XDHB_ECOLI
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 03-AUG-2022, entry version 145.
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; 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;
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; Q46800; -.
DR PRIDE; Q46800; -.
DR EnsemblBacteria; AAC75905; AAC75905; b2867.
DR EnsemblBacteria; BAE76933; BAE76933; BAE76933.
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; MVEINFD; -.
DR PhylomeDB; Q46800; -.
DR BioCyc; EcoCyc:G7486-MON; -.
DR BioCyc; MetaCyc:G7486-MON; -.
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; IC:ComplexPortal.
DR GO; GO:0002197; C:xanthine dehydrogenase complex; IC: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; IC:ComplexPortal.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 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 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; SSF55447; 1.
DR SUPFAM; SSF56176; SSF56176; 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
