ID   A0A5K7S404_9BACT        Unreviewed;       615 AA.
AC   A0A5K7S404;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   27-NOV-2024, entry version 17.
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=AQPE_0342 {ECO:0000313|EMBL:BBE16205.1};
OS   Aquipluma nitroreducens.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC   Aquipluma.
OX   NCBI_TaxID=2010828 {ECO:0000313|EMBL:BBE16205.1, ECO:0000313|Proteomes:UP001193389};
RN   [1] {ECO:0000313|EMBL:BBE16205.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MeG22 {ECO:0000313|EMBL:BBE16205.1};
RX   DOI=10.1099/ijsem.0.004551;
RA   Watanabe M., Kojima H., Fukui M.;
RT   "Aquipluma nitroreducens gen. nov. sp. nov., a novel facultatively
RT   anaerobic bacterium isolated from a freshwater lake.";
RL   Int. J. Syst. Evol. Microbiol. 70:6408-6413(2020).
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; AP018694; BBE16205.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5K7S404; -.
DR   KEGG; anf:AQPE_0342; -.
DR   Proteomes; UP001193389; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:TreeGrafter.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IEA:TreeGrafter.
DR   GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IEA:TreeGrafter.
DR   CDD; cd00714; GFAT; 1.
DR   CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR   CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR   FunFam; 3.40.50.10490:FF:000001; Glutamine--fructose-6-phosphate aminotransferase [isomerizing]; 1.
DR   FunFam; 3.40.50.10490:FF:000002; Glutamine--fructose-6-phosphate aminotransferase [isomerizing]; 1.
DR   FunFam; 3.60.20.10:FF:000006; Glutamine--fructose-6-phosphate aminotransferase [isomerizing]; 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:UP001193389};
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..222
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          292..431
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          464..605
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        610
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   615 AA;  68167 MW;  BD7606D37ED46173 CRC64;
     MCGIVAYIGY SEAFPILING LKHLEYRGYD SSGIALLQKG QTTNIFKKKG KVKELERYCE
     GKDMTGCLGM AHTRWATHGE PNDTNAHPHV SMRRLFTIVH NGIIENYGKL KKDLSEKGYT
     FYSETDTEVL ANLIEYMYVQ GEVLDAEQAV RMALSRVVGA FGLVVMCQAE ALKLIAARRS
     SPLAIGIGQN EYYLASDATP LVEYTQRVVY LDDNDVAILT SNSFTLKTID VDKEKIPEIQ
     KLELSIGALE KNGYDHFMLK EIFEQPETIE ASFRGRINTK NNEIILGRLT DVMPRILEAQ
     RIVLIACGTS WHAALIGEYL IEELARIPVE VEYASEFRYR NPVLSSNDVV LAISQSGETA
     DTLSAVRMAK EHQAMVLGIC NVVGSSMSRE TDAGIYTHAG SEIGVASTKA FTAQVTVLTL
     LALRLARLKQ TIPEERFHAI VTDLLAAPEK IRTILQSSNH IQYIANKYRD AVNALYLGRG
     YLFPVALEGA LKLKEISYIH AEGYAAGEMK HGPIALIDNN IPVVVVAPKD RYYEKVVSNI
     QEVKARKGNV IAVVSMGDNR LKGMVNDVLE IPESDPIVTP LLTVIPLQLF AYYIAVLRGC
     DVDQPRNLAK SVTVE
//