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Database: UniProt
Entry: U2E4G0_9GAMM
LinkDB: U2E4G0_9GAMM
Original site: U2E4G0_9GAMM 
ID   U2E4G0_9GAMM            Unreviewed;       610 AA.
AC   U2E4G0;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
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:ERJ18736.1};
GN   ORFNames=SSPSH_002229 {ECO:0000313|EMBL:ERJ18736.1};
OS   Salinisphaera shabanensis E1L3A.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Salinisphaerales;
OC   Salinisphaeraceae; Salinisphaera.
OX   NCBI_TaxID=1033802 {ECO:0000313|EMBL:ERJ18736.1, ECO:0000313|Proteomes:UP000006242};
RN   [1] {ECO:0000313|EMBL:ERJ18736.1, ECO:0000313|Proteomes:UP000006242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E1L3A {ECO:0000313|EMBL:ERJ18736.1,
RC   ECO:0000313|Proteomes:UP000006242};
RX   PubMed=21705588; DOI=10.1128/JB.05459-11;
RA   Antunes A., Alam I., Bajic V.B., Stingl U.;
RT   "Genome sequence of Salinisphaera shabanensis, a gammaproteobacterium from
RT   the harsh, variable environment of the brine-seawater interface of the
RT   Shaban Deep in the Red Sea.";
RL   J. Bacteriol. 193:4555-4556(2011).
RN   [2] {ECO:0000313|EMBL:ERJ18736.1, ECO:0000313|Proteomes:UP000006242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E1L3A {ECO:0000313|EMBL:ERJ18736.1,
RC   ECO:0000313|Proteomes:UP000006242};
RX   PubMed=24324765;
RA   Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U.,
RA   Bajic V.B.;
RT   "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples from
RT   the Red Sea Extremophiles.";
RL   PLoS ONE 8:E82210-E82210(2013).
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:ERJ18736.1}.
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DR   EMBL; AFNV02000015; ERJ18736.1; -; Genomic_DNA.
DR   RefSeq; WP_006914552.1; NZ_AFNV02000015.1.
DR   AlphaFoldDB; U2E4G0; -.
DR   STRING; 1033802.SSPSH_002229; -.
DR   eggNOG; COG0449; Bacteria.
DR   OrthoDB; 9761808at2; -.
DR   Proteomes; UP000006242; 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:UP000006242};
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..435
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          459..600
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        605
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   610 AA;  65945 MW;  A4AED2D99A5236D0 CRC64;
     MCGIVGASAQ RNVEPILLEG LRRLEYRGYD SAGMALVNDG ALDRTRAVGK VQALADKLAE
     APRPGVLGIA HTRWATHGGV SETNAHPHVS SSRIAVVHNG IIENFEPLRE RLREAGYEFT
     SQTDTEVVAH LIDSHLGDSG DLATAVRTTV DELDGAYALA VVCRDDPHTL VATRSGSPLV
     LGVGIGEHFV ASDVAALLPV TRDFIYLEEG DLVVLTHERY TIIDGSGAEV DRPVKESGLS
     LSATEKGSYR HFMLKEIYEQ PRALAETWQG RVSADDIFAS SISAEARELL DGVEYIHIVA
     CGTSHHAGLV ARYWLEAMAR IPCNVELASE YRYRDPVVPK NCLFVTLSQS GETADTLAAL
     RYAKSLGTGD GGYLATLAIC NKPESSLTRE SDLVLMTHAG PEIGVASTKA FTTQLLCLLL
     LTGMLERSAD DRRALAEEIH QLATSVERVL ELDNAIRHLA EEFVDKDHAL FLGRGPMYPI
     AMEGALKLKE ISYLHAEAYA AGELKHGPLA LVDEKMPVIA IAPKNDWLEK VKSNLQEVRA
     RGGKLYVFAD AASGLDTGPG ITVLDMPHVD ETLAPIAYTV PLQLLAYHVA VAKGTDVDQP
     RNLAKSVTVE
//
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