ID   XDHA_ECO57              Reviewed;         752 AA.
AC   Q8X6C7;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Xanthine dehydrogenase molybdenum-binding subunit;
DE            EC=1.17.1.4;
GN   Name=xdhA; OrderedLocusNames=Z4205, ECs3739;
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadota; 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=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   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AE005174; AAG57995.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37162.1; -; Genomic_DNA.
DR   PIR; C91096; C91096.
DR   PIR; G85941; G85941.
DR   RefSeq; NP_311766.1; NC_002695.1.
DR   AlphaFoldDB; Q8X6C7; -.
DR   SMR; Q8X6C7; -.
DR   STRING; 155864.Z4205; -.
DR   GeneID; 916443; -.
DR   KEGG; ece:Z4205; -.
DR   KEGG; ecs:ECs_3739; -.
DR   PATRIC; fig|386585.9.peg.3901; -.
DR   eggNOG; COG1529; Bacteria.
DR   HOGENOM; CLU_001681_2_1_6; -.
DR   UniPathway; UPA00604; UER00661.
DR   UniPathway; UPA00604; UER00662.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005506; F:iron ion 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; 3.90.1170.50; 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   3: Inferred from homology;
KW   Metal-binding; Molybdenum; NAD; Oxidoreductase; Purine metabolism;
KW   Purine salvage; Reference proteome.
FT   CHAIN           1..752
FT                   /note="Xanthine dehydrogenase molybdenum-binding subunit"
FT                   /id="PRO_0000166089"
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;  81370 MW;  C42D8B8B7B386BB4 CRC64;
     MRVDAIAKVT GRARYTDDYV MAGMCYAKYV RSPIAHGYAV SINDEQARSL PGVLAIFTWE
     DVPDIPFATA GHAWTLDENK RDTADRALLT RHVRHHGDAV AIVVARDELT AEKAAQLVSI
     EWEELPVITT PEAALAEDAA PIHNGGNLLK QSTMSTGNVQ QTIDAADYQV QGHYQTPVIQ
     HCHMESVTSL AWMEDDSRIT IVSSTQIPHI VRRVVGQALD IPWSCVRVIK TFVGGGFGNK
     QDVLEEPMAA FLTSKLGGIP VKVSLSREEC FLATRTRHAF TIDGQMGVNR DGTLKGYSLD
     VLSNTGAYVS HGHSIASAGG NKVAYLYPRC AYAYSSKTCY TNLPSAGAMR GYGAPQVVFA
     VESMLDDAAT ALGIDPVEIR LRNASREGDA 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
//