(data stored in ACNUC30630 zone)

SWISSPROT: GLMS_TROW8

ID   GLMS_TROW8              Reviewed;         616 AA.
AC   Q83IA1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   11-DEC-2019, entry version 104.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000255|HAMAP-Rule:MF_00164};
DE            EC=2.6.1.16 {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=GFAT {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=Hexosephosphate aminotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
GN   Name=glmS {ECO:0000255|HAMAP-Rule:MF_00164}; OrderedLocusNames=TW158;
OS   Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropheryma.
OX   NCBI_TaxID=218496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW08/27;
RX   PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA   Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA   Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA   Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA   Relman D.A.;
RT   "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT   Tropheryma whipplei.";
RL   Lancet 361:637-644(2003).
CC   -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC       fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC       {ECO:0000255|HAMAP-Rule:MF_00164}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-
CC         phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00164};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00164}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00164}.
DR   EMBL; BX251410; CAD66838.1; -; Genomic_DNA.
DR   RefSeq; WP_011096119.1; NC_004551.1.
DR   SMR; Q83IA1; -.
DR   PRIDE; Q83IA1; -.
DR   EnsemblBacteria; CAD66838; CAD66838; TW158.
DR   KEGG; tws:TW158; -.
DR   HOGENOM; HOG000258896; -.
DR   KO; K00820; -.
DR   OMA; AYTHAGP; -.
DR   BioCyc; GCF_000196075:G1EE9-169-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1901137; P:carbohydrate derivative biosynthetic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR   CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   HAMAP; MF_00164; GlmS; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR035466; GlmS/AgaS_SIS.
DR   InterPro; IPR035490; GlmS/FrlB_SIS.
DR   InterPro; IPR005855; GlmS_trans.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001347; SIS.
DR   PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR01135; glmS; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS51464; SIS; 2.
PE   3: Inferred from homology;
DR   PRODOM; Q83IA1.
DR   SWISS-2DPAGE; Q83IA1.
KW   Aminotransferase; Cytoplasm; Glutamine amidotransferase; Repeat;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   CHAIN           2..616
FT                   /note="Glutamine--fructose-6-phosphate aminotransferase
FT                   [isomerizing]"
FT                   /id="PRO_0000135406"
FT   DOMAIN          2..222
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   DOMAIN          289..428
FT                   /note="SIS 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   DOMAIN          461..606
FT                   /note="SIS 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   ACT_SITE        2
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   ACT_SITE        611
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   616 AA;  67172 MW;  711A1871E2C62E77 CRC64;
     MCGIIGYSGP RPAAEVLLKG LERLEYRGYD SAGIAVVTDK AYIESVKKSG KLNVLKTCLE
     RRTTPIVGST GIGHTRWATH GEPSDRNAHP HMDTEQSLAI VHNGIIENSD VLKRELLASG
     KSFTSETDTE VVAHLLSDAF KKTQDLVQAF VEVTQRLEGA FAVVAIHKDQ PNTIVAAKNN
     SPLLLGFGQG ENFLASDIAA FAEYTQRVAN IDQERIVALS GDSVYITDFA GHPVDYEVHT
     VSWHPASVDS SGWSSFMLKE IFEEPQAVEN TLKGRTEDGT VILPECDHIR DDLLAIDRVV
     LVGCGTAAYA AMTASYSIEA WAGLPVSVEL SHEFRYREPV LNSKTLAVFI SQSGETMDSL
     MAVRYARQAG VKTISVCNVM DSSIPKESHA VIYTKAGPEV AVASTKSFVC QIVVLYLLAL
     YLGQLRGFRS IFPRQKAVCE LNRLPVKLKQ VLEIYESVRQ LAHWMSDSRS ILFLGRHAGY
     PIALEAALKL KELAYIHAEG FAAGELKHGP IALIEPGQPV FVIVPSPVGS PILHAKVISN
     IREIKSRGAR IIAIAAEGDS AVLPHADSVL RIPLTRYSFE PLLSIVPLQI FALELAADKG
     FDVDRPRNLA KSVTVE
//

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