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Database: UniProt
Entry: G4QN09_GLANF
LinkDB: G4QN09_GLANF
Original site: G4QN09_GLANF 
ID   G4QN09_GLANF            Unreviewed;       610 AA.
AC   G4QN09;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 65.
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:AEP31428.1};
GN   OrderedLocusNames=GNIT_3334 {ECO:0000313|EMBL:AEP31428.1};
OS   Glaciecola nitratireducens (strain JCM 12485 / KCTC 12276 / FR1064).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Glaciecola.
OX   NCBI_TaxID=1085623 {ECO:0000313|EMBL:AEP31428.1, ECO:0000313|Proteomes:UP000009282};
RN   [1] {ECO:0000313|EMBL:AEP31428.1, ECO:0000313|Proteomes:UP000009282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 12485 / KCTC 12276 / FR1064
RC   {ECO:0000313|Proteomes:UP000009282};
RX   PubMed=22123761; DOI=10.1128/JB.06296-11;
RA   Bian F., Qin Q.L., Xie B.B., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA   Chen X.L., Zhou B.C., Zhang Y.Z.;
RT   "Complete genome sequence of seawater bacterium Glaciecola nitratireducens
RT   FR1064T.";
RL   J. Bacteriol. 193:7006-7007(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; CP003060; AEP31428.1; -; Genomic_DNA.
DR   RefSeq; WP_014110299.1; NC_016041.1.
DR   AlphaFoldDB; G4QN09; -.
DR   STRING; 1085623.GNIT_3334; -.
DR   KEGG; gni:GNIT_3334; -.
DR   eggNOG; COG0449; Bacteria.
DR   HOGENOM; CLU_012520_5_2_6; -.
DR   OrthoDB; 9761808at2; -.
DR   Proteomes; UP000009282; 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:UP000009282};
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..219
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;  66790 MW;  4BE70693DEFE800B CRC64;
     MCGIVGAIAE RNVVEILLEG LRRLEYRGYD SAGVALLDGE GNLKRERQVG KVKALSDAII
     AKPIKGATGI AHTRWATHGG VNEKNAHPHF SNERIAVVHN GIIENYEALR RDLQAKGYTF
     GSDTDTETIA HTVHEEVKKG KDLLLAVQDS VKQFHGAYGT VIMDKEDANR VVVARSGSPL
     VIGLGIGENF IASDQMALLP VTRRFIFLEE GDVAEITRTS VTIYDHNGDK VEREVFDSEL
     EHDAGDKGGY RHYMLKEIHE QPTVVRNTLQ GRLGETDLVE GIFGAGSEDI LKDIKHVQII
     ACGTSYHSGM TARYWLEQYA NVSCNVEIAS EFRYRKSVVH PNSLIVTISQ SGETADTLAA
     LRLAKQNGYK SSLTICNVPG SSLVRESDMA FMTLAGAEIG VASTKAFTTQ LTAFLMLTLA
     IGKYNGMLAA DKKAIIDGLH SLPTKLEETL TLTNGIEQLA EEFADKQHSL FLGRGDQYPI
     AMEGALKLKE ISYIHAEAYA SGELKHGPLA LIDEEMPVIV VAPNNELLEK LKSNVEEVRA
     RGGIMYVFAD KEAQFASDET MRVINVPHCE APIAPIVYTL PLQLLSYYVA VIKGTDVDQP
     RNLAKSVTVE
//
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