ID I2F217_9BACT Unreviewed; 608 AA.
AC I2F217;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|ARBA:ARBA00016090, ECO:0000256|HAMAP-Rule:MF_00164};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916, ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=GFAT {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=Hexosephosphate aminotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
GN Name=glmS {ECO:0000256|HAMAP-Rule:MF_00164};
GN ORFNames=Theba_0236 {ECO:0000313|EMBL:AFK05970.1};
OS Mesotoga prima MesG1.Ag.4.2.
OC Bacteria; Thermotogota; Thermotogae; Kosmotogales; Kosmotogaceae; Mesotoga.
OX NCBI_TaxID=660470 {ECO:0000313|EMBL:AFK05970.1, ECO:0000313|Proteomes:UP000002881};
RN [1] {ECO:0000313|EMBL:AFK05970.1, ECO:0000313|Proteomes:UP000002881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mesG1.Ag.4.2 {ECO:0000313|Proteomes:UP000002881};
RX PubMed=22798451;
RA Zhaxybayeva O., Swithers K.S., Foght J., Green A.G., Bruce D., Detter C.,
RA Han S., Teshima H., Han J., Woyke T., Pitluck S., Nolan M., Ivanova N.,
RA Pati A., Land M.L., Dlutek M., Doolittle W.F., Noll K.M., Nesbo C.L.;
RT "Genome Sequence of the Mesophilic Thermotogales Bacterium Mesotoga prima
RT MesG1.Ag.4.2 Reveals the Largest Thermotogales Genome To Date.";
RL Genome Biol. Evol. 4:700-708(2012).
CC -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC {ECO:0000256|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:0000256|ARBA:ARBA00001031, ECO:0000256|HAMAP-
CC Rule:MF_00164};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00164}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003532; AFK05970.1; -; Genomic_DNA.
DR RefSeq; WP_014730132.1; NC_017934.1.
DR AlphaFoldDB; I2F217; -.
DR STRING; 660470.Theba_0236; -.
DR KEGG; mpg:Theba_0236; -.
DR eggNOG; COG0449; Bacteria.
DR HOGENOM; CLU_012520_5_2_0; -.
DR Proteomes; UP000002881; 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; cd00714; GFAT; 1.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR HAMAP; MF_00164; GlmS; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR005855; GFAT.
DR InterPro; IPR047084; GFAT_N.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR NCBIfam; TIGR01135; glmS; 1.
DR PANTHER; PTHR10937; GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING; 1.
DR PANTHER; PTHR10937:SF0; GLUTAMINE--FRUCTOSE-6-PHOSPHATE TRANSAMINASE (ISOMERIZING); 1.
DR Pfam; PF13522; GATase_6; 1.
DR Pfam; PF01380; SIS; 2.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS51464; SIS; 2.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW Rule:MF_00164}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000002881};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00164}.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT DOMAIN 2..218
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 285..424
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 457..598
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT ACT_SITE 2
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT ACT_SITE 603
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 608 AA; 66795 MW; 8CF8D0161DF8B8D5 CRC64;
MCGIVGMVGK DLTIRKLVDA LKKLEYRGYD SAGVAVNSRD GLRVMKAVGM ISSLEKLLGD
DLDSNVIQGI AHTRWATHGG PSDFNAHPHT DCTGKIAVVH NGIIENYDVL RLDLEKKGHI
FKSVTDTETI AHLIEEHYSG DIISAVRHAL LDLEGAYAIG VVHQDHPDVI VAARKGSPLV
VGSTGESGFL ASDVTPLLKY IRDVYFVDDG EFVVIRPEGI SISRMDGTSV RKPSTKITWS
EDSAEKSGYE HFMLKEIFEE PQTLRNALMG RIRGGVPNFN EIEHLREEIE KARSLTILAC
GTSFHAGLVF QRFLQDYTEI RAEVEVASEF RYRRLQEGFS DLVVAISQSG ETADTLEGIR
KAKKLGTKII SLTNVVGSTI SRESDAVIYI NAGPEIGVAA TKTYVAQLAV LLLLGAAIAD
IAGRSGFDIP KIVNELEGMP TVFENTLPTA DEQCKRLAAE HSDYKHFMYI GRGYSYASAL
EGALKLKEIS YIHASGYQAG ELKHGPIALL DKDFPVFAIV PEDELKSKMI SNIMETRARD
AKVLALCSEN DKEVAKSVNS RIEVPRVLDP IYPLVMSPYL QLFAYYIAVK KGLDPDKPRN
LAKSVTVE
//
