XDHB_ECO57
ID XDHB_ECO57 Reviewed; 292 AA.
AC Q8X6C5;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Xanthine dehydrogenase FAD-binding subunit;
DE EC=1.17.1.4;
GN Name=xdhB; OrderedLocusNames=Z4206, ECs3740;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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) (By similarity). {ECO:0000250}.
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; AE005174; AAG57996.2; -; Genomic_DNA.
DR EMBL; BA000007; BAB37163.1; -; Genomic_DNA.
DR PIR; D91096; D91096.
DR PIR; H85941; H85941.
DR RefSeq; NP_311767.1; NC_002695.1.
DR RefSeq; WP_000459192.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X6C5; -.
DR SMR; Q8X6C5; -.
DR STRING; 155864.EDL933_4068; -.
DR PRIDE; Q8X6C5; -.
DR EnsemblBacteria; AAG57996; AAG57996; Z4206.
DR EnsemblBacteria; BAB37163; BAB37163; ECs_3740.
DR GeneID; 916440; -.
DR KEGG; ece:Z4206; -.
DR KEGG; ecs:ECs_3740; -.
DR PATRIC; fig|386585.9.peg.3902; -.
DR eggNOG; COG1319; Bacteria.
DR HOGENOM; CLU_058050_0_1_6; -.
DR OMA; MVEINFD; -.
DR UniPathway; UPA00604; UER00661.
DR UniPathway; UPA00604; UER00662.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
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; IEA:UniProtKB-UniPathway.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW FAD; Flavoprotein; NAD; Oxidoreductase; Purine metabolism; Purine salvage;
KW Reference proteome.
FT CHAIN 1..292
FT /note="Xanthine dehydrogenase FAD-binding subunit"
FT /id="PRO_0000166093"
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; 31561 MW; FEC44F9990BF9BC1 CRC64;
MFDFASYHRA ATLADAINLL ADNPQAKLLA GGTDVLIQLH HHNDRYRHIV DIHNLAELRG
ITLAEDGSLR IGSATTFTQL IEDSITQRHL PALCAAASSI AGPQIRNVAT YGGNICNGAT
SADSATPTLI YDAKLEIHSP RGVRFVPING FHTGPGKVSL EHDEILVAFH FPPQPKEHVG
SAHFKYAMRD AMDISTIGCA AHCRLDNGNF SELRLAFGVA APTPIRCQHA EQTAQNAPLN
LQTLEAISES VLQDVAPRSS WRASKEFRLH LIQTMTKKVI SEAVAAAGGK LQ
