位置:首页 > 蛋白库 > HPRT_MACFA
HPRT_MACFA
ID   HPRT_MACFA              Reviewed;         218 AA.
AC   Q6LDD9; Q4R5K4;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Hypoxanthine-guanine phosphoribosyltransferase;
DE            Short=HGPRT;
DE            Short=HGPRTase;
DE            EC=2.4.2.8 {ECO:0000250|UniProtKB:P00492};
GN   Name=HPRT1; Synonyms=HPRT; ORFNames=QbsA-10852, QflA-10339;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1505533; DOI=10.1002/em.2850200205;
RA   Harbach P.R., Filipunas A.L., Wang Y., Aaron C.S.;
RT   "DNA sequence analysis of spontaneous and N-ethyl-N-nitrosourea-induced
RT   hprt mutations arising in vivo in cynomolgus monkey T-lymphocytes.";
RL   Environ. Mol. Mutagen. 20:96-105(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain stem;
RA   Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT   "Isolation and characterization of cDNA for macaque neurological disease
RT   genes.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Frontal cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts guanine to guanosine monophosphate, and hypoxanthine
CC       to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-
CC       phosphoribosylpyrophosphate onto the purine. Plays a central role in
CC       the generation of purine nucleotides through the purine salvage pathway
CC       (By similarity). {ECO:0000250}.
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; EC=2.4.2.8;
CC         Evidence={ECO:0000250|UniProtKB:P00492};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975;
CC         Evidence={ECO:0000250|UniProtKB:P00492};
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; EC=2.4.2.8;
CC         Evidence={ECO:0000250|UniProtKB:P00492};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426;
CC         Evidence={ECO:0000250|UniProtKB:P00492};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions per subunit. The magnesium ions are
CC       essentially bound to the substrate and have few direct interactions
CC       with the protein. {ECO:0000250};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC       from hypoxanthine: step 1/1.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. {ECO:0000305}.
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; S43335; AAD13829.1; -; mRNA.
DR   EMBL; AB125173; BAD51961.1; -; mRNA.
DR   EMBL; AB169539; BAE01621.1; -; mRNA.
DR   RefSeq; NP_001270523.1; NM_001283594.1.
DR   AlphaFoldDB; Q6LDD9; -.
DR   SMR; Q6LDD9; -.
DR   STRING; 9541.XP_005594676.1; -.
DR   Ensembl; ENSMFAT00000081840; ENSMFAP00000058312; ENSMFAG00000042557.
DR   GeneID; 101867079; -.
DR   CTD; 3251; -.
DR   eggNOG; KOG3367; Eukaryota.
DR   GeneTree; ENSGT00940000155028; -.
DR   OrthoDB; 1537610at2759; -.
DR   UniPathway; UPA00591; UER00648.
DR   Proteomes; UP000233100; Chromosome X.
DR   Bgee; ENSMFAG00000042557; Expressed in temporal lobe and 13 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0052657; F:guanine phosphoribosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0046038; P:GMP catabolic process; ISS:UniProtKB.
DR   GO; GO:0006178; P:guanine salvage; ISS:UniProtKB.
DR   GO; GO:0046100; P:hypoxanthine metabolic process; ISS:UniProtKB.
DR   GO; GO:0043103; P:hypoxanthine salvage; ISS:UniProtKB.
DR   GO; GO:0046040; P:IMP metabolic process; ISS:UniProtKB.
DR   GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0045964; P:positive regulation of dopamine metabolic process; ISS:UniProtKB.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; ISS:UniProtKB.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   InterPro; IPR005904; Hxn_phspho_trans.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR01203; HGPRTase; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Glycosyltransferase; Isopeptide bond; Magnesium;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Purine salvage;
KW   Reference proteome; Transferase; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P00492"
FT   CHAIN           2..218
FT                   /note="Hypoxanthine-guanine phosphoribosyltransferase"
FT                   /id="PRO_0000139586"
FT   ACT_SITE        138
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         69
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250"
FT   BINDING         134..142
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250"
FT   BINDING         186..188
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P00492"
FT   MOD_RES         103
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00493"
FT   MOD_RES         142
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P27605"
FT   CROSSLNK        115
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00492"
FT   CROSSLNK        115
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00492"
FT   CONFLICT        56
FT                   /note="E -> K (in Ref. 3; BAE01621)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   218 AA;  24579 MW;  1928EE69517CCB40 CRC64;
     MATRSPGVVI SDDEPGYDLD LFCIPNHYAE DLERVFIPHG LIMDRTERLA RDVMKEMGGH
     HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI RLKSYCNDQS TGDIKVIGGD
     DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV RQYNPKMVKV ASLLVKRTPR SVGYKPDFVG
     FEIPDKFVVG YALDYNEYFR DLNHVCVISE TGKAKYKA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024