XDHA_ECOLI
ID XDHA_ECOLI Reviewed; 752 AA.
AC Q46799; Q2M9X4;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Putative xanthine dehydrogenase molybdenum-binding subunit XdhA;
DE EC=1.17.1.4;
GN Name=xdhA; Synonyms=ygeS; OrderedLocusNames=b2866, JW5462;
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 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). Deletion results in increased adenine sensitivity,
CC suggesting that this protein contributes to the conversion of adenine
CC to guanine nucleotides during purine salvage.
CC {ECO:0000269|PubMed:10986234}.
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=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {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}.
CC -!- INDUCTION: Is not solely regulated by nitrogen limitation.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U28375; AAA83047.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75904.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76932.1; -; Genomic_DNA.
DR PIR; B65070; B65070.
DR RefSeq; NP_417342.1; NC_000913.3.
DR AlphaFoldDB; Q46799; -.
DR SMR; Q46799; -.
DR BioGRID; 4262319; 8.
DR ComplexPortal; CPX-5122; XdhABC xanthine dehydrogenase complex.
DR IntAct; Q46799; 1.
DR STRING; 511145.b2866; -.
DR PaxDb; Q46799; -.
DR PRIDE; Q46799; -.
DR EnsemblBacteria; AAC75904; AAC75904; b2866.
DR EnsemblBacteria; BAE76932; BAE76932; BAE76932.
DR GeneID; 947116; -.
DR KEGG; ecj:JW5462; -.
DR KEGG; eco:b2866; -.
DR PATRIC; fig|511145.12.peg.2959; -.
DR EchoBASE; EB2861; -.
DR eggNOG; COG1529; Bacteria.
DR HOGENOM; CLU_001681_2_1_6; -.
DR InParanoid; Q46799; -.
DR OMA; CTHNPLG; -.
DR PhylomeDB; Q46799; -.
DR BioCyc; EcoCyc:G7485-MON; -.
DR BioCyc; MetaCyc:G7485-MON; -.
DR BRENDA; 1.17.1.4; 2026.
DR UniPathway; UPA00604; UER00661.
DR UniPathway; UPA00604; UER00662.
DR PRO; PR:Q46799; -.
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:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IMP:EcoliWiki.
DR GO; GO:0004854; F:xanthine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0009114; P:hypoxanthine catabolic process; IC:ComplexPortal.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IC:ComplexPortal.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH.
DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR PANTHER; PTHR11908; PTHR11908; 2.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF54665; SSF54665; 1.
DR SUPFAM; SSF56003; SSF56003; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Molybdenum; NAD; Oxidoreductase; Purine metabolism;
KW Purine salvage; Reference proteome.
FT CHAIN 1..752
FT /note="Putative xanthine dehydrogenase molybdenum-binding
FT subunit XdhA"
FT /id="PRO_0000166088"
FT BINDING 206
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
FT BINDING 516
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
SQ SEQUENCE 752 AA; 81321 MW; DD16E1FAA8497AC4 CRC64;
MRVDAIAKVT GRARYTDDYV MAGMCYAKYV RSPIAHGYAV SINDEQARSL PGVLAIFTWE
DVPDIPFATA GHAWTLDENK RDTADRALLT RHVRHHGDAV AIVVARDELT AEKAAQLVSI
EWQELPVITT PEAALAEDAA PIHNGGNLLK QSTMSTGNVQ QTIDAADYQV QGHYQTPVIQ
HCHMESVTSL AWMEDDSRIT IVSSTQIPHI VRRVVGQALD IPWSCVRVIK PFVGGGFGNK
QDVLEEPMAA FLTSKLGGIP VKVSLSREEC FLATRTRHAF TIDGQMGVNR DGTLKGYSLD
VLSNTGAYAS HGHSIASAGG NKVAYLYPRC AYAYSSKTCY TNLPSAGAMR GYGAPQVVFA
VESMLDDAAT ALGIDPVEIR LRNAAREGDA NPLTGKRIYS AGLPECLEKG RKIFEWEKRR
AECQNQQGNL RRGVGVACFS YTSNTWPVGV EIAGARLLMN QDGTINVQSG ATEIGQGADT
VFSQMVAETV GVPVSDVRVI STQDTDVTPF DPGAFASRQS YVAAPALRSA ALLLKEKIIA
HAAVMLHQSA MNLTLIKGHI VLVERPEEPL MSLKDLAMDA FYHPERGGQL SAESSIKTTT
NPPAFGCTFV DLTVDIALCK VTINRILNVH DSGHILNPLL AEGQVHGGMG MGIGWALFEE
MIIDAKSGVV RNPNLLDYKM PTMPDLPQLE SAFVEINEPQ SAYGHKSLGE PPIIPVAAAI
RNAVKMATGV AINTLPLTPK RLYEEFHLAG LI
