(data stored in ACNUC7421 zone)

SWISSPROT: XGPT_ECODH

ID   XGPT_ECODH              Reviewed;         152 AA.
AC   B1XDY1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 57.
DE   RecName: Full=Xanthine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01903};
DE            EC=2.4.2.22 {ECO:0000255|HAMAP-Rule:MF_01903};
DE   AltName: Full=Xanthine-guanine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01903};
DE            Short=XGPRT {ECO:0000255|HAMAP-Rule:MF_01903};
GN   Name=gpt {ECO:0000255|HAMAP-Rule:MF_01903};
GN   OrderedLocusNames=ECDH10B_0220;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
CC   -!- FUNCTION: Acts on guanine, xanthine and to a lesser extent
CC       hypoxanthine. {ECO:0000255|HAMAP-Rule:MF_01903}.
CC   -!- CATALYTIC ACTIVITY: XMP + diphosphate = 5-phospho-alpha-D-ribose
CC       1-diphosphate + xanthine. {ECO:0000255|HAMAP-Rule:MF_01903}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01903};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01903};
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway;
CC       XMP from xanthine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01903}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01903}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01903}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01903}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. XGPT subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01903}.
DR   EMBL; CP000948; ACB01405.1; -; Genomic_DNA.
DR   RefSeq; WP_001291990.1; NC_010473.1.
DR   ProteinModelPortal; B1XDY1; -.
DR   SMR; B1XDY1; -.
DR   EnsemblBacteria; ACB01405; ACB01405; ECDH10B_0220.
DR   KEGG; ecd:ECDH10B_0220; -.
DR   eggNOG; COG0503; LUCA.
DR   HOGENOM; HOG000226805; -.
DR   KO; K00769; -.
DR   OMA; FHRDCRA; -.
DR   UniPathway; UPA00602; UER00658.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000310; F:xanthine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR   GO; GO:0032265; P:XMP salvage; IEA:UniProtKB-UniPathway.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   HAMAP; MF_01903; XGPRT; 1.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR023747; Xanthine_Guanine_PRibTrfase.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1XDY1.
DR   SWISS-2DPAGE; B1XDY1.
KW   Cell inner membrane; Cell membrane; Glycosyltransferase; Magnesium;
KW   Membrane; Metal-binding; Purine salvage; Transferase.
FT   CHAIN         1    152       Xanthine phosphoribosyltransferase.
FT                                /FTId=PRO_1000188744.
FT   REGION       37     38       5-phosphoribose 1-diphosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01903}.
FT   REGION       92     96       5-phosphoribose 1-diphosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01903}.
FT   METAL        89     89       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01903}.
FT   BINDING      69     69       5-phosphoribose 1-diphosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01903}.
FT   BINDING      92     92       Xanthine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01903}.
FT   BINDING     135    135       Xanthine; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01903}.
SQ   SEQUENCE   152 AA;  16971 MW;  F0AD813127E7200D CRC64;
     MSEKYIVTWD MLQIHARKLA SRLMPSEQWK GIIAVSRGGL VPGALLAREL GIRHVDTVCI
     SSYDHDNQRE LKVLKRAEGD GEGFIVIDDL VDTGGTAVAI REMYPKAHFV TIFAKPAGRP
     LVDDYVVDIP QDTWIEQPWD MGVVFVPPIS GR
//

If you have problems or comments...

PBIL Back to PBIL home page