ID   PAOA_ECOLI              Reviewed;         229 AA.
AC   P77165; Q2MCD6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   02-SEP-2026, entry version 177.
DE   RecName: Full=Aldehyde oxidoreductase iron-sulfur-binding subunit PaoA {ECO:0000305};
DE            EC=1.2.99.6 {ECO:0000269|PubMed:19368556, ECO:0000269|PubMed:21081498};
DE   Flags: Precursor;
GN   Name=paoA {ECO:0000303|PubMed:21081498}; Synonyms=yagT;
GN   OrderedLocusNames=b0286, JW0280;
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   EXPORT VIA THE TAT-SYSTEM.
RX   PubMed=17218314; DOI=10.1074/jbc.m610507200;
RA   Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B.,
RA   Palmer T., Georgiou G.;
RT   "Export pathway selectivity of Escherichia coli twin arginine translocation
RT   signal peptides.";
RL   J. Biol. Chem. 282:8309-8316(2007).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT,
RP   SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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   [6]
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   [7]
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   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND 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   [9] {ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H}
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR
RP   (2FE-2S), COFACTOR, AND SUBUNIT.
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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000269|PubMed:19368556, ECO:0000269|PubMed:27622978,
CC         ECO:0000303|PubMed:30945846};
CC       Note=Binds 2 [2Fe-2S] clusters. {ECO:0000269|PubMed:27622978,
CC       ECO:0000305|PubMed:19368556};
CC   -!- ACTIVITY REGULATION: The complex requires PaoD for activity.
CC       {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   -!- INTERACTION:
CC       P77165; P0AFM2: proX; NbExp=2; IntAct=EBI-1115563, EBI-1129961;
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:19368556}.
CC   -!- PTM: Exported by the Tat system (PubMed:17218314). The position of the
CC       signal peptide cleavage has not been experimentally proven (Probable).
CC       {ECO:0000269|PubMed:17218314, ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Mutation results in complete impairment of cell
CC       growth in the presence of cinnamaldehyde.
CC       {ECO:0000269|PubMed:19368556}.
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DR   EMBL; U73857; AAB18015.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73389.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76070.1; -; Genomic_DNA.
DR   PIR; F64754; F64754.
DR   RefSeq; NP_414820.1; NC_000913.3.
DR   RefSeq; WP_000070700.1; NZ_CP009789.1.
DR   PDB; 5G5G; X-ray; 1.70 A; A=1-229.
DR   PDB; 5G5H; X-ray; 2.30 A; A=1-229.
DR   AlphaFoldDB; P77165; -.
DR   SMR; P77165; -.
DR   BioGRID; 4259786; 14.
DR   BioGRID; 849706; 3.
DR   ComplexPortal; CPX-4281; PaoABC periplasmic aldehyde oxidoreductase.
DR   FunCoup; P77165; 149.
DR   IntAct; P77165; 12.
DR   STRING; 511145.b0286; -.
DR   jPOST; P77165; -.
DR   PaxDb; 511145-b0286; -.
DR   EnsemblBacteria; AAC73389; AAC73389; b0286.
DR   GeneID; 945330; -.
DR   KEGG; ecj:JW0280; -.
DR   KEGG; eco:b0286; -.
DR   KEGG; ecoc:C3026_01395; -.
DR   KEGG; ecoc:C3026_24030; -.
DR   PATRIC; fig|1411691.4.peg.1992; -.
DR   EchoBASE; EB3329; -.
DR   eggNOG; COG2080; Bacteria.
DR   HOGENOM; CLU_052511_1_0_6; -.
DR   InParanoid; P77165; -.
DR   OMA; RCTGYGG; -.
DR   OrthoDB; 9775084at2; -.
DR   PhylomeDB; P77165; -.
DR   BioCyc; EcoCyc:G6157-MONOMER; -.
DR   BioCyc; MetaCyc:G6157-MONOMER; -.
DR   BRENDA; 1.17.1.4; 2026.
DR   PRO; PR:P77165; -.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR   GO; GO:1990204; C:oxidoreductase complex; IPI:ComplexPortal.
DR   GO; GO:0042597; C:periplasmic space; IBA:GO_Central.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:EcoCyc.
DR   GO; GO:0047770; F:carboxylate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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   CDD; cd00207; fer2; 1.
DR   FunFam; 1.10.150.120:FF:000005; Aldehyde dehydrogenase iron-sulfur subunit; 1.
DR   FunFam; 3.10.20.30:FF:000020; Xanthine dehydrogenase iron-sulfur subunit; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 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; IPR052914; Aldehyde_Oxdr_Iron-Sulfur.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   NCBIfam; NF008514; PRK11433.1; 1.
DR   PANTHER; PTHR45331:SF1; ALDEHYDE OXIDOREDUCTASE IRON-SULFUR-BINDING SUBUNIT PAOA; 1.
DR   PANTHER; PTHR45331; OXIDOREDUCTASE, IRON-SULPHUR BINDING SUBUNIT-RELATED-RELATED; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51318; TAT; 1.
DR   PDBsum; 5G5G; -.
DR   PDBsum; 5G5H; -.
PE   1: Evidence at protein level;
KW   2Fe-2S; 3D-structure; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW   Periplasm; 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_0000189414"
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   COMPBIAS        9..21
FT                   /note="Basic and acidic residues"
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:0000269|PubMed:27622978,
FT                   ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT   BINDING         104
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:27622978,
FT                   ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT   BINDING         105
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:27622978,
FT                   ECO:0007744|PDB:5G5H"
FT   BINDING         107
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:27622978,
FT                   ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT   BINDING         119
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:27622978,
FT                   ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT   BINDING         158
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:27622978,
FT                   ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT   BINDING         161
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:27622978,
FT                   ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT   BINDING         208
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:27622978,
FT                   ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT   BINDING         210
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:27622978,
FT                   ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT   HELIX           56..59
FT                   /evidence="ECO:0007829|PDB:5G5G"
FT   STRAND          60..67
FT                   /evidence="ECO:0007829|PDB:5G5G"
FT   STRAND          70..77
FT                   /evidence="ECO:0007829|PDB:5G5G"
FT   HELIX           85..89
FT                   /evidence="ECO:0007829|PDB:5G5G"
FT   STRAND          100..104
FT                   /evidence="ECO:0007829|PDB:5G5G"
FT   STRAND          108..111
FT                   /evidence="ECO:0007829|PDB:5G5G"
FT   STRAND          114..117
FT                   /evidence="ECO:0007829|PDB:5G5G"
FT   HELIX           118..120
FT                   /evidence="ECO:0007829|PDB:5G5G"
FT   HELIX           123..126
FT                   /evidence="ECO:0007829|PDB:5G5G"
FT   STRAND          130..132
FT                   /evidence="ECO:0007829|PDB:5G5G"
FT   HELIX           134..137
FT                   /evidence="ECO:0007829|PDB:5G5G"
FT   HELIX           145..153
FT                   /evidence="ECO:0007829|PDB:5G5G"
FT   STRAND          157..159
FT                   /evidence="ECO:0007829|PDB:5G5G"
FT   HELIX           162..177
FT                   /evidence="ECO:0007829|PDB:5G5G"
FT   STRAND          186..190
FT                   /evidence="ECO:0007829|PDB:5G5H"
FT   HELIX           191..193
FT                   /evidence="ECO:0007829|PDB:5G5G"
FT   HELIX           196..202
FT                   /evidence="ECO:0007829|PDB:5G5G"
FT   TURN            203..205
FT                   /evidence="ECO:0007829|PDB:5G5G"
FT   HELIX           213..225
FT                   /evidence="ECO:0007829|PDB:5G5G"
SQ   SEQUENCE   229 AA;  24343 MW;  216961D7BD21836C CRC64;
     MSNQGEYPED NRVGKHEPHD LSLTRRDLIK VSAATAATAV VYPHSTLAAS VPAATPAPEI
     MPLTLKVNGK TEQLEVDTRT TLLDTLRENL HLIGTKKGCD HGQCGACTVL VNGRRLNACL
     TLAVMHQGAE ITTIEGLGSP DNLHPMQAAF IKHDGFQCGY CTSGQICSSV AVLKEIQDGI
     PSHVTVDLVS APETTADEIR ERMSGNICRC GAYANILAAI EDAAGEIKS
//