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Database: UniProt
Entry: E8XHU9_SALT4
LinkDB: E8XHU9_SALT4
Original site: E8XHU9_SALT4 
ID   E8XHU9_SALT4            Unreviewed;       609 AA.
AC   E8XHU9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 69.
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:ADX19653.1};
GN   OrderedLocusNames=STM474_4040 {ECO:0000313|EMBL:ADX19653.1};
OS   Salmonella typhimurium (strain 4/74).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=909946 {ECO:0000313|EMBL:ADX19653.1, ECO:0000313|Proteomes:UP000008978};
RN   [1] {ECO:0000313|EMBL:ADX19653.1, ECO:0000313|Proteomes:UP000008978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4/74 {ECO:0000313|Proteomes:UP000008978};
RX   PubMed=21478351; DOI=10.1128/JB.00394-11;
RA   Richardson E.J., Limaye B., Inamdar H., Datta A., Manjari K.S.,
RA   Pullinger G.D., Thomson N.R., Joshi R.R., Watson M., Stevens M.P.;
RT   "Genome sequences of Salmonella enterica serovar typhimurium, Choleraesuis,
RT   Dublin, and Gallinarum strains of well- defined virulence in food-producing
RT   animals.";
RL   J. Bacteriol. 193:3162-3163(2011).
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}.
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DR   EMBL; CP002487; ADX19653.1; -; Genomic_DNA.
DR   RefSeq; WP_000334066.1; NC_016857.1.
DR   AlphaFoldDB; E8XHU9; -.
DR   SMR; E8XHU9; -.
DR   KEGG; seb:STM474_4040; -.
DR   PATRIC; fig|909946.3.peg.4131; -.
DR   HOGENOM; CLU_012520_5_2_6; -.
DR   OMA; ASEYRYA; -.
DR   Proteomes; UP000008978; 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   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          286..426
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          458..599
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        604
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   609 AA;  66877 MW;  EB758F57B88EE8FB CRC64;
     MCGIVGAIAQ RDVAEILLEG LRRLEYRGYD SAGLAVVDAE GHMTRLRRLG KVQMLAQAAE
     EHPLHGGTGI AHTRWATHGE PSEANAHPHV SEHIVVVHNG IIENHEPLRE ALKARGYTFV
     SETDTEVIAH LVNWELKQGG TLREAVLRAI PQLRGAYGTV IMDTRHPDTL LAARSGSPLV
     IGLGMGENFI ASDQLALLPV TRRFIFLEEG DIAEITRRSV NIFDNTGAEV KRQDIESNLQ
     YDAGDKGIYR HYMQKEIYEQ PNAIKNTLTG RISHGQVDLS ELGPNADELL SKVEHIQILA
     CGTSYNSGMV SRYWFESLAG IPCDVEIASE FRYRKSAVRR NSLMITLSQS GETADTLAGL
     RLSKELGYLG SLAICNVPGS SLVRESDLAL MTNAGTEIGV ASTKAFTTQL TVLLMLVAKL
     SRLKGLDASI EHDIVHGLQA LPSRIEQMLS QDKRIELLAE DFSDKHHALF LGRGDQYPIA
     LEGALKLKEI SYIHAEAYAA GELKHGPLAL IDADMPVIVV APNNELLEKL KSNIEEVRAR
     GGQLYVFADQ DAGFVSNDNM HIIEMPHVEE VIAPIFYTVP LQLLAYHVAL IKGTDVDQPR
     NLAKSVTVE
//
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