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XGPT_SINMW
ID   XGPT_SINMW              Reviewed;         165 AA.
AC   A6U9A2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=Smed_1386;
OS   Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=366394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM419;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA   Richardson P.;
RT   "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL   Submitted (JUN-2007) 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: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; CP000738; ABR60232.1; -; Genomic_DNA.
DR   RefSeq; WP_011975542.1; NC_009636.1.
DR   RefSeq; YP_001327067.1; NC_009636.1.
DR   AlphaFoldDB; A6U9A2; -.
DR   SMR; A6U9A2; -.
DR   STRING; 366394.Smed_1386; -.
DR   EnsemblBacteria; ABR60232; ABR60232; Smed_1386.
DR   GeneID; 61614219; -.
DR   KEGG; smd:Smed_1386; -.
DR   PATRIC; fig|366394.8.peg.4514; -.
DR   eggNOG; COG2236; Bacteria.
DR   HOGENOM; CLU_080904_3_0_5; -.
DR   OMA; FHRDCRA; -.
DR   OrthoDB; 1819460at2; -.
DR   UniPathway; UPA00602; UER00658.
DR   UniPathway; UPA00909; UER00887.
DR   Proteomes; UP000001108; 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.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Glycosyltransferase; Magnesium;
KW   Membrane; Metal-binding; Purine salvage; Transferase.
FT   CHAIN           1..165
FT                   /note="Xanthine-guanine phosphoribosyltransferase"
FT                   /id="PRO_1000070616"
FT   BINDING         41..42
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         98..106
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         99
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT   BINDING         102..106
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT   BINDING         102
FT                   /ligand="guanine"
FT                   /ligand_id="ChEBI:CHEBI:16235"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT   BINDING         102
FT                   /ligand="xanthine"
FT                   /ligand_id="ChEBI:CHEBI:17712"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT   BINDING         144..145
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT   BINDING         145
FT                   /ligand="guanine"
FT                   /ligand_id="ChEBI:CHEBI:16235"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
FT   BINDING         145
FT                   /ligand="xanthine"
FT                   /ligand_id="ChEBI:CHEBI:17712"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01903"
SQ   SEQUENCE   165 AA;  18374 MW;  7D8005E7F53D2D68 CRC64;
     MSLPEKAFPV SWDQFHRDAR ALAWRLADNG QEWRAMVCIT RGGLVPAAIV SRELNIRMIE
     TVCIASYHDY DTQGQMKVLK SISPEIAKSG GEGVLIVDDL TDTGKTAAEV RAMLPKAHFA
     AVYAKPKGRP LVDTFVTEVS QDTWIYFPWD LGFTYQEPIA KGTRG
 
 
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