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Database: UniProt
Entry: B8DWC1_BIFA0
LinkDB: B8DWC1_BIFA0
Original site: B8DWC1_BIFA0 
ID   B8DWC1_BIFA0            Unreviewed;       187 AA.
AC   B8DWC1;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 64.
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:ACL28772.1};
GN   OrderedLocusNames=BLA_0473 {ECO:0000313|EMBL:ACL28772.1};
OS   Bifidobacterium animalis subsp. lactis (strain AD011).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=442563 {ECO:0000313|EMBL:ACL28772.1, ECO:0000313|Proteomes:UP000002456};
RN   [1] {ECO:0000313|EMBL:ACL28772.1, ECO:0000313|Proteomes:UP000002456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD011 {ECO:0000313|EMBL:ACL28772.1,
RC   ECO:0000313|Proteomes:UP000002456};
RX   PubMed=19011029; DOI=10.1128/JB.01515-08;
RA   Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., Yoon S.H.,
RA   Kim D.-W., Ji G.E., Park H.-S., Oh T.K.;
RT   "Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp.
RT   lactis AD011.";
RL   J. Bacteriol. 191:678-679(2009).
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; CP001213; ACL28772.1; -; Genomic_DNA.
DR   RefSeq; WP_004268795.1; NC_011835.1.
DR   AlphaFoldDB; B8DWC1; -.
DR   STRING; 442563.BLA_0473; -.
DR   GeneID; 66532858; -.
DR   KEGG; bla:BLA_0473; -.
DR   HOGENOM; CLU_073615_0_0_11; -.
DR   OMA; TMDWMAV; -.
DR   UniPathway; UPA00591; UER00648.
DR   Proteomes; UP000002456; 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:ACL28772.1}; Magnesium {ECO:0000256|RuleBase:RU364099};
KW   Metal-binding {ECO:0000256|RuleBase:RU364099};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU364099};
KW   Purine salvage {ECO:0000256|ARBA:ARBA00022726,
KW   ECO:0000256|RuleBase:RU364099};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002456};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364099}.
FT   DOMAIN          16..164
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
SQ   SEQUENCE   187 AA;  21014 MW;  DC72238A98701051 CRC64;
     MRIVDVQNEI DHELITHDEI MKRIQEAADQ VSEDYKHTLP LLVCVLKGAA NTMTAFAQAM
     SIQVELDYMS LSSYGAGTSS SGTITVRQDL SRDVRGRDVI IVEDIIDSGR TLDWLVNELK
     SRGAKSVEIF ALLEKPARRV IDVDVKYKGF EIPDEFVVGF GLDYDERYRN LDSIAVLKPE
     VYEGAVQ
//
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