(data stored in ACNUC7421 zone)

SWISSPROT: PAOA_ECO57

ID   PAOA_ECO57              Reviewed;         229 AA.
AC   Q8X6I9;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAY-2019, entry version 115.
DE   RecName: Full=Aldehyde oxidoreductase iron-sulfur-binding subunit PaoA {ECO:0000250|UniProtKB:P77165};
DE            EC=1.2.99.6 {ECO:0000250|UniProtKB:P77165};
DE   Flags: Precursor;
GN   Name=paoA {ECO:0000250|UniProtKB:P77165}; Synonyms=yagT;
GN   OrderedLocusNames=Z0352, ECs0316;
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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Oxidizes aldehydes to the corresponding carboxylic acids
CC       with a preference for aromatic aldehydes. It might play a role in
CC       the detoxification of aldehydes to avoid cell damage.
CC       {ECO:0000250|UniProtKB:P77165}.
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:P77165};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
CC         Evidence={ECO:0000250|UniProtKB:P77165};
CC       Note=Binds 2 [2Fe-2S] clusters. {ECO:0000250|UniProtKB:P77165};
CC   -!- SUBUNIT: Heterotrimer composed of PaoA, PaoB and PaoC.
CC       {ECO:0000250|UniProtKB:P77165}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P77165}.
CC   -!- PTM: Exported by the Tat system (By similarity). The position of
CC       the signal peptide cleavage has not been experimentally proven
CC       (Probable). {ECO:0000250|UniProtKB:P77165, ECO:0000305}.
DR   EMBL; AE005174; AAG54611.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33739.1; -; Genomic_DNA.
DR   PIR; D90668; D90668.
DR   PIR; G85518; G85518.
DR   RefSeq; NP_308343.1; NC_002695.1.
DR   RefSeq; WP_000070685.1; NZ_SDVX01000001.1.
DR   SMR; Q8X6I9; -.
DR   STRING; 155864.EDL933_0317; -.
DR   PRIDE; Q8X6I9; -.
DR   EnsemblBacteria; AAG54611; AAG54611; Z0352.
DR   EnsemblBacteria; BAB33739; BAB33739; BAB33739.
DR   GeneID; 914415; -.
DR   KEGG; ece:Z0352; -.
DR   KEGG; ecs:ECs0316; -.
DR   PATRIC; fig|386585.9.peg.410; -.
DR   eggNOG; ENOG4107XKX; Bacteria.
DR   eggNOG; COG2080; LUCA.
DR   HOGENOM; HOG000166647; -.
DR   KO; K13483; -.
DR   BioCyc; ECOO157:YAGT-MONOMER; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0047770; F:carboxylate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR002888; 2Fe-2S-bd.
DR   InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   Pfam; PF10518; TAT_signal; 1.
DR   SUPFAM; SSF47741; SSF47741; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8X6I9.
DR   SWISS-2DPAGE; Q8X6I9.
KW   2Fe-2S; Complete proteome; Iron; Iron-sulfur; Metal-binding;
KW   Oxidoreductase; Periplasm; Reference proteome; Signal.
FT   SIGNAL        1     53       Tat-type signal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00648}.
FT   CHAIN        54    229       Aldehyde oxidoreductase iron-sulfur-
FT                                binding subunit PaoA.
FT                                /FTId=PRO_0000189415.
FT   DOMAIN       61    137       2Fe-2S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   METAL        99     99       Iron-sulfur (2Fe-2S) 1.
FT                                {ECO:0000250|UniProtKB:P77165}.
FT   METAL       104    104       Iron-sulfur (2Fe-2S) 1.
FT                                {ECO:0000250|UniProtKB:P77165}.
FT   METAL       105    105       Iron-sulfur (2Fe-2S) 1; via amide
FT                                nitrogen. {ECO:0000250|UniProtKB:P77165}.
FT   METAL       107    107       Iron-sulfur (2Fe-2S) 1.
FT                                {ECO:0000250|UniProtKB:P77165}.
FT   METAL       119    119       Iron-sulfur (2Fe-2S) 1.
FT                                {ECO:0000250|UniProtKB:P77165}.
FT   METAL       158    158       Iron-sulfur (2Fe-2S) 2.
FT                                {ECO:0000250|UniProtKB:P77165}.
FT   METAL       161    161       Iron-sulfur (2Fe-2S) 2.
FT                                {ECO:0000250|UniProtKB:P77165}.
FT   METAL       208    208       Iron-sulfur (2Fe-2S) 2.
FT                                {ECO:0000250|UniProtKB:P77165}.
FT   METAL       210    210       Iron-sulfur (2Fe-2S) 2.
FT                                {ECO:0000250|UniProtKB:P77165}.
SQ   SEQUENCE   229 AA;  24364 MW;  7200EEDE9A0E3F0E CRC64;
     MSNQGEYPED NRVGKHEPHD LSLTRRDLIK VSAATAAAAV VYPHSTLAAS VPAATPAPEI
     MPLTLKVNGK TEQLEVDTRT TLLDALRENL HLIGTKKGCD HGQCGACTVL VNGRRLNACL
     TLAVMHQGAE ITTIEGLGSP DNLHPMQAAF IKHDGFQCGY CTSGQICSSV AVLKEIQDGI
     PSHVTVDLVS PPERTADEIR ERMSGNICRC GAYANILAAI EDAAGEIKS
//

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