ID E6L0C7_9PAST Unreviewed; 164 AA.
AC E6L0C7;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 63.
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=xpt {ECO:0000313|EMBL:EFU66930.1};
GN Synonyms=gpt {ECO:0000256|HAMAP-Rule:MF_01903};
GN ORFNames=HMPREF9064_1859 {ECO:0000313|EMBL:EFU66930.1};
OS Aggregatibacter segnis ATCC 33393.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=888057 {ECO:0000313|EMBL:EFU66930.1, ECO:0000313|Proteomes:UP000032871};
RN [1] {ECO:0000313|EMBL:EFU66930.1, ECO:0000313|Proteomes:UP000032871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33393 {ECO:0000313|EMBL:EFU66930.1,
RC ECO:0000313|Proteomes:UP000032871};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (DEC-2010) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:EFU66930.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEPS01000014; EFU66930.1; -; Genomic_DNA.
DR AlphaFoldDB; E6L0C7; -.
DR STRING; 739.GCA_001059425_01041; -.
DR HOGENOM; CLU_080904_3_0_6; -.
DR UniPathway; UPA00602; UER00658.
DR UniPathway; UPA00909; UER00887.
DR Proteomes; UP000032871; 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}; Reference proteome {ECO:0000313|Proteomes:UP000032871};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01903}.
FT DOMAIN 25..154
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 100..108
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 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903"
FT BINDING 104..108
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903"
FT BINDING 104
FT /ligand="guanine"
FT /ligand_id="ChEBI:CHEBI:16235"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903"
FT BINDING 104
FT /ligand="xanthine"
FT /ligand_id="ChEBI:CHEBI:17712"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903"
FT BINDING 146..147
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903"
FT BINDING 147
FT /ligand="guanine"
FT /ligand_id="ChEBI:CHEBI:16235"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903"
FT BINDING 147
FT /ligand="xanthine"
FT /ligand_id="ChEBI:CHEBI:17712"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01903"
SQ SEQUENCE 164 AA; 18362 MW; 1D03E47EB281C575 CRC64;
MPVKFLKGVF MSEKYVVTWD MFHMHARKLS ERLLPASQWK GIVAVSRGGL FPGAVLAREL
GIRHVETICI ASYNHDKQGE LQVLHAAQLE NGGEGFIVID DLVDTGNTAR AIREMYPNAH
FVTVFAKPAG AELVDDYVVD IPQNTWIEQP WDMGICFVPP LARK
//
