ID A0A0A6VE79_9BACI Unreviewed; 611 AA.
AC A0A0A6VE79;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 08-NOV-2023, entry version 40.
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 ECO:0000313|EMBL:NEY19042.1};
GN ORFNames=G4D61_03540 {ECO:0000313|EMBL:NEY19042.1}, NG54_01820
GN {ECO:0000313|EMBL:KHD86590.1};
OS Heyndrickxia ginsengihumi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX NCBI_TaxID=363870 {ECO:0000313|EMBL:KHD86590.1, ECO:0000313|Proteomes:UP000030588};
RN [1] {ECO:0000313|EMBL:KHD86590.1, ECO:0000313|Proteomes:UP000030588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M2.11 {ECO:0000313|EMBL:KHD86590.1,
RC ECO:0000313|Proteomes:UP000030588};
RA Toymentseva A., Boulygina E.A., Kazakov S.V., Kayumov I., Suleimanova A.D.,
RA Mardanova A.M., Maria S.N., Sergey M.Y., Sharipova M.R.;
RT "Draft genome of phytase producing Bacillus ginsengihumi strain M2.11.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:NEY19042.1, ECO:0000313|Proteomes:UP000476934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gsoil 114 {ECO:0000313|EMBL:NEY19042.1,
RC ECO:0000313|Proteomes:UP000476934};
RA Feng H.;
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:NEY19042.1, ECO:0000313|Proteomes:UP000476934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gsoil 114 {ECO:0000313|EMBL:NEY19042.1,
RC ECO:0000313|Proteomes:UP000476934};
RA Xie J.;
RT "Bacillus aquiflavi sp. nov., isolated from yellow water of strong flavor
RT Chinese baijiu in Yibin region of China.";
RL Submitted (MAR-2020) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:KHD86590.1}.
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DR EMBL; JRUN01000003; KHD86590.1; -; Genomic_DNA.
DR EMBL; JAAIWK010000003; NEY19042.1; -; Genomic_DNA.
DR RefSeq; WP_025728897.1; NZ_JRUN01000003.1.
DR AlphaFoldDB; A0A0A6VE79; -.
DR STRING; 363870.NG54_01820; -.
DR OrthoDB; 106547at2; -.
DR Proteomes; UP000030588; Unassembled WGS sequence.
DR Proteomes; UP000476934; 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}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000030588};
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 287..426
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 456..601
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT ACT_SITE 606
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 611 AA; 67721 MW; A1EB44E0C4AEB875 CRC64;
MSGIVGYIGK HSAQSILIDC LRRLDYRGYD SAGIAISNFH EIQLRKEKGR VEDLEASLQL
EPIINGNLGI GHTRWASHGT PTISNSHPLC DEEERFFVVH NGIIENYQQL KKFLLEEGYH
FHTDTDTEVI PHLLAHYDTG HFEETVREVI PLLKGTFALA ILSKNDPNQM IALSQNNPLI
IGFGQDEAYL SSDIPALLPY TKDIYPIKNG ELAVLTQTAV EVKTLSGDKV TPKRVHIQWN
HEELELQQYE HYMLKEIMEQ PEAIKRTLKG RLTEDGVAIP ELEGFLHSRN LQSFEKIMIV
GSGTSYHSGI IGKKILDSLI EIPVEVAIAS EFSCEHSTLT DKHLVIVVSQ SGETADTLSA
LKEAKKYGTP TIAITNHWKS TLSRQADCTI YTYEGQELAV AATKAYTSQI TGLVLLAIVL
AKQMNGRGVE QIPVLLDALH SLSEDVEKCL IMTQDAIDQF AQITNDQEKI FIVGRGSDYV
LALEGALKLQ EVAYIHADAY AAGEMKHGTM ALITPGIPVI ALATQHHLRE KTVNNIKEMK
ARDAYVVGIT TIGDDSISSV VDEVMYIPEA HPLLMPILAA IPLQLLAYYA GCVRGYNVDR
PRNLAKSLTV E
//