(data stored in ACNUC7421 zone)

HOGENOM: STPYO2_1_PE1001

ID   STPYO2_1_PE1001                      STANDARD;      PRT;   604 AA.
AC   STPYO2_1_PE1001; Q8P0S7;
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=Glucosamine--fructose-6-phosphate aminotransferase
DE   (STPYO2_1.PE1001) [isomerizing]; EC=2.6.1 16;AltName:
DE   Full=D-fructose-6-phosphate amidotransferase;AltName: Full=GFAT;AltName:
DE   Full=Glucosamine-6-phosphate synthase;AltName: Full=Hexosephosphate
DE   aminotransferase;AltName: Full=L-glutamine-D-fructose-6-phosphate
DE   amidotransferase; .
GN   Name=glmS; OrderedLocusNames=spyM18_1228;
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.PE1001.
CC       Streptococcus pyogenes MGAS8232, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:GLMS_STRP8
CC   -!- FUNCTION: Catalyzes the first step in hexosamine metabolism,
CC       converting fructose-6P into glucosamine-6P using glutamine as a
CC       nitrogen source (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-glutamine + D-fructose 6-phosphate = L-
CC       glutamate + D-glucosamine 6-phosphate.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain.
CC   -!- SIMILARITY: Contains 2 SIS domains.
CC   -!- GENE_FAMILY: HOG000258896 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q8P0S7; -.
DR   EMBL; AE009949; AAL97838.1; -; Genomic_DNA.
DR   RefSeq; NP_607339.1; NC_003485.1.
DR   ProteinModelPortal; Q8P0S7; -.
DR   MEROPS; C44.971; -.
DR   EnsemblBacteria; EBSTRT00000029849; EBSTRP00000028771; EBSTRG00000029849.
DR   GeneID; 994415; -.
DR   GenomeReviews; AE009949_GR; spyM18_1228.
DR   KEGG; spm:spyM18_1228; -.
DR   GeneTree; EBGT00050000027331; -.
DR   OMA; KNHSFVS; -.
DR   ProtClustDB; PRK00331; -.
DR   BioCyc; SPYO186103:SPYM18_1228-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:EC.
DR   GO; GO:0005529; F:sugar binding; IEA:InterPro.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00164; GlmS; 1; -.
DR   InterPro; IPR000583; GATase_2.
DR   InterPro; IPR017932; GATase_II.
DR   InterPro; IPR005855; GlmS_trans.
DR   InterPro; IPR001347; SIS.
DR   Pfam; PF00310; GATase_2; 2.
DR   Pfam; PF01380; SIS; 2.
DR   TIGRFAMs; TIGR01135; GlmS; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS51464; SIS; 2.
DR   HOGENOMDNA; STPYO2_1.PE1001; -.
KW   Aminotransferase; Complete proteome; Cytoplasm;
KW   Glutamine amidotransferase; Repeat; Transferase.
SQ   SEQUENCE   604 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MCGIVGVVGN RNATDILMQG LEKLEYRGYD SAGIFVANAN QTNLIKSVGR IADLRAKIGI
     DVAGSTGIGH TRWATHGQST EDNAHPHTSQ TGRFVLVHNG VIENYLHIKT EFLAGHDFKG
     QTDTEIAVHL IGKFVEEDKL SVLEAFKKAL SIIEGSYAFA LMDSQATDTI YVAKNKSPLL
     IGLGEGYNMV CSDAMAMIRE TSEFMEIHDK ELVILTKDKV TVTDYDGKEL IRDSYTAELD
     LSDIGKGTYP FYMLKEIDEQ PTVMRQLIST YADETGNVQV DPAIITSIQE ADRLYILAAG
     TSYHAGFATK NMLEQLTDTP VELGVASEWG YHMPLLSKKP MFILLSQSGE TADSRQVLVK
     ANAMGIPSLT VTNVPGSTLS RESTYTMLIH AGPEIAVAST KAYTAQIAAL AFLAKAVGEA
     NGKQEALDFN LVHELSLVAQ SIEATLSEKD LVAEKVQALL ATTRNAFYIG RGNDYYVAME
     AALKLKEISY IQCEGFAAGE LKHGTISLIE EDTPVIALIS SSQLVASHTR GNIQEVAARG
     AHVLTVVEEG LDREGDDIIV NKVHPFLAPI AMVIPTQLIA YYASLQRGLD VDKPRNLAKA
     VTVE
//

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