(data stored in ACNUC7421 zone)

HOGENOM: STPYO2_1_PE10

ID   STPYO2_1_PE10                        STANDARD;      PRT;   180 AA.
AC   STPYO2_1_PE10; Q7CNQ9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Hypoxanthine-guanine phosphoribosyltransferase;
DE   Short=HGPRT; Short=HGPRTase; EC=2.4.2 8; (STPYO2_1.PE10).
GN   Name=hpt; OrderedLocusNames=spyM18_0013;
OS   STREPTOCOCCUS PYOGENES MGAS8232.
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; Streptococcus.
OX   NCBI_TaxID=186103;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS STPYO2_1.PE10.
CC       Streptococcus pyogenes MGAS8232, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:HPRT_STRP8
CC   -!- CATALYTIC ACTIVITY: IMP + diphosphate = hypoxanthine + 5-phospho-
CC       alpha-D-ribose 1-diphosphate.
CC   -!- CATALYTIC ACTIVITY: GMP + diphosphate = guanine + 5-phospho-alpha-
CC       D-ribose 1-diphosphate.
CC   -!- COFACTOR: Binds 2 magnesium ions per subunit. The magnesium ions
CC       are essentially bound to the substrate and have few direct
CC       interactions with the protein (By similarity).
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway;
CC       IMP from hypoxanthine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family.
CC   -!- GENE_FAMILY: HOG000236520 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q7CNQ9; -.
DR   EMBL; AE009949; AAL96846.1; -; Genomic_DNA.
DR   RefSeq; NP_606347.1; NC_003485.1.
DR   ProteinModelPortal; Q7CNQ9; -.
DR   SMR; Q7CNQ9; 3-178.
DR   EnsemblBacteria; EBSTRT00000030148; EBSTRP00000029070; EBSTRG00000030148.
DR   GeneID; 995231; -.
DR   GenomeReviews; AE009949_GR; spyM18_0013.
DR   KEGG; spm:spyM18_0013; -.
DR   GeneTree; EBGT00050000028142; -.
DR   OMA; INAHYAD; -.
DR   ProtClustDB; CLSK883890; -.
DR   BioCyc; SPYO186103:SPYM18_0013-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IEA:EC.
DR   GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IEA: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:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR   InterPro; IPR005904; Hxn_phspho_trans.
DR   InterPro; IPR000836; PRibTrfase.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   TIGRFAMs; TIGR01203; HGPRTase; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
DR   HOGENOMDNA; STPYO2_1.PE10; -.
KW   hypoxanthine-guanine phosphoribosyltransferase;
KW   Complete proteome; Cytoplasm; Glycosyltransferase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Purine salvage; Transferase.
SQ   SEQUENCE   180 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLEQDIQKIL YSENDIIRKT KKLGEQLTKD YQEKNPLMIG VLKGSVPFMA ELMKHIDTHV
     EIDFMVVSSY HGGTSSSGEV KILKDVDTNI EGRDIIIVED IIDTGRTLKY LRDMFKYRKA
     NTIKIATLFD KPEGRVVKIE ADYVCYNIPN EFIVGFGLDY AENYRNLPYV GVLKEEVYSK
//

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