(data stored in ACNUC13767 zone)

HOGENOM: SAENT2_1_PE3468

ID   SAENT2_1_PE3468                      STANDARD;      PRT;   609 AA.
AC   SAENT2_1_PE3468; Q8Z2Q2;
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   (SAENT2_1.PE3468) [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=STY3917, t3658;
OS   SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHI STR. CT18.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella; Salmonella enterica subsp. enterica
OC   serovar Typhi.
OX   NCBI_TaxID=220341;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SAENT2_1.PE3468.
CC       Salmonella enterica subsp. enterica serovar Typhi str. CT18 chromosome,
CC       complete genome.
CC   -!- ANNOTATIONS ORIGIN:GLMS_SALTI
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: HOG000258898 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q8Z2Q2; -.
DR   EMBL; AL627280; CAD03134.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO71155.1; -; Genomic_DNA.
DR   RefSeq; NP_458082.1; NC_003198.1.
DR   RefSeq; NP_807295.1; NC_004631.1.
DR   ProteinModelPortal; Q8Z2Q2; -.
DR   SMR; Q8Z2Q2; 2-609.
DR   GeneID; 1068375; -.
DR   GeneID; 1250165; -.
DR   GenomeReviews; AE014613_GR; t3658.
DR   GenomeReviews; AL513382_GR; STY3917.
DR   KEGG; stt:t3658; -.
DR   KEGG; sty:STY3917; -.
DR   OMA; YWFEALA; -.
DR   ProtClustDB; PRK00331; -.
DR   BioCyc; SENT209261:T3658-MON; -.
DR   BioCyc; SENT220341:STY3917-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; SAENT2_1.PE3468; -.
KW   Aminotransferase; Complete proteome; Cytoplasm;
KW   Glutamine amidotransferase; Repeat; Transferase.
SQ   SEQUENCE   609 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MCGIVGAIAQ RDVAEILLEG LRRLEYRGYD SAGLAVVDAE GHMTRLRRLG KVQMLAQAAE
     EHPLHGGTGI AHTRWATHGE PSEANAHPHV SEHIVVVHNG IIENHEPLRE ALKARGYTFV
     SETDTEVIAH LVNWELKQGG TLRDAILRAI PQLRGAYGTV IMDTRHPDTL LAARSGSPLV
     IGLGMGENFI ASDQLALLPV TRRFIFLEEG DIAEITRRSV NIFDNTGAEV KRQDIESNLQ
     YDAGDKGIYR HYMQKEIYEQ PNAIKNTLTG RISHGQVDLS ELGPNADDLL SKVEHIQILA
     CGTSYNSGMV SRYWFESLAG IPCDVEIASE FRYRKSAVRR NSLMITLSQS GETADTLAGL
     RLSKELGYLG SLAICNVPGS SLVRESDLAL MTNAGTEIGV ASTKAFTTQL TVLLMLVAKL
     SRLKGLDASI EHDIVHGLQA LPSRIEQMLS QDKRIELLAE DFSDKHHALF LGRGDQYPIA
     LEGALKLKEI SYIHAEAYAA GELKHGPLAL IDADMPVIVV APNNELLEKL KSNIEEVRAR
     GGQLYVFSDQ DAGFVSSDNM HIIEMPHVEE VIAPIFYTVP LQLLAYHVAL IKGTDVDQPR
     NLAKSVTVE
//

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