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   27-MAR-2024, entry version 157.
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; 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   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; 511145-b2866; -.
DR   EnsemblBacteria; AAC75904; AAC75904; b2866.
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; SMSEAPY; -.
DR   PhylomeDB; Q46799; -.
DR   BioCyc; EcoCyc:G7485-MONOMER; -.
DR   BioCyc; MetaCyc:G7485-MONOMER; -.
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; NAS:ComplexPortal.
DR   GO; GO:0002197; C:xanthine dehydrogenase complex; NAS: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; NAS:ComplexPortal.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; NAS:ComplexPortal.
DR   Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR   Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
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-like.
DR   InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR   InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR   InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR   PANTHER; PTHR11908:SF132; ALDEHYDE OXIDASE 1-RELATED; 1.
DR   PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 1.
DR   Pfam; PF02738; MoCoBD_1; 1.
DR   Pfam; PF20256; MoCoBD_2; 1.
DR   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR   SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 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
//