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Database: UniProt
Entry: K8WVI1_9GAMM
LinkDB: K8WVI1_9GAMM
Original site: K8WVI1_9GAMM 
ID   K8WVI1_9GAMM            Unreviewed;       610 AA.
AC   K8WVI1;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
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=OO7_01776 {ECO:0000313|EMBL:EKT61392.1};
OS   Providencia sneebia DSM 19967.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Providencia.
OX   NCBI_TaxID=1141660 {ECO:0000313|EMBL:EKT61392.1, ECO:0000313|Proteomes:UP000010290};
RN   [1] {ECO:0000313|EMBL:EKT61392.1, ECO:0000313|Proteomes:UP000010290}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19967 {ECO:0000313|EMBL:EKT61392.1,
RC   ECO:0000313|Proteomes:UP000010290};
RX   PubMed=23145767; DOI=10.1186/1471-2164-13-612;
RA   Galac M.R., Lazzaro B.P.;
RT   "Comparative genomics of bacteria in the genus Providencia isolated from
RT   wild Drosophila melanogaster.";
RL   BMC Genomics 13:612-612(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   -!- 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:EKT61392.1}.
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DR   EMBL; AKKN01000002; EKT61392.1; -; Genomic_DNA.
DR   RefSeq; WP_008914244.1; NZ_CM001773.1.
DR   AlphaFoldDB; K8WVI1; -.
DR   PATRIC; fig|1141660.3.peg.353; -.
DR   HOGENOM; CLU_012520_5_2_6; -.
DR   OrthoDB; 9761808at2; -.
DR   Proteomes; UP000010290; 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:UP000010290};
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..427
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;  67102 MW;  C28A26951B8A84A6 CRC64;
     MCGIVGAVAQ RDIAEILIEG LRRLEYRGYD SAGLAVVDQE GHLQRLREVG KVQMLAEEAE
     KTPVFGGTGI AHTRWATHGV PSERNAHPHT SEYIAVVHNG IIENYQELKE ELKKLGYVFS
     SETDTEVIAH LVHHEQQKGG SLIEVVQRVI PQLRGAYGTV IMDSRIPELL VAARSGSPLV
     IGLGVGENFL ASDQLALLPV TRRFMYLEEG DIAEITRRSV RIFDHQGQEV EREQIESSVQ
     YDAGDKGVYR HYMQKEIYEQ PMAIKNTLEG HFNKDNGIDL SELGASAQET LSKVEHIQIV
     ACGTSYNAGM VARYWFESLA GIPCDVEIAS EYRYRNPAYR KNSLMITLSQ SGETADTLAA
     LRLSKDLGYL TSLAICNVAG SSLVRESDFA LMTKAGAEIG VASTKAFTTQ LTVLLMLVAY
     MGRLKGAAPE LEENIAHALH ALPARIESML SQDKVIEALA EDFSDKNHAL FLGRGDQYPI
     AVEGALKLKE ISYIHAEAYA AGELKHGPLA LIDADMPVII IAPNNELLEK LKSNIEEVRA
     RGGLLYVFAD QDAGFQASEN MKIISLPHVE ELIAPIFYTV PLQLLSYHVA LIKGTDVDQP
     RNLAKSVTVE
//
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