ID   XDHB_ECOLI              Reviewed;         292 AA.
AC   Q46800; Q2M9X3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=Putative xanthine dehydrogenase FAD-binding subunit XdhB;
DE            EC=1.17.1.4;
GN   Name=xdhB; Synonyms=ygeT; OrderedLocusNames=b2867, JW2835;
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;
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   [2]
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   [3]
RP   DISCUSSION OF FUNCTION.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=10986234; DOI=10.1128/jb.182.19.5332-5341.2000;
RA   Xi H., Schneider B.L., Reitzer L.;
RT   "Purine catabolism in Escherichia coli and function of xanthine
RT   dehydrogenase in purine salvage.";
RL   J. Bacteriol. 182:5332-5341(2000).
CC   -!- FUNCTION: Presumed to be a dehydrogenase, but possibly an oxidase.
CC       Participates in limited purine salvage (requires aspartate) but does
CC       not support aerobic growth on purines as the sole carbon source (purine
CC       catabolism).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) + xanthine = H(+) + NADH + urate;
CC         Xref=Rhea:RHEA:16669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17712, ChEBI:CHEBI:17775, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.17.1.4;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + hypoxanthine + NAD(+) = H(+) + NADH + xanthine;
CC         Xref=Rhea:RHEA:24670, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17368, ChEBI:CHEBI:17712, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.17.1.4;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Purine metabolism; hypoxanthine degradation; urate from
CC       hypoxanthine: step 1/2.
CC   -!- PATHWAY: Purine metabolism; hypoxanthine degradation; urate from
CC       hypoxanthine: step 2/2.
CC   -!- SUBUNIT: Heterotrimer of XdhA, XdhB and XdhC. {ECO:0000305}.
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DR   EMBL; U28375; AAA83048.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75905.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76933.1; -; Genomic_DNA.
DR   PIR; C65070; C65070.
DR   RefSeq; NP_417343.1; NC_000913.3.
DR   RefSeq; WP_000459182.1; NZ_LN832404.1.
DR   AlphaFoldDB; Q46800; -.
DR   SMR; Q46800; -.
DR   BioGRID; 4262320; 136.
DR   ComplexPortal; CPX-5122; XdhABC xanthine dehydrogenase complex.
DR   IntAct; Q46800; 5.
DR   STRING; 511145.b2867; -.
DR   PaxDb; 511145-b2867; -.
DR   EnsemblBacteria; AAC75905; AAC75905; b2867.
DR   GeneID; 75205296; -.
DR   GeneID; 947205; -.
DR   KEGG; ecj:JW2835; -.
DR   KEGG; eco:b2867; -.
DR   PATRIC; fig|1411691.4.peg.3867; -.
DR   EchoBASE; EB2862; -.
DR   eggNOG; COG1319; Bacteria.
DR   HOGENOM; CLU_058050_0_1_6; -.
DR   InParanoid; Q46800; -.
DR   OMA; AMTTHHD; -.
DR   OrthoDB; 9814706at2; -.
DR   PhylomeDB; Q46800; -.
DR   BioCyc; EcoCyc:G7486-MONOMER; -.
DR   BioCyc; MetaCyc:G7486-MONOMER; -.
DR   BRENDA; 1.17.1.4; 2026.
DR   UniPathway; UPA00604; UER00661.
DR   UniPathway; UPA00604; UER00662.
DR   PRO; PR:Q46800; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal.
DR   GO; GO:0002197; C:xanthine dehydrogenase complex; NAS:ComplexPortal.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004854; F:xanthine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009114; P:hypoxanthine catabolic process; IMP:EcoliWiki.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; NAS:ComplexPortal.
DR   Gene3D; 3.30.465.10; -; 1.
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; PF03450; CO_deh_flav_C; 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   4: Predicted;
KW   FAD; Flavoprotein; NAD; Oxidoreductase; Purine metabolism; Purine salvage;
KW   Reference proteome.
FT   CHAIN           1..292
FT                   /note="Putative xanthine dehydrogenase FAD-binding subunit
FT                   XdhB"
FT                   /id="PRO_0000166092"
FT   DOMAIN          1..176
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   BINDING         27..34
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         109..113
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   292 AA;  31557 MW;  74A07D137DA857E8 CRC64;
     MFDFASYHRA ATLADAINLL ADNPQAKLLA GGTDVLIQLH HHNDRYRHIV DIHNLAELRG
     ITLAEDGSLR IGSATTFTQL IEDPITQRHL PALCAAATSI AGPQIRNVAT YGGNICNGAT
     SADSATPTLI YDAKLEIHSP RGVRFVPING FHTGPGKVSL EHDEILVAFH FPPQPKEHAG
     SAHFKYAMRD AMDISTIGCA AHCRLDNGNF SELRLAFGVA APTPIRCQHA EQTAQNAPLN
     LQTLEAISES VLQDVAPRSS WRASKEFRLH LIQTMTKKVI SEAVAAAGGK LQ
//