ID H6RPW2_BLASD Unreviewed; 194 AA.
AC H6RPW2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Hypoxanthine phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011895, ECO:0000256|RuleBase:RU364099};
DE EC=2.4.2.8 {ECO:0000256|ARBA:ARBA00011895, ECO:0000256|RuleBase:RU364099};
GN Name=hpt {ECO:0000313|EMBL:CCG01531.1};
GN OrderedLocusNames=BLASA_0575 {ECO:0000313|EMBL:CCG01531.1};
OS Blastococcus saxobsidens (strain DD2).
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG01531.1, ECO:0000313|Proteomes:UP000007517};
RN [1] {ECO:0000313|EMBL:CCG01531.1, ECO:0000313|Proteomes:UP000007517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD2 {ECO:0000313|EMBL:CCG01531.1,
RC ECO:0000313|Proteomes:UP000007517};
RX PubMed=22535935; DOI=10.1128/JB.00320-12;
RA Chouaia B., Crotti E., Brusetti L., Daffonchio D., Essoussi I., Nouioui I.,
RA Sbissi I., Ghodhbane-Gtari F., Gtari M., Vacherie B., Barbe V., Medigue C.,
RA Gury J., Pujic P., Normand P.;
RT "Genome Sequence of Blastococcus saxobsidens DD2, a Stone-Inhabiting
RT Bacterium.";
RL J. Bacteriol. 194:2752-2753(2012).
RN [2] {ECO:0000313|Proteomes:UP000007517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517};
RA Genoscope.;
RT "Complete genome sequence of Blastococcus saxobsidens strain DD2.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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; 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; FO117623; CCG01531.1; -; Genomic_DNA.
DR AlphaFoldDB; H6RPW2; -.
DR STRING; 1146883.BLASA_0575; -.
DR KEGG; bsd:BLASA_0575; -.
DR eggNOG; COG0634; Bacteria.
DR HOGENOM; CLU_073615_0_0_11; -.
DR OrthoDB; 9802824at2; -.
DR UniPathway; UPA00591; UER00648.
DR Proteomes; UP000007517; 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|RuleBase:RU364099,
KW ECO:0000313|EMBL:CCG01531.1};
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:UP000007517};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364099}.
FT DOMAIN 30..175
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
SQ SEQUENCE 194 AA; 20955 MW; 72231A238E104473 CRC64;
MTEPATTPGA LGPDHGYGPD IDHVTLTEAQ IQEKIGELAA QVAADYAGKE VLLVGVLKGA
VLFMSDFARA LQLPTQMEFM AVSSYGSSTS SSGVVRILKD LDRDITGKHV LVLEDIIDSG
LTLSWLLKNL GGRAPASLEV CALLRKPDAV KVQVPVKYIG FDIPNEFVVG YGLDYAERYR
DLPYIATLKP SVYQ
//
