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 25-MAY-2022, entry version 112.
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; Tropherymataceae; 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}.
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DR EMBL; BX251410; CAD66838.1; -; Genomic_DNA.
DR RefSeq; WP_011096119.1; NC_004551.1.
DR AlphaFoldDB; Q83IA1; -.
DR SMR; Q83IA1; -.
DR GeneID; 67387931; -.
DR KEGG; tws:TW158; -.
DR HOGENOM; CLU_012520_5_2_11; -.
DR OMA; ASEYRYA; -.
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_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR Pfam; PF01380; SIS; 2.
DR SUPFAM; SSF53697; SSF53697; 1.
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;
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 REGION 70..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
