBUNIT: Heterotrimer composed of PaoA, PaoB and PaoC. CC {ECO:0000269|PubMed:19368556, ECO:0000269|PubMed:24492481, CC ECO:0000269|PubMed:27622978, ECO:0000269|PubMed:30945846}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:19368556}. CC -!- DISRUPTION PHENOTYPE: Mutation results in complete impairment of cell CC growth in the presence of cinnamaldehyde. CC {ECO:0000269|PubMed:19368556}. CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U73857; AAB18013.1; -; Genomic_DNA. DR EMBL; U00096; AAC73387.1; -; Genomic_DNA. DR EMBL; AP009048; BAE76068.1; -; Genomic_DNA. DR PIR; D64754; D64754. DR RefSeq; NP_414818.1; NC_000913.3. DR RefSeq; WP_000667026.1; NZ_CP009789.1. DR PDB; 5G5G; X-ray; 1.70 A; C=1-732. DR PDB; 5G5H; X-ray; 2.30 A; C=1-732. DR AlphaFoldDB; P77489; -. DR SMR; P77489; -. DR BioGRID; 4261492; 29. DR ComplexPortal; CPX-4281; PaoABC periplasmic aldehyde oxidoreductase. DR FunCoup; P77489; 150. DR IntAct; P77489; 11. DR STRING; 511145.b0284; -. DR jPOST; P77489; -. DR PaxDb; 511145-b0284; -. DR EnsemblBacteria; AAC73387; AAC73387; b0284. DR GeneID; 944961; -. DR KEGG; ecj:JW0278; -. DR KEGG; eco:b0284; -. DR KEGG; ecoc:C3026_01385; -. DR KEGG; ecoc:C3026_24020; -. DR PATRIC; fig|1411691.4.peg.1994; -. DR EchoBASE; EB3327; -. DR eggNOG; COG1529; Bacteria. DR HOGENOM; CLU_001681_2_2_6; -. DR InParanoid; P77489; -. DR OMA; PYAYERH; -. DR OrthoDB; 6177861at2; -. DR PhylomeDB; P77489; -. DR BioCyc; EcoCyc:G6155-MONOMER; -. DR BioCyc; MetaCyc:G6155-MONOMER; -. DR BRENDA; 1.17.1.4; 2026. DR PRO; PR:P77489; -. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; NAS:EcoCyc. DR GO; GO:1990204; C:oxidoreductase complex; IPI:ComplexPortal. DR GO; GO:0042597; C:periplasmic space; NAS:ComplexPortal. DR GO; GO:0047770; F:carboxylate reductase activity; IEA:UniProtKB-EC. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0030151; F:molybdenum ion binding; IDA:EcoCyc. DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IDA:EcoCyc. DR GO; GO:0110095; P:cellular detoxification of aldehyde; IDA:ComplexPortal. DR GO; GO:0006974; P:DNA damage response; IEP:EcoliWiki. DR FunFam; 3.30.365.10:FF:000016; Xanthine dehydrogenase yagR molybdenum-binding subunit; 1. DR Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1. DR Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4. DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b. DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf. DR InterPro; IPR016208; Ald_Oxase/xanthine_DH-like. DR InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1. DR InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2. DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf. DR InterPro; IPR049648; PaoC-like. DR NCBIfam; NF041671; peri_hyde_PaoC; 1. DR PANTHER; PTHR11908:SF123; ALDEHYDE OXIDOREDUCTASE MOLYBDENUM-BINDING SUBUNIT PAOC; 1. DR PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1. DR Pfam; PF01315; Ald_Xan_dh_C; 1. DR Pfam; PF02738; MoCoBD_1; 1. DR Pfam; PF20256; MoCoBD_2; 1. DR SMART; SM01008; Ald_Xan_dh_C; 1. DR SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1. DR SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1. DR PDBsum; 5G5G; -. DR PDBsum; 5G5H; -. PE 1: Evidence at protein level; KW 3D-structure; Metal-binding; Molybdenum; Oxidoreductase; Periplasm; KW Reference proteome. FT CHAIN 1..732 FT /note="Aldehyde oxidoreductase molybdenum-binding subunit FT PaoC" FT /id="PRO_0000166090" FT ACT_SITE 692 FT /note="Proton acceptor" FT /evidence="ECO:0000305|PubMed:19368556" FT BINDING 241..242 FT /ligand="Mo-molybdopterin cytosine dinucleotide" FT /ligand_id="ChEBI:CHEBI:71308" FT /evidence="ECO:0000269|PubMed:27622978, FT ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H" FT BINDING 468..470 FT /ligand="Mo-molybdopterin cytosine dinucleotide" FT /ligand_id="ChEBI:CHEBI:71308" FT /evidence="ECO:0000269|PubMed:27622978, FT ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H" FT BINDING 511..512 FT /ligand="Mo-molybdopterin cytosine dinucleotide" FT /ligand_id="ChEBI:CHEBI:71308" FT /evidence="ECO:0000269|PubMed:27622978, FT ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H" FT BINDING 615..621 FT /ligand="Mo-molybdopterin cytosine dinucleotide" FT /ligand_id="ChEBI:CHEBI:71308" FT /evidence="ECO:0000269|PubMed:27622978, FT ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H" FT BINDING 625 FT /ligand="Mo-molybdopterin cytosine dinucleotide" FT /ligand_id="ChEBI:CHEBI:71308" FT /evidence="ECO:0000269|PubMed:27622978, FT ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H" FT BINDING 688..691 FT /ligand="Mo-molybdopterin cytosine dinucleotide" FT /ligand_id="ChEBI:CHEBI:71308" FT /evidence="ECO:0000269|PubMed:27622978, FT ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H" FT MUTAGEN 440 FT /note="R->H,K: Decrease in catalytic efficiency." FT /evidence="ECO:0000269|PubMed:27622978" FT MUTAGEN 692 FT /note="E->Q: Loss of activity." FT /evidence="ECO:0000269|PubMed:19368556" FT HELIX 11..14 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 22..24 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 27..31 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 42..44 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 49..55 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 57..67 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 69..72 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 77..82 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 83..86 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 111..119 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 120..127 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 131..136 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 143..147 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 160..163 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 165..171 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 173..182 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 194..200 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 203..208 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 213..224 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 228..230 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 231..234 FT /evidence="ECO:0007829|PDB:5G5G" FT TURN 242..245 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 250..262 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 266..269 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 272..274 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 275..278 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 285..293 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 299..311 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 314..316 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 321..324 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 330..340 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 354..372 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 376..382 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 386..388 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 391..397 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 401..412 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 414..416 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 429..441 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 447..453 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 459..462 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 468..470 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 472..484 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 488..490 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 491..494 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 501..503 FT /evidence="ECO:0007829|PDB:5G5H" FT HELIX 511..534 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 538..540 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 541..544 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 547..550 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 553..556 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 557..560 FT /evidence="ECO:0007829|PDB:5G5G" FT TURN 561..563 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 566..574 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 577..580 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 584..596 FT /evidence="ECO:0007829|PDB:5G5G" FT TURN 597..599 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 602..612 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 619..638 FT /evidence="ECO:0007829|PDB:5G5G" FT TURN 646..649 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 650..653 FT /evidence="ECO:0007829|PDB:5G5G" FT TURN 656..658 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 664..666 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 669..674 FT /evidence="ECO:0007829|PDB:5G5G" FT TURN 680..682 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 693..695 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 698..710 FT /evidence="ECO:0007829|PDB:5G5G" FT STRAND 716..718 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 721..723 FT /evidence="ECO:0007829|PDB:5G5G" FT HELIX 725..727 FT /evidence="ECO:0007829|PDB:5G5G" SQ SEQUENCE 732 AA; 78088 MW; AF198715794F0138 CRC64; MKFDKPAGEN PIDQLKVVGR PHDRIDGPLK TTGTARYAYE WHEEAPNAAY GYIVGSAIAK GRLTALDTDA AQKAPGVLAV ITASNAGALG KGDKNTARLL GGPTIEHYHQ AIALVVAETF EQARAAASLV QAHYRRNKGA YSLADEKQAV NQPPEDTPDK NVGDFDGAFT SAAVKIDATY TTPDQSHMAM EPHASMAVWD GNKLTLWTSN QMIDWCRTDL AKTLKVPVEN VRIISPYIGG GFGGKLFLRS DALLAALAAR AVKRPVKVML PRPSIPNNTT HRPATLQHLR IGADQSGKIT AISHESWSGN LPGGTPETAV QQSELLYAGA NRHTGLRLAT LDLPEGNAMR APGEAPGLMA LEIAIDELAE KAGIDPVEFR ILNDTQVDPA DPTRCFSRRQ LIECLRTGAD KFGWKQRNAT PGQVRDGEWL VGHGVAAGFR NNLLEKSGAR VHLEQNGTVT VETDMTDIGT GSYTILAQTA AEMLGVPLEQ VAVHLGDSSF PVSAGSGGQW GANTSTSGVY AACMKLREMI ASAVGFDPEQ SQFADGKITN GTRSATLHEA TAGGRLTAEE SIEFGTLSKE YQQSTFAGHF VEVGVHSATG EVRVRRMLAV CAAGRILNPK TARSQVIGAM TMGMGAALME ELAVDDRLGY FVNHDMAGYE VPVHADIPKQ EVIFLDDTDP ISSPMKAKGV GELGLCGVSA AIANAVYNAT GIRVRDYPIT LDKLLDKLPD VV //