ID   A0A1Y4H2M5_9FIRM        Unreviewed;       608 AA.
AC   A0A1Y4H2M5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   05-DEC-2018, entry version 5.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|HAMAP-Rule:MF_00164, ECO:0000256|SAAS:SAAS00887593};
DE            EC=2.6.1.16 {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; Clostridiales; Ruminococcaceae;
OC   Drancourtella.
OX   NCBI_TaxID=1965589 {ECO:0000313|EMBL:OUP02344.1, ECO:0000313|Proteomes:UP000196338};
RN   [1] {ECO:0000313|EMBL:OUP02344.1, ECO:0000313|Proteomes:UP000196338}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An210 {ECO:0000313|EMBL:OUP02344.1,
RC   ECO:0000313|Proteomes:UP000196338};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T.,
RA   Cizek A., 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,
CC       converting fructose-6P into glucosamine-6P using glutamine as a
CC       nitrogen source. {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,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725,
CC         ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={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       ECO:0000256|SAAS:SAAS00887591}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OUP02344.1}.
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DR   EMBL; NFJS01000004; OUP02344.1; -; Genomic_DNA.
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   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.
DR   PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR   Pfam; PF01380; SIS; 2.
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|HAMAP-Rule:MF_00164};
KW   Complete proteome {ECO:0000313|Proteomes:UP000196338};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164,
KW   ECO:0000256|SAAS:SAAS00887588};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00164}.
FT   INIT_MET      1      1       Removed. {ECO:0000256|HAMAP-Rule:
FT                                MF_00164}.
FT   DOMAIN        2    218       Glutamine amidotransferase type-2.
FT                                {ECO:0000259|PROSITE:PS51278}.
FT   DOMAIN      285    424       SIS. {ECO:0000259|PROSITE:PS51464}.
FT   DOMAIN      457    598       SIS. {ECO:0000259|PROSITE:PS51464}.
FT   ACT_SITE      2      2       Nucleophile; for GATase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00164}.
FT   ACT_SITE    603    603       For Fru-6P isomerization activity.
FT                                {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
//