XGPT_CROS8
ID XGPT_CROS8 Reviewed; 152 AA.
AC A7MEN2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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}; OrderedLocusNames=ESA_03115;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU78343.1; -; Genomic_DNA.
DR RefSeq; WP_004385350.1; NC_009778.1.
DR AlphaFoldDB; A7MEN2; -.
DR SMR; A7MEN2; -.
DR EnsemblBacteria; ABU78343; ABU78343; ESA_03115.
DR GeneID; 45665576; -.
DR GeneID; 56731807; -.
DR KEGG; esa:ESA_03115; -.
DR HOGENOM; CLU_080904_3_0_6; -.
DR OMA; FHRDCRA; -.
DR OrthoDB; 1819460at2; -.
DR UniPathway; UPA00602; UER00658.
DR UniPathway; UPA00909; UER00887.
DR Proteomes; UP000000260; Chromosome.
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; IEA:RHEA.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000310; F:xanthine phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032263; P:GMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-UniRule.
DR GO; GO:0032265; P:XMP salvage; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Glycosyltransferase; Magnesium;
KW Membrane; Metal-binding; Purine salvage; Transferase.
FT CHAIN 1..152
FT /note="Xanthine-guanine phosphoribosyltransferase"
FT /id="PRO_1000070609"
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:0000255|HAMAP-Rule:MF_01903"
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:0000255|HAMAP-Rule:MF_01903"
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:0000255|HAMAP-Rule:MF_01903"
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"
SQ SEQUENCE 152 AA; 16914 MW; 8071594D09559C5A CRC64;
MSEKYVVTWD MLQIHARKLA SRLLPAEQWK GIIAVSRGGL VPGALLAREL GIRHVDTVCI
SSYDHDNQRE LKVIKRAEGD GEGFIVVDDL VDTGGTAVAI REMYPKARFV TIFAKPAGQP
LVDDYVIDIP QDTWIEQPWD MGVVFVPPLS GR
