ID   A0A1Y4H2M5_9FIRM        Unreviewed;       608 AA.
AC   A0A1Y4H2M5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   25-MAY-2022, entry version 14.
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=B5F37_03875 {ECO:0000313|EMBL:OUP02344.1};
OS   Drancourtella sp. An210.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Drancourtella; unclassified Drancourtella.
OX   NCBI_TaxID=1965589 {ECO:0000313|EMBL:OUP02344.1, ECO:0000313|Proteomes:UP000196338};
RN   [1] {ECO:0000313|Proteomes:UP000196338}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An210 {ECO:0000313|Proteomes:UP000196338};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:OUP02344.1}.
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DR   EMBL; NFJS01000004; OUP02344.1; -; Genomic_DNA.
DR   EnsemblBacteria; OUP02344; OUP02344; B5F37_03875.
DR   Proteomes; UP000196338; 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; cd05008; SIS_GlmS_GlmD_1; 1.
DR   CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   HAMAP; MF_00164; GlmS; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR035466; GlmS/AgaS_SIS.
DR   InterPro; IPR035490; GlmS/FrlB_SIS.
DR   InterPro; IPR005855; GlmS_trans.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF53697; SSF53697; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR01135; glmS; 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          285..424
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          457..598
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        603
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   608 AA;  67412 MW;  F5B5B358B1B7F263 CRC64;
     MCGIVGYIGT EQAAPILLSG LSKLEYRGYD SAGIAVYDGT KVNVAKTKGR LKVLTEQTHD
     GQKLPGKLGI GHTRWATHGS PSDMNAHPHA NSDVSIVVVH NGIIENYIKL KRKLEKKGYT
     FVSETDTEVI AHLLDYYYRG NPLEAVTKIM HRMEGSYALG ILFKDHPNEL YAVRKDSPLI
     VGHTKGGSII ASDVPAVLKY TRDVYFIENE EIVRMTESEM EFFTVDEEPL QKEPVHIDWD
     ENAAEKGGYE HFMLKEMYEQ PKAITDTFSP RLKNGDIVID ELGMSDGDIR EIRKIMIVAC
     GSAYHTGVTG KYVFEGLARI PVEVDLASEF RYRDPILDEG TLVVVISQSG ETADSLAALR
     EAKARGRRVL GIVNVVGSSI AREADNVMYT WAGPEIAVAT TKAYSCQLIA LYLLAMKFAK
     VRGMVSESEL EEMITELKKI PAQVEMLLNN KDRIQKFANR YLAAKNIFFI GRGIDYAISL
     EGSLKLKEIS YIHSEAYAAG ELKHGTISLI EDGTLVTALV TQEELYKKTI SNIVEVKTRG
     AFVMAVTNTG NTDVEKAADY VVYIPKTNKY FANSLAIIPL QLFGYYVSVG RGCDVDKPRN
     LAKSVTVE
//