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 03-AUG-2022, entry version 126.
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., 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: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:190135;
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 the
CC signal peptide cleavage has not been experimentally proven (Probable).
CC {ECO:0000250|UniProtKB:P77165, ECO:0000305}.
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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_SWKA01000005.1.
DR AlphaFoldDB; Q8X6I9; -.
DR SMR; Q8X6I9; -.
DR STRING; 155864.EDL933_0317; -.
DR EnsemblBacteria; AAG54611; AAG54611; Z0352.
DR EnsemblBacteria; BAB33739; BAB33739; ECs_0316.
DR GeneID; 914415; -.
DR KEGG; ece:Z0352; -.
DR KEGG; ecs:ECs_0316; -.
DR PATRIC; fig|386585.9.peg.410; -.
DR eggNOG; COG2080; Bacteria.
DR HOGENOM; CLU_052511_1_0_6; -.
DR OMA; FIKHDGY; -.
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: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;
KW 2Fe-2S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Periplasm;
KW Reference proteome; Signal.
FT SIGNAL 1..53
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 54..229
FT /note="Aldehyde oxidoreductase iron-sulfur-binding subunit
FT PaoA"
FT /id="PRO_0000189415"
FT DOMAIN 61..137
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 99
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P77165"
FT BINDING 104
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P77165"
FT BINDING 105
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P77165"
FT BINDING 107
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P77165"
FT BINDING 119
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P77165"
FT BINDING 158
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P77165"
FT BINDING 161
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P77165"
FT BINDING 208
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P77165"
FT BINDING 210
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="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
