ID   HGPRT_MYCAV             Reviewed;         203 AA.
AC   P96794;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   13-SEP-2023, entry version 94.
DE   RecName: Full=Hypoxanthine-guanine phosphoribosyltransferase;
DE            Short=HGPRT;
DE            Short=HGPRTase;
DE            EC=2.4.2.8 {ECO:0000250|UniProtKB:P9WHQ9};
GN   Name=hpt; Synonyms=hprT;
OS   Mycobacterium avium.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1764;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Bergeson S.E., Barry R., Allen T., Hwang H., Ullman B.;
RL   Submitted (FEB-1997) 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 hypoxanthine
CC       and guanine to form the corresponding ribonucleotides IMP (inosine 5'-
CC       monophosphate) and GMP (guanosine 5'-monophosphate), with the release
CC       of PPi. {ECO:0000250|UniProtKB:P9WHQ9}.
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:P9WHQ9};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975;
CC         Evidence={ECO:0000250|UniProtKB:P9WHQ9};
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:P9WHQ9};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426;
CC         Evidence={ECO:0000250|UniProtKB:P9WHQ9};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P9WHQ9};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC       from hypoxanthine: step 1/1. {ECO:0000250|UniProtKB:P9WHQ9}.
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis via salvage pathway; GMP
CC       from guanine: step 1/1. {ECO:0000250|UniProtKB:P9WHQ9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. {ECO:0000305}.
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DR   EMBL; U88875; AAB48623.1; -; Genomic_DNA.
DR   AlphaFoldDB; P96794; -.
DR   SMR; P96794; -.
DR   UniPathway; UPA00591; UER00648.
DR   UniPathway; UPA00909; UER00887.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0032263; P:GMP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
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   NCBIfam; TIGR01203; HGPRTase; 1.
DR   PANTHER; PTHR43340:SF1; HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR43340; HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycosyltransferase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Purine salvage; Transferase.
FT   CHAIN           1..203
FT                   /note="Hypoxanthine-guanine phosphoribosyltransferase"
FT                   /id="PRO_0000139607"
FT   ACT_SITE        126
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9M2"
FT   BINDING         66
FT                   /ligand="diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:33019"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHQ9"
FT   BINDING         67
FT                   /ligand="diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:33019"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHQ9"
FT   BINDING         122
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHQ9"
FT   BINDING         123
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHQ9"
FT   BINDING         154
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHQ9"
FT   BINDING         175..176
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHQ9"
FT   BINDING         182
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHQ9"
FT   BINDING         188
FT                   /ligand="diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:33019"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHQ9"
SQ   SEQUENCE   203 AA;  22329 MW;  C0E30AEC38F7F086 CRC64;
     MGVAQISSAI TPAQPAELYP GDIKSVLLTA EQIQARIAEL GREIGDNYRD AAAETGQDLL
     LITVLKGAVI FVTDLARAIP LPTQFEFMAV SSYGSSTSSS GVVRILKDLD RDIQGRDVLI
     VEDVVDSGLT LSWLLRNLST RHPRSLRVCT LLRKPDARGA HVDIAYVGFD IPNDFVVGYG
     LDYDERYRDL SYIGTLDPRV YQQ
//