PAOA_ECOLI
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 03-AUG-2022, entry version 160.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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] {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. It might play a role in the
CC detoxification of aldehydes to avoid cell damage.
CC {ECO:0000269|PubMed:19368556}.
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:0000269|PubMed:19368556, ECO:0000269|PubMed:21081498};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:19368556, ECO:0000269|PubMed:27622978};
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}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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_SSZK01000048.1.
DR PDB; 5G5G; X-ray; 1.70 A; A=1-229.
DR PDB; 5G5H; X-ray; 2.30 A; A=1-229.
DR PDBsum; 5G5G; -.
DR PDBsum; 5G5H; -.
DR AlphaFoldDB; P77165; -.
DR SMR; P77165; -.
DR BioGRID; 4259786; 3.
DR BioGRID; 849706; 3.
DR ComplexPortal; CPX-4281; PaoABC periplasmic aldehyde oxidoreductase.
DR IntAct; P77165; 12.
DR STRING; 511145.b0286; -.
DR jPOST; P77165; -.
DR PaxDb; P77165; -.
DR PRIDE; P77165; -.
DR EnsemblBacteria; AAC73389; AAC73389; b0286.
DR EnsemblBacteria; BAE76070; BAE76070; BAE76070.
DR GeneID; 945330; -.
DR KEGG; ecj:JW0280; -.
DR KEGG; eco:b0286; -.
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; FIKHDGY; -.
DR PhylomeDB; P77165; -.
DR BioCyc; EcoCyc:G6157-MON; -.
DR BioCyc; MetaCyc:G6157-MON; -.
DR BRENDA; 1.17.1.4; 2026.
DR PRO; PR:P77165; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990204; C:oxidoreductase complex; IPI:ComplexPortal.
DR GO; GO:0042597; C:periplasmic space; IDA:EcoCyc.
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:UniProtKB-KW.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IDA:EcoCyc.
DR GO; GO:0019439; P:aromatic compound catabolic process; IDA:ComplexPortal.
DR GO; GO:0110095; P:cellular detoxification of aldehyde; IDA:ComplexPortal.
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 Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR SUPFAM; SSF47741; SSF47741; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51318; TAT; 1.
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 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 STRAND 60..67
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 82..88
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 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
