(data stored in ACNUC13767 zone)

HOGENOM: IDLOI1_1_PE2604

ID   IDLOI1_1_PE2604                      STANDARD;      PRT;   610 AA.
AC   IDLOI1_1_PE2604; Q5QZH5;
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   (IDLOI1_1.PE2604) [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=IL2616;
OS   IDIOMARINA LOIHIENSIS L2TR.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS IDLOI1_1.PE2604.
CC       Idiomarina loihiensis L2TR chromosome, complete genome.
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:GLMS_IDILO
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; Q5QZH5; -.
DR   EMBL; AE017340; AAV83448.1; -; Genomic_DNA.
DR   RefSeq; YP_156997.1; NC_006512.1.
DR   ProteinModelPortal; Q5QZH5; -.
DR   SMR; Q5QZH5; 2-610.
DR   GeneID; 3173330; -.
DR   GenomeReviews; AE017340_GR; IL2616.
DR   KEGG; ilo:IL2616; -.
DR   NMPDR; fig|283942.3.peg.2603; -.
DR   OMA; QFAKKTS; -.
DR   BioCyc; ILOI283942:IL2616-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; IDLOI1_1.PE2604; -.
KW   Aminotransferase; Complete proteome; Cytoplasm;
KW   Glutamine amidotransferase; Repeat; Transferase.
SQ   SEQUENCE   610 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MCGIVGATSE RRVTGILLEG LKRLEYRGYD SAGVAVIDAD NHLKSVRRTG KVQELKDAIE
     QNPLDGTIGI AHTRWATHGG VTEANAHPHR SEDEIAVVHN GIIENHERLR EELQAEGYVF
     NSQTDTEVIA HLIHHERKTH GDLLAAVKSA VRQLEGAYGT VVMDTQYPER LVVARSGSPL
     VIGVGIGENF VASDQLALLP VTRQFIYLEE GDVADINRTE IDIYDSEGNA VEREVVESDV
     SYDAGGKGQY RHFMLKEIYE QPIAVRNTLE GRLSEISVLD NAFGENAADI LKDIEHVQIV
     ACGTSYHAGM VARYWLESMA NVSCNVEIAS EFRYRKSYVH PNSLLVTISQ SGETADTLAA
     LRLSKKLGYK GSLTICNVGS SSMVRESDLA FLTRAGAEIG VASTKAFTTQ LTGLLMLTLG
     IGKYRGMPEQ QQEAVVHALQ ALPTKLEEAV SLADEIEELA QDFANKEHSL FLGRGNQYPI
     AMEGALKLKE ISYIHAEAYA AGELKHGPLA LIDEEMPVIV VAPNNDLLEK LKSNVEEVRA
     RGGLMYVFAD KNARFKGDDS LTVLNVCHCD EVIAPIVYTV PLQLLSYYVA LIKGTDVDQP
     RNLAKSVTVE
//

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