GLMS_FRATT
ID GLMS_FRATT Reviewed; 612 AA.
AC Q5NHQ9;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 107.
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=FTT_0388;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
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; AJ749949; CAG45021.1; -; Genomic_DNA.
DR RefSeq; WP_003020072.1; NZ_CP010290.1.
DR RefSeq; YP_169433.1; NC_006570.2.
DR PDB; 3TBF; X-ray; 2.28 A; A/B/C/D/E/F/G/H=241-612.
DR PDBsum; 3TBF; -.
DR AlphaFoldDB; Q5NHQ9; -.
DR SMR; Q5NHQ9; -.
DR IntAct; Q5NHQ9; 2.
DR STRING; 177416.FTT_0388; -.
DR PRIDE; Q5NHQ9; -.
DR DNASU; 3192352; -.
DR EnsemblBacteria; CAG45021; CAG45021; FTT_0388.
DR KEGG; ftu:FTT_0388; -.
DR eggNOG; COG0449; Bacteria.
DR OMA; ASEYRYA; -.
DR Proteomes; UP000001174; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Cytoplasm; Glutamine amidotransferase;
KW Reference proteome; Repeat; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT CHAIN 2..612
FT /note="Glutamine--fructose-6-phosphate aminotransferase
FT [isomerizing]"
FT /id="PRO_0000135332"
FT DOMAIN 2..219
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT DOMAIN 287..427
FT /note="SIS 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT DOMAIN 460..602
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 607
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:3TBF"
FT HELIX 261..270
FT /evidence="ECO:0007829|PDB:3TBF"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:3TBF"
FT HELIX 287..292
FT /evidence="ECO:0007829|PDB:3TBF"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:3TBF"
FT HELIX 303..318
FT /evidence="ECO:0007829|PDB:3TBF"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:3TBF"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:3TBF"
FT STRAND 343..352
FT /evidence="ECO:0007829|PDB:3TBF"
FT HELIX 355..364
FT /evidence="ECO:0007829|PDB:3TBF"
FT TURN 365..368
FT /evidence="ECO:0007829|PDB:3TBF"
FT STRAND 369..381
FT /evidence="ECO:0007829|PDB:3TBF"
FT HELIX 382..386
FT /evidence="ECO:0007829|PDB:3TBF"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:3TBF"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:3TBF"
FT HELIX 405..424
FT /evidence="ECO:0007829|PDB:3TBF"
FT HELIX 430..441
FT /evidence="ECO:0007829|PDB:3TBF"
FT HELIX 443..451
FT /evidence="ECO:0007829|PDB:3TBF"
FT HELIX 454..461
FT /evidence="ECO:0007829|PDB:3TBF"
FT HELIX 462..464
FT /evidence="ECO:0007829|PDB:3TBF"
FT STRAND 469..474
FT /evidence="ECO:0007829|PDB:3TBF"
FT HELIX 478..493
FT /evidence="ECO:0007829|PDB:3TBF"
FT STRAND 496..501
FT /evidence="ECO:0007829|PDB:3TBF"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:3TBF"
FT TURN 505..512
FT /evidence="ECO:0007829|PDB:3TBF"
FT STRAND 518..523
FT /evidence="ECO:0007829|PDB:3TBF"
FT HELIX 529..541
FT /evidence="ECO:0007829|PDB:3TBF"
FT STRAND 545..551
FT /evidence="ECO:0007829|PDB:3TBF"
FT HELIX 552..557
FT /evidence="ECO:0007829|PDB:3TBF"
FT STRAND 564..568
FT /evidence="ECO:0007829|PDB:3TBF"
FT HELIX 575..595
FT /evidence="ECO:0007829|PDB:3TBF"
SQ SEQUENCE 612 AA; 67444 MW; 5B358856A65E7245 CRC64;
MCGIVGANST RNVTNILIEG LKKLEYRGYD SAGLAIIDDK NNIDICKEVG KVIELEKSVH
NLANFKGDIG IAHTRWATHG KPSKNNSHPH ASESFCIVHN GVIENFAELK KVLINDGYKF
KSDTDTEVIA HLLQKEWRDN FSIVDNIKYI MAMLKGAYAV AIISQKFSDK IVAVRSGSPL
VIGVGIDENF ISSDALSLLP VTNKFSYLDE GDIAIISKDN VEVFDNNGAA KNLEVEEYNY
SSSSASKDGY KHYMLKEIYE QPEAVSNTIL ASLADGEISL DSFDKRAKEL FEKTKHICIV
ACGTSYNAGM TAKYWIEKYA KVPCSVEIAS EIRYRDNVVV DGSLFVSISQ SGETADTLES
LRKSKKQNYV GSMCICNVPN SSLVRESDIA FMTKAGVEIG VASTKAFTTQ LVALAIFTLV
IAKLKNSLTD QQIAKYTEEL KNIRALVMGA LKLDTEIDQI SEYFSDKEHT IFLGRGLYYP
IAIEGALKLK EISYIHAEAY PSGELKHGPL ALVDKNMPIV AVVPNDELLD KTLSNLQEVH
ARGGKLILFV DKAVKERVNF DNSIVLELDA GHDFSAPVVF TIPLQLLSYH VAIIKGTDVD
QPRNLAKSVT VE
