ID A0A1Y4H2M5_9FIRM Unreviewed; 608 AA. AC A0A1Y4H2M5; DT 30-AUG-2017, integrated into UniProtKB/TrEMBL. DT 30-AUG-2017, sequence version 1. DT 17-JUN-2020, entry version 8. DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|HAMAP-Rule:MF_00164, ECO:0000256|SAAS:SAAS01229024}; 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; 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|HAMAP-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:SAAS01229031}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164, ECO:0000256|SAAS:SAAS01229030}; KW Transferase {ECO:0000256|HAMAP-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 //