ID A3XBV3_9RHOB Unreviewed; 172 AA.
AC A3XBV3;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE RecName: Full=Xanthine-guanine phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01903};
DE Short=XGPRT {ECO:0000256|HAMAP-Rule:MF_01903};
DE EC=2.4.2.22 {ECO:0000256|HAMAP-Rule:MF_01903};
DE AltName: Full=Xanthine phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01903};
GN Name=gpt {ECO:0000256|HAMAP-Rule:MF_01903};
GN ORFNames=MED193_03742 {ECO:0000313|EMBL:EAQ44700.1};
OS Roseobacter sp. MED193.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=314262 {ECO:0000313|EMBL:EAQ44700.1, ECO:0000313|Proteomes:UP000005943};
RN [1] {ECO:0000313|EMBL:EAQ44700.1, ECO:0000313|Proteomes:UP000005943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED193 {ECO:0000313|EMBL:EAQ44700.1,
RC ECO:0000313|Proteomes:UP000005943};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC 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:0000256|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:0000256|HAMAP-Rule:MF_01903};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01903};
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis via salvage pathway; GMP
CC from guanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01903}.
CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via salvage pathway; XMP
CC from xanthine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01903}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01903}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01903};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01903}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. XGPT subfamily. {ECO:0000256|HAMAP-Rule:MF_01903}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAQ44700.1}.
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DR EMBL; AANB01000008; EAQ44700.1; -; Genomic_DNA.
DR RefSeq; WP_009808278.1; NZ_CH902583.1.
DR AlphaFoldDB; A3XBV3; -.
DR STRING; 314262.MED193_03742; -.
DR eggNOG; COG2236; Bacteria.
DR HOGENOM; CLU_080904_3_0_5; -.
DR OrthoDB; 9789690at2; -.
DR UniPathway; UPA00602; UER00658.
DR UniPathway; UPA00909; UER00887.
DR Proteomes; UP000005943; Unassembled WGS sequence.
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; XANTHINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR39563:SF1; XANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01903};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_01903};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01903};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01903};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01903};
KW Purine salvage {ECO:0000256|ARBA:ARBA00022726, ECO:0000256|HAMAP-
KW Rule:MF_01903};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01903}.
FT DOMAIN 14..164
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
FT BINDING 47..48
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903"
FT BINDING 84
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903"
FT BINDING 84
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903"
FT BINDING 107..115
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903"
FT BINDING 111..115
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903"
FT BINDING 111
FT /ligand="guanine"
FT /ligand_id="ChEBI:CHEBI:16235"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903"
FT BINDING 111
FT /ligand="xanthine"
FT /ligand_id="ChEBI:CHEBI:17712"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903"
FT BINDING 153..154
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903"
FT BINDING 154
FT /ligand="guanine"
FT /ligand_id="ChEBI:CHEBI:16235"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903"
FT BINDING 154
FT /ligand="xanthine"
FT /ligand_id="ChEBI:CHEBI:17712"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903"
SQ SEQUENCE 172 AA; 19189 MW; 310A6DD62AE60520 CRC64;
MTDRLPHEKG FHISWDQIHR DSRALAWRLD GQGPNDGAWR AVVAITRGGM APAMIVSREL
DIRTVDTISV KSYHSGGGAQ DQQREAQVLK SPDAELMGDG EGILIIDDLV DSGKTLELVR
KMYPKAHCAT VYAKPKGEPM VDTFITGVSQ DTWIFFPWDM ALQYVEPYRG TD
//
