PAOC_ECO57
ID PAOC_ECO57 Reviewed; 732 AA.
AC Q8X6J4;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Aldehyde oxidoreductase molybdenum-binding subunit PaoC {ECO:0000250|UniProtKB:P77489};
DE EC=1.2.99.6 {ECO:0000250|UniProtKB:P77489};
GN Name=paoC {ECO:0000250|UniProtKB:P77489}; Synonyms=yagR;
GN OrderedLocusNames=Z0350, ECs0314;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Oxidizes aldehydes to the corresponding carboxylic acids with
CC a preference for aromatic aldehydes. It might play a role in the
CC detoxification of aldehydes to avoid cell damage.
CC {ECO:0000250|UniProtKB:P77489}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + an aldehyde + 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:0000250|UniProtKB:P77489};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin cytosine dinucleotide; Xref=ChEBI:CHEBI:71308;
CC Evidence={ECO:0000250|UniProtKB:P77489};
CC -!- SUBUNIT: Heterotrimer composed of PaoA, PaoB and PaoC.
CC {ECO:0000250|UniProtKB:P77489}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P77489}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AE005174; AAG54609.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB33737.1; -; Genomic_DNA.
DR PIR; B90668; B90668.
DR PIR; E85518; E85518.
DR RefSeq; NP_308341.1; NC_002695.1.
DR RefSeq; WP_000667043.1; NZ_SEKT01000039.1.
DR AlphaFoldDB; Q8X6J4; -.
DR SMR; Q8X6J4; -.
DR STRING; 155864.EDL933_0315; -.
DR EnsemblBacteria; AAG54609; AAG54609; Z0350.
DR EnsemblBacteria; BAB33737; BAB33737; ECs_0314.
DR GeneID; 914413; -.
DR KEGG; ece:Z0350; -.
DR KEGG; ecs:ECs_0314; -.
DR PATRIC; fig|386585.9.peg.408; -.
DR eggNOG; COG1529; Bacteria.
DR HOGENOM; CLU_001681_2_2_6; -.
DR OMA; SWMRAPG; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0047770; F:carboxylate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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.
DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR PANTHER; PTHR11908; PTHR11908; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF54665; SSF54665; 1.
DR SUPFAM; SSF56003; SSF56003; 1.
PE 3: Inferred from homology;
KW Metal-binding; Molybdenum; Oxidoreductase; Periplasm; Reference proteome.
FT CHAIN 1..732
FT /note="Aldehyde oxidoreductase molybdenum-binding subunit
FT PaoC"
FT /id="PRO_0000166091"
FT ACT_SITE 692
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P77489"
FT BINDING 241..242
FT /ligand="Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71308"
FT /evidence="ECO:0000250|UniProtKB:P77489"
FT BINDING 468..470
FT /ligand="Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71308"
FT /evidence="ECO:0000250|UniProtKB:P77489"
FT BINDING 511..512
FT /ligand="Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71308"
FT /evidence="ECO:0000250|UniProtKB:P77489"
FT BINDING 615..621
FT /ligand="Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71308"
FT /evidence="ECO:0000250|UniProtKB:P77489"
FT BINDING 625
FT /ligand="Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71308"
FT /evidence="ECO:0000250|UniProtKB:P77489"
FT BINDING 688..691
FT /ligand="Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71308"
FT /evidence="ECO:0000250|UniProtKB:P77489"
SQ SEQUENCE 732 AA; 78135 MW; A996E91BEB2643F6 CRC64;
MKFDKPAGEN PIDQLKVVGR PHDRIDGPLK TTGTARYAYE WHEESPNAAY GYIVGSAIAK
GRLTALDTDA AQKAPGVLPV ITASNAGALS KGDKNTARLL GGPTIEHYHQ AIALVVAETF
EQARAAASLV QAHYRRNKGA YSLADEKQAV SQPPEDTPDK NVGDFDGAFS SAAVKIDATY
TTPDQSHMAM EPHASMAVWD GNKLTLWTSN QMIDWCRTDL AKTLKVPVEN VRIISPYIGG
GFGGKLFLRS DALLAALAAR AVKRPVKVML PRPSIPNNTT HRPATLQHLR IGADQSGKIT
AISHESWSGN LPGGTPETAV QQSELLYAGA NRHTGLRLAT LDLPEGNAMR APGEAPGLMA
LEIAIDELAE KAGIDPVEFR ILNDTQIDPA DPTRRFSRRQ LIECLRTGAD KFGWKQRNAT
PGQVRDGEWL VGHGVAAGFR NNLLEKSGAR VHLEPNGTVT VETDMTDIGT GSYTILAQTA
AEMLGVPLEQ VAVHLGDSSF PVSAGSGGQW GANTSTSGVY AACVKLREMI ASAVGFDPEQ
SQFADGKITN GTRSAILHEA TAGGRLTAEE SIEFGTLSKE YQQSTFAGHF VEVGVHSATG
EVRVRRMLAV CAAGRILNPK TARSQVIGAM TMGMGAALME ELAVDDRLGY FVNHDMAGYE
VPVHADIPKQ EVIFLDDTDP ISSPMKAKGV GELGLCGVSA AIANAVYNAT GIRVRDYPIT
LDKLLDKLPD VV
