ID A0A2B7GZ94_9EURY Unreviewed; 596 AA.
AC A0A2B7GZ94;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|HAMAP-Rule:MF_00164};
DE EC=2.6.1.16 {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 ECO:0000313|EMBL:PGF18015.1};
GN ORFNames=CP556_19195 {ECO:0000313|EMBL:PGF18015.1};
OS Natrinema sp. CBA1119.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1608465 {ECO:0000313|EMBL:PGF18015.1, ECO:0000313|Proteomes:UP000223005};
RN [1] {ECO:0000313|EMBL:PGF18015.1, ECO:0000313|Proteomes:UP000223005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBA1119 {ECO:0000313|EMBL:PGF18015.1,
RC ECO:0000313|Proteomes:UP000223005};
RA Roh S.W., Kim Y.B., Kim J.Y.;
RT "Genome sequences of Natrinema thermophila CBA1119T.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PGF18015.1}.
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DR EMBL; PDBS01000001; PGF18015.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7GZ94; -.
DR OrthoDB; 372195at2157; -.
DR Proteomes; UP000223005; Unassembled WGS sequence.
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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
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 280..422
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 446..586
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 591
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 596 AA; 63867 MW; 72CC37969AB64C7B CRC64;
MCGIIGYTGT ERVASDILLT GLSGLEYRGY DSAGLSVSGE SLMVYKRRGE VSALEAAVPD
EGIDGTAGIG HTRWSTHGPP TDENAHPHTD CTESVAVVHN GIIENYQSLR DELEAGEHTF
ESATDTEVIP HLIENALTTG ASREEAFREA VSRLDGSYAI AAVFSDSETV YAARHESPLV
LGIGDDGHYL ASDVPAFIEY TDRVVYLDDG QFARINPAGI VVTDAQGAIV ETAIETVAWD
PEDAGKSGYD HYMLKEIHEQ PRAIRQCLRQ RVTELDGDVT IEELASLDCD GPVQFVACGT
SYHAACYGAQ LLREWDVSAQ CFLASEYDAA SIPVSDGTLV VGVTQSGETA DTMRALRAAN
RTGATTLALT NTVGSSAVRE CDHAMLIRAG PEISVAATKT FASQQVALAM LASVLSETCS
APPVKRLRTL PDQVQWVLDT SNARSIAETY EDADAYFFIG RGYNAPVARE GALKMKEITY
KHAEGFAAGE LKHGPLAMVS DRTPVFALVT GDATATRTLG NVTEVEARDA PVIAVTDSPA
DVDRYVDHVL EVPTAGPRLT PILANVQLQL VAYWVANRLG RSIDKPRNLA KSVTVE
//
