XDHA_ECO57
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 03-AUG-2022, entry version 115.
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; 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=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.EDL933_4067; -.
DR EnsemblBacteria; AAG57995; AAG57995; Z4205.
DR EnsemblBacteria; BAB37162; BAB37162; ECs_3739.
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 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 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
