XGPT_YERPE
ID XGPT_YERPE Reviewed; 152 AA.
AC Q8ZC05; Q0WC61; Q74WW8; Q7CK60;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Xanthine-guanine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01903};
DE Short=XGPRT {ECO:0000255|HAMAP-Rule:MF_01903};
DE EC=2.4.2.- {ECO:0000255|HAMAP-Rule:MF_01903};
DE EC=2.4.2.22 {ECO:0000255|HAMAP-Rule:MF_01903};
DE AltName: Full=Xanthine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01903};
GN Name=gpt {ECO:0000255|HAMAP-Rule:MF_01903};
GN OrderedLocusNames=YPO3225, y0963, YP_0708;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
RN [4] {ECO:0007744|PDB:5XTK}
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) IN COMPLEX WITH GMP.
RA Pavithra G.C., Ramagopal U.A.;
RT "Crystal structure of Xanthine-guanine phosphoribosyltransferase from
RT Yersinia pestis.";
RL Submitted (JUN-2017) to the PDB data bank.
RN [5] {ECO:0007744|PDB:6KP5}
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS).
RA Lankipalli S., Ramagopal U.A.;
RT "crystal structure of Xanthine-guanine phosphoribosyltransferase (XGPRT)
RT from Yersinia pestis in P21212 space group.";
RL Submitted (AUG-2019) to the PDB data bank.
RN [6] {ECO:0007744|PDB:6KQC}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANT PHE-136.
RA Lankipalli S., Ramagopal U.A.;
RT "Crystal structure of E136F mutant of Xanthine-guanine
RT phosphoribosyltransferase from Yersinia pestis.";
RL Submitted (AUG-2019) to the PDB data bank.
CC -!- FUNCTION: Purine salvage pathway enzyme that catalyzes the transfer of
CC the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-
CC diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and
CC xanthine to form the corresponding ribonucleotides GMP (guanosine 5'-
CC monophosphate) and XMP (xanthosine 5'-monophosphate), with the release
CC of PPi. To a lesser extent, also acts on hypoxanthine.
CC {ECO:0000255|HAMAP-Rule:MF_01903}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + GMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC guanine; Xref=Rhea:RHEA:25424, ChEBI:CHEBI:16235, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58017, ChEBI:CHEBI:58115; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01903};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01903};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + XMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC xanthine; Xref=Rhea:RHEA:10800, ChEBI:CHEBI:17712, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57464, ChEBI:CHEBI:58017; EC=2.4.2.22;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01903};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10802;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01903};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC hypoxanthine; Xref=Rhea:RHEA:17973, ChEBI:CHEBI:17368,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58053;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01903};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975;
CC Evidence={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 -!- PATHWAY: Purine metabolism; GMP biosynthesis via salvage pathway; GMP
CC from guanine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01903}.
CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway; XMP
CC 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 phosphoribosyltransferase
CC family. XGPT subfamily. {ECO:0000255|HAMAP-Rule:MF_01903}.
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DR EMBL; AL590842; CAL21819.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM84544.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS60974.1; -; Genomic_DNA.
DR PIR; AH0391; AH0391.
DR RefSeq; WP_002208704.1; NZ_WUCM01000034.1.
DR RefSeq; YP_002348127.1; NC_003143.1.
DR PDB; 5XTK; X-ray; 1.74 A; A/B=1-152.
DR PDB; 6KP5; X-ray; 1.10 A; A/B=1-152.
DR PDB; 6KQC; X-ray; 1.70 A; A/B=1-152.
DR PDBsum; 5XTK; -.
DR PDBsum; 6KP5; -.
DR PDBsum; 6KQC; -.
DR AlphaFoldDB; Q8ZC05; -.
DR SMR; Q8ZC05; -.
DR STRING; 214092.YPO3225; -.
DR PaxDb; Q8ZC05; -.
DR DNASU; 1145910; -.
DR EnsemblBacteria; AAM84544; AAM84544; y0963.
DR EnsemblBacteria; AAS60974; AAS60974; YP_0708.
DR GeneID; 66842670; -.
DR KEGG; ype:YPO3225; -.
DR KEGG; ypk:y0963; -.
DR KEGG; ypm:YP_0708; -.
DR PATRIC; fig|214092.21.peg.3686; -.
DR eggNOG; COG2236; Bacteria.
DR HOGENOM; CLU_080904_3_0_6; -.
DR OMA; FHRDCRA; -.
DR UniPathway; UPA00602; UER00658.
DR UniPathway; UPA00909; UER00887.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IEA:RHEA.
DR GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000310; F:xanthine phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0032263; P:GMP salvage; IBA:GO_Central.
DR GO; GO:0032264; P:IMP salvage; IBA:GO_Central.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-UniRule.
DR GO; GO:0032265; P:XMP salvage; IBA:GO_Central.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR HAMAP; MF_01903; XGPRT; 1.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR023747; Xanthine_Guanine_PRibTrfase.
DR PANTHER; PTHR39563; PTHR39563; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Glycosyltransferase;
KW Magnesium; Membrane; Metal-binding; Purine salvage; Reference proteome;
KW Transferase.
FT CHAIN 1..152
FT /note="Xanthine-guanine phosphoribosyltransferase"
FT /id="PRO_0000139695"
FT BINDING 37..38
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT BINDING 69
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT BINDING 69
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:5XTK"
FT BINDING 88..96
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT BINDING 92..96
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:5XTK"
FT BINDING 92
FT /ligand="guanine"
FT /ligand_id="ChEBI:CHEBI:16235"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT BINDING 92
FT /ligand="xanthine"
FT /ligand_id="ChEBI:CHEBI:17712"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT BINDING 134..135
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PDB:5XTK"
FT BINDING 135
FT /ligand="guanine"
FT /ligand_id="ChEBI:CHEBI:16235"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT BINDING 135
FT /ligand="xanthine"
FT /ligand_id="ChEBI:CHEBI:17712"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:6KP5"
FT HELIX 9..22
FT /evidence="ECO:0007829|PDB:6KP5"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:6KP5"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:6KP5"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:6KP5"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:6KP5"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:6KP5"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:6KP5"
FT STRAND 84..94
FT /evidence="ECO:0007829|PDB:6KP5"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:6KP5"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:6KP5"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:6KP5"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:6KP5"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:6KP5"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6KP5"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:6KP5"
SQ SEQUENCE 152 AA; 16966 MW; FACA8D10E3A76A94 CRC64;
MNEKYVVTWD MLQIHARKLA QRLLPAEQWK GIIAVSRGGL VPAGILAREL GIRYVDTVCI
SSYDHDNQRD LKVLKRAEGD GEGFIVIDDL VDTGGTATAI REMYPKAHFV TIFAKPAGRP
LVDDYVVDIP QNTWIEQPWD MAVTFVAPLS GK
