(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHM0_GEOS0

ID   A0A0F6BHM0_GEOS0        Unreviewed;       181 AA.
AC   A0A0F6BHM0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 24.
DE   RecName: Full=Hypoxanthine phosphoribosyltransferase {ECO:0000256|RuleBase:RU364099};
DE            EC=2.4.2.8 {ECO:0000256|RuleBase:RU364099};
GN   OrderedLocusNames=GY4MC1_0065 {ECO:0000313|EMBL:ADP72921.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72921.1};
RN   [1] {ECO:0000313|EMBL:ADP72921.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72921.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU364099};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU364099};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC       from hypoxanthine: step 1/1. {ECO:0000256|RuleBase:RU364099}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU364099}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. {ECO:0000256|RuleBase:RU364099}.
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DR   EMBL; CP002293; ADP72921.1; -; Genomic_DNA.
DR   RefSeq; WP_003247471.1; NC_014650.1.
DR   EnsemblBacteria; ADP72921; ADP72921; GY4MC1_0065.
DR   GeneID; 29237313; -.
DR   KEGG; gmc:GY4MC1_0065; -.
DR   KO; K00760; -.
DR   OMA; TMDWMAV; -.
DR   OrthoDB; 1819460at2; -.
DR   BioCyc; GSP581103:G1GOQ-78-MONOMER; -.
DR   UniPathway; UPA00591; UER00648.
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   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR01203; HGPRTase; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BHM0.
DR   SWISS-2DPAGE; A0A0F6BHM0.
KW   Cytoplasm {ECO:0000256|RuleBase:RU364099};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU364099,
KW   ECO:0000313|EMBL:ADP72921.1}; Magnesium {ECO:0000256|RuleBase:RU364099};
KW   Metal-binding {ECO:0000256|RuleBase:RU364099};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU364099};
KW   Purine salvage {ECO:0000256|RuleBase:RU364099};
KW   Transferase {ECO:0000256|RuleBase:RU364099, ECO:0000313|EMBL:ADP72921.1}.
FT   DOMAIN          15..161
FT                   /note="Pribosyltran"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
SQ   SEQUENCE   181 AA;  20488 MW;  059FCD4FA07F1CAD CRC64;
     MGMKDDIQKI LITEQQIQEK VKELGKLLTE EYEGRFPLAV GVLKGAMPFM ADLLKHIDTY
     LEMDFMDVSS YGNATVSSGE VKILKDLNTS VEGRDILIIE DIIDSGLTLS YLVDLFRYRK
     ANSIKIVTLL DKPSGRKANI QADYTGFIVP DEFVVGYGLD YCEKYRNLPY IGVLKPEVYN
     K
//

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