PAOB_ECOLI
ID PAOB_ECOLI Reviewed; 318 AA.
AC P77324; Q2MCD7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Aldehyde oxidoreductase FAD-binding subunit PaoB {ECO:0000305};
DE EC=1.2.99.6 {ECO:0000269|PubMed:19368556, ECO:0000269|PubMed:21081498};
GN Name=paoB {ECO:0000303|PubMed:21081498}; Synonyms=yagS;
GN OrderedLocusNames=b0285, JW0279;
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 FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
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 [5]
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 [6]
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 [7] {ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH FAD AND IRON-SULFUR
RP (4FE-4S), 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=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:19368556, ECO:0000269|PubMed:27622978};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:27622978};
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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:19368556}.
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DR EMBL; U73857; AAB18014.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73388.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76069.1; -; Genomic_DNA.
DR PIR; E64754; E64754.
DR RefSeq; NP_414819.1; NC_000913.3.
DR RefSeq; WP_000643333.1; NZ_SSZK01000048.1.
DR PDB; 5G5G; X-ray; 1.70 A; B=1-318.
DR PDB; 5G5H; X-ray; 2.30 A; B=1-318.
DR PDBsum; 5G5G; -.
DR PDBsum; 5G5H; -.
DR AlphaFoldDB; P77324; -.
DR SMR; P77324; -.
DR BioGRID; 4259785; 121.
DR ComplexPortal; CPX-4281; PaoABC periplasmic aldehyde oxidoreductase.
DR IntAct; P77324; 8.
DR STRING; 511145.b0285; -.
DR jPOST; P77324; -.
DR PaxDb; P77324; -.
DR PRIDE; P77324; -.
DR EnsemblBacteria; AAC73388; AAC73388; b0285.
DR EnsemblBacteria; BAE76069; BAE76069; BAE76069.
DR GeneID; 66671420; -.
DR GeneID; 945710; -.
DR KEGG; ecj:JW0279; -.
DR KEGG; eco:b0285; -.
DR PATRIC; fig|1411691.4.peg.1993; -.
DR EchoBASE; EB3328; -.
DR eggNOG; COG1319; Bacteria.
DR HOGENOM; CLU_058050_1_0_6; -.
DR InParanoid; P77324; -.
DR OMA; GGTHIYR; -.
DR PhylomeDB; P77324; -.
DR BioCyc; EcoCyc:G6156-MON; -.
DR BioCyc; MetaCyc:G6156-MON; -.
DR BRENDA; 1.17.1.4; 2026.
DR PRO; PR:P77324; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990204; C:oxidoreductase complex; IPI:ComplexPortal.
DR GO; GO:0042597; C:periplasmic space; NAS:EcoCyc.
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:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
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 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 1: Evidence at protein level;
KW 3D-structure; 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_0000166094"
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:0000269|PubMed:27622978,
FT ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT BINDING 108
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27622978,
FT ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT BINDING 119
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:27622978,
FT ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT BINDING 129
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:27622978,
FT ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT BINDING 138
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:27622978,
FT ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT BINDING 157
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:27622978,
FT ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT BINDING 164
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27622978,
FT ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT BINDING 213
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27622978,
FT ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT BINDING 230
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27622978,
FT ECO:0007744|PDB:5G5G, ECO:0007744|PDB:5G5H"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 34..39
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 109..113
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:5G5G"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:5G5G"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 165..171
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 224..231
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:5G5G"
FT STRAND 254..264
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 273..277
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 279..286
FT /evidence="ECO:0007829|PDB:5G5G"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:5G5G"
FT TURN 294..297
FT /evidence="ECO:0007829|PDB:5G5G"
FT HELIX 298..315
FT /evidence="ECO:0007829|PDB:5G5G"
SQ SEQUENCE 318 AA; 33858 MW; 7D51C2B30C9BB222 CRC64;
MKAFTYERVN TPAEAALSAQ RVPGAKFIAG GTNLLDLMKL EIETPTHLID VNGLGLDKIE
VTDAGGLRIG ALVRNTDLAA HERVRRDYAV LSRALLAGAS GQLRNQATTA GNLLQRTRCP
YFYDTNQPCN KRLPGSGCAA LEGFSRQHAV VGVSEACIAT HPSDMAVAMR LLDAVVETIT
PEGKTRSITL ADFYHPPGKT PHIETALLPG ELIVAVTLPP PLGGKHIYRK VRDRASYAFA
LVSVAAIIQP DGSGRVALGG VAHKPWRIEA ADAQLSQGAQ AVYDTLFASA HPTAENTFKL
LLAKRTLASV LAEARAQA
