ID A0A1P8W9T0_9PLAN Unreviewed; 620 AA. AC A0A1P8W9T0; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 02-JUN-2021, entry version 18. 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:APZ90817.1}; GN ORFNames=Fuma_00401 {ECO:0000313|EMBL:APZ90817.1}; OS Fuerstia marisgermanicae. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Fuerstia. OX NCBI_TaxID=1891926 {ECO:0000313|EMBL:APZ90817.1, ECO:0000313|Proteomes:UP000187735}; RN [1] {ECO:0000313|EMBL:APZ90817.1, ECO:0000313|Proteomes:UP000187735} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NH11 {ECO:0000313|EMBL:APZ90817.1, RC ECO:0000313|Proteomes:UP000187735}; RX PubMed=28066393; DOI=10.3389/fmicb.2016.02079; RA Kohn T., Heuer A., Jogler M., Vollmers J., Boedeker C., Bunk B., Rast P., RA Borchert D., Glockner I., Freese H.M., Klenk H.P., Overmann J., RA Kaster A.K., Rohde M., Wiegand S., Jogler C.; RT "Fuerstia marisgermanicae gen. nov., sp. nov., an Unusual Member of the RT Phylum Planctomycetes from the German Wadden Sea."; RL Front. Microbiol. 7:2079-2079(2016). 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 --------------------------------------------------------------------------- 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; CP017641; APZ90817.1; -; Genomic_DNA. DR RefSeq; WP_077028047.1; NZ_CP017641.1. DR EnsemblBacteria; APZ90817; APZ90817; Fuma_00401. DR KEGG; fmr:Fuma_00401; -. DR OrthoDB; 43416at2; -. DR Proteomes; UP000187735; 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; 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|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:UP000187735}; 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..229 FT /note="Glutamine amidotransferase type-2" FT /evidence="ECO:0000259|PROSITE:PS51278" FT DOMAIN 298..437 FT /note="SIS" FT /evidence="ECO:0000259|PROSITE:PS51464" FT DOMAIN 469..610 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 615 FT /note="For Fru-6P isomerization activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164" SQ SEQUENCE 620 AA; 67755 MW; D96F14B242975121 CRC64; MCGIVGYVGS RPVSDLLLEG LHRLEYRGYD SAGIAVMTDT EIVVRKKSGR VGELAQLIKQ QPVVGSIGIG HTRWATHGET TDENSHPHLG GNGEVVIVHN GVIENYDSLR TQLQTLGYVF RSQTDTEVVA HLIAHHLGEQ LKLSDSEPGV DVCLKAVHTT LDRLKGTYGL CAMFRDCPDT LIAARSGSPL VIGVGKDEYF LASDASPLVG YTQDVVYLAD NEVAVLQPSK MTVAHRTSGS VQPSIQTLDQ VSSDIDLGDY PHYMLKEIFE QPQTIENALR GRLDSEEATA VIGGLNLTAQ QLRTIDRVVL TACGTSWHAG LVGEYLLEEF ARLPTEVEYA SELRYRNPPM SDRTLVFAIT QSGETADTLA AMRECKRKGH PTLAICNVVG STIGREADGG MYLRAGPEIG VASTKAFTSQ VTVLTLLALY LGRMRHLSYP AGKRIIKQLR DMPSKIEEAL KCNDRVAEIA AKYAKYDNYL YLGRLYNFPV ALEGALKLKE ISYIHAEGYP AAEMKHGPIA LVDEQTPSVF IVPKCGIQPK VISNMEEVKA RKGPVIAIAC EGDAEVARIA DDVIYVPDVE EYLQPLVCAI PLQLLSYHVA LLRGCNVDRP RNLAKSVTVE //