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   27-MAR-2024, entry version 159.
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; Pseudomonadota; 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; 511145-b0285; -.
DR   EnsemblBacteria; AAC73388; AAC73388; b0285.
DR   GeneID; 75204628; -.
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   OrthoDB; 9814706at2; -.
DR   PhylomeDB; P77324; -.
DR   BioCyc; EcoCyc:G6156-MONOMER; -.
DR   BioCyc; MetaCyc:G6156-MONOMER; -.
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; 3.30.465.10; -; 2.
DR   Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
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   PANTHER; PTHR42659:SF5; ALDEHYDE OXIDOREDUCTASE FAD-BINDING SUBUNIT PAOB-RELATED; 1.
DR   PANTHER; PTHR42659; XANTHINE DEHYDROGENASE SUBUNIT C-RELATED; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 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
//