ID G2T1V4_ROSHA Unreviewed; 176 AA.
AC G2T1V4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Hypoxanthine phosphoribosyltransferase {ECO:0000256|RuleBase:RU364099};
DE EC=2.4.2.8 {ECO:0000256|RuleBase:RU364099};
GN OrderedLocusNames=RHOM_02380 {ECO:0000313|EMBL:AEN95598.1};
OS Roseburia hominis (strain DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=585394 {ECO:0000313|EMBL:AEN95598.1, ECO:0000313|Proteomes:UP000008178};
RN [1] {ECO:0000313|EMBL:AEN95598.1, ECO:0000313|Proteomes:UP000008178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183
RC {ECO:0000313|Proteomes:UP000008178};
RX PubMed=26543119; DOI=10.1128/genomeA.01286-15;
RA Travis A.J., Kelly D., Flint H.J., Aminov R.I.;
RT "Complete genome sequence of the human gut symbiont Roseburia hominis.";
RL Genome Announc. 3:E0128615-E0128615(2015).
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:0000256|ARBA:ARBA00002049}.
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:0000256|ARBA:ARBA00000210};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426;
CC Evidence={ECO:0000256|ARBA:ARBA00000210};
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:0000256|ARBA:ARBA00001442};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975;
CC Evidence={ECO:0000256|ARBA:ARBA00001442};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|RuleBase:RU364099};
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis via salvage pathway; GMP
CC from guanine: step 1/1. {ECO:0000256|ARBA:ARBA00004676}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC from hypoxanthine: step 1/1. {ECO:0000256|ARBA:ARBA00004669,
CC ECO:0000256|RuleBase:RU364099}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU364099}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000256|ARBA:ARBA00008391, ECO:0000256|RuleBase:RU364099}.
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DR EMBL; CP003040; AEN95598.1; -; Genomic_DNA.
DR RefSeq; WP_014078643.1; NC_015977.1.
DR AlphaFoldDB; G2T1V4; -.
DR STRING; 585394.RHOM_02380; -.
DR GeneID; 77458120; -.
DR KEGG; rho:RHOM_02380; -.
DR eggNOG; COG0634; Bacteria.
DR HOGENOM; CLU_073615_0_0_9; -.
DR OrthoDB; 9802824at2; -.
DR BioCyc; RHOM585394:G1H02-484-MONOMER; -.
DR UniPathway; UPA00591; UER00648.
DR Proteomes; UP000008178; Chromosome.
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: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.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU364099};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU364099};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU364099};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364099};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364099};
KW Purine salvage {ECO:0000256|ARBA:ARBA00022726,
KW ECO:0000256|RuleBase:RU364099};
KW Reference proteome {ECO:0000313|Proteomes:UP000008178};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364099}.
FT DOMAIN 13..159
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
SQ SEQUENCE 176 AA; 19830 MW; 588197A2A6C87F65 CRC64;
MKIKKINVHL TEEQIEQRVR ELGAEISKVY GDEPVCLICI LKGSVFFTCE LAKRITSPVE
IEFMSVSSYG SGTSSSGVVR IVNDLGTSIE GKNVLVIEDI IDSGRTLSYL LENLKTRNPK
TLRLCTLLDK PDRRVVDVNV DYVGFVIPDE FVVGYGLDYD QKYRNLPYIG FVEIEE
//
