(data stored in SCRATCH zone)

SWISSPROT: D6XV58_BACIE

ID   D6XV58_BACIE            Unreviewed;       180 AA.
AC   D6XV58;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 54.
DE   RecName: Full=Hypoxanthine phosphoribosyltransferase {ECO:0000256|RuleBase:RU364099};
DE            EC=2.4.2.8 {ECO:0000256|RuleBase:RU364099};
GN   OrderedLocusNames=Bsel_0065 {ECO:0000313|EMBL:ADH97616.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97616.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97616.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-
CC         diphosphate + hypoxanthine; Xref=Rhea:RHEA:17973,
CC         ChEBI:CHEBI:17368, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017,
CC         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;
CC       IMP from hypoxanthine: step 1/1. {ECO:0000256|RuleBase:RU364099}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU364099}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000256|RuleBase:RU364099}.
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DR   EMBL; CP001791; ADH97616.1; -; Genomic_DNA.
DR   STRING; 439292.Bsel_0065; -.
DR   EnsemblBacteria; ADH97616; ADH97616; Bsel_0065.
DR   KEGG; bse:Bsel_0065; -.
DR   eggNOG; ENOG4108UGV; Bacteria.
DR   eggNOG; COG0634; LUCA.
DR   HOGENOM; HOG000236520; -.
DR   KO; K00760; -.
DR   OMA; TMDWMAV; -.
DR   UniPathway; UPA00591; UER00648.
DR   Proteomes; UP000000271; 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   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; D6XV58.
DR   SWISS-2DPAGE; D6XV58.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Cytoplasm {ECO:0000256|RuleBase:RU364099};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU364099,
KW   ECO:0000313|EMBL:ADH97616.1};
KW   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   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Transferase {ECO:0000256|RuleBase:RU364099,
KW   ECO:0000313|EMBL:ADH97616.1}.
FT   DOMAIN       13    159       Pribosyltran. {ECO:0000259|Pfam:PF00156}.
SQ   SEQUENCE   180 AA;  19965 MW;  07B2B8A3CDAF805C CRC64;
     MKDDILEVLV SEEEIQEKVA ELGGEITKMY EGKFPLVIGI LKGCLPFMGD LIQKVDTHLE
     FDMMDVSSYG EGFVSSGEVK IVKDLNTSVA GRDLLIVEDI IDSGTTLHYL VNLFYHRGAN
     SVKIVTLLDK PDGRTADVKA DLAGFIVPDK FVVGYGLDYI EKYRNLPFVG VLKPEVYQGK
//

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