PAOB_ECO57
ID PAOB_ECO57 Reviewed; 318 AA.
AC Q8X6J0;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Aldehyde oxidoreductase FAD-binding subunit PaoB {ECO:0000250|UniProtKB:P77324};
DE EC=1.2.99.6 {ECO:0000250|UniProtKB:P77324};
GN Name=paoB {ECO:0000250|UniProtKB:P77324}; Synonyms=yagS;
GN OrderedLocusNames=Z0351, ECs0315;
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:P77324}.
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:P77324};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P77324};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P77324};
CC -!- SUBUNIT: Heterotrimer composed of PaoA, PaoB and PaoC.
CC {ECO:0000250|UniProtKB:P77324}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P77324}.
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DR EMBL; AE005174; AAG54610.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB33738.1; -; Genomic_DNA.
DR PIR; C90668; C90668.
DR PIR; F85518; F85518.
DR RefSeq; NP_308342.1; NC_002695.1.
DR RefSeq; WP_000643341.1; NZ_SDVX01000001.1.
DR AlphaFoldDB; Q8X6J0; -.
DR SMR; Q8X6J0; -.
DR STRING; 155864.EDL933_0316; -.
DR EnsemblBacteria; AAG54610; AAG54610; Z0351.
DR EnsemblBacteria; BAB33738; BAB33738; ECs_0315.
DR GeneID; 914414; -.
DR KEGG; ece:Z0351; -.
DR KEGG; ecs:ECs_0315; -.
DR PATRIC; fig|386585.9.peg.409; -.
DR eggNOG; COG1319; Bacteria.
DR HOGENOM; CLU_058050_1_0_6; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0047770; F:carboxylate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 2.
DR InterPro; IPR005107; CO_DH_flav_C.
DR InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR Pfam; PF00941; FAD_binding_5; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF55447; SSF55447; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Periplasm; Reference proteome.
FT CHAIN 1..318
FT /note="Aldehyde oxidoreductase FAD-binding subunit PaoB"
FT /id="PRO_0000166095"
FT DOMAIN 1..223
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 26..34
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P77324"
FT BINDING 108
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P77324"
FT BINDING 119
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P77324"
FT BINDING 129
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P77324"
FT BINDING 138
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P77324"
FT BINDING 157
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P77324"
FT BINDING 164
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P77324"
FT BINDING 213
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P77324"
FT BINDING 230
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P77324"
SQ SEQUENCE 318 AA; 33886 MW; 32C48CE9D0F16F90 CRC64;
MKAFTYERVN TPAEAALSAQ RVPGAKFIAG GTNLLDLMKL EIETPTHLID VNGLGLDKIE
VTDAGGLRIG ALVRNTDLVA HERVRRDYAV LSRALLAGAS GQLRNQATTA GNLLQRTRCP
YFYDTNQPCN KRLPGSGCAA LEGFSRQHAV VGVSEACIAT HPSDMAVAMR LLDAVVETIT
PEGKTRSITL ADFYHPPGKT PHIETALLPG ELIVAVTLPP PLGGKHIYRK VRDRASYTFA
LVSVAAIIQP DGSGRVALGG VAHKPWRIEA ADAQLSQGAQ AVYDALFASA HPTAENTFKL
LLAKRTLASV LAEARAQA
