ID A0A9P3PUK9_LYOSH Unreviewed; 699 AA. AC A0A9P3PUK9; DT 13-SEP-2023, integrated into UniProtKB/TrEMBL. DT 13-SEP-2023, sequence version 1. DT 29-MAY-2024, entry version 5. DE RecName: Full=glutamine--fructose-6-phosphate transaminase (isomerizing) {ECO:0000256|ARBA:ARBA00012916}; DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916}; DE AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000256|ARBA:ARBA00033302}; DE AltName: Full=Hexosephosphate aminotransferase {ECO:0000256|ARBA:ARBA00029805}; GN Name=GFA1 {ECO:0000313|EMBL:GLB42275.1}; GN ORFNames=LshimejAT787_1102900 {ECO:0000313|EMBL:GLB42275.1}; OS Lyophyllum shimeji (Hon-shimeji) (Tricholoma shimeji). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae; Lyophyllum. OX NCBI_TaxID=47721 {ECO:0000313|EMBL:GLB42275.1, ECO:0000313|Proteomes:UP001063166}; RN [1] {ECO:0000313|EMBL:GLB42275.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AT787 {ECO:0000313|EMBL:GLB42275.1}; RA Kobayashi Y., Shibata T., Hirakawa H., Shigenobu S., Nishiyama T., RA Yamada A., Hasebe M., Kawaguchi M.; RT "The genome of Lyophyllum shimeji provides insight into the initial RT evolution of ectomycorrhizal fungal genome."; RL Submitted (JUL-2022) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in amino sugar synthesis (formation of chitin, CC supplies the amino sugars of asparagine-linked oligosaccharides of CC glycoproteins). {ECO:0000256|ARBA:ARBA00003267}. 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}; CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D- CC glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D- CC fructose 6-phosphate: step 1/1. {ECO:0000256|ARBA:ARBA00004775}. 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:GLB42275.1}. 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; BRPK01000011; GLB42275.1; -; Genomic_DNA. DR Proteomes; UP001063166; Unassembled WGS sequence. 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:InterPro. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:TreeGrafter. DR GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic 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 Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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 4: Predicted; KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576}; KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962}; KW Reference proteome {ECO:0000313|Proteomes:UP001063166}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 2..299 FT /note="Glutamine amidotransferase type-2" FT /evidence="ECO:0000259|PROSITE:PS51278" FT DOMAIN 378..517 FT /note="SIS" FT /evidence="ECO:0000259|PROSITE:PS51464" FT DOMAIN 549..689 FT /note="SIS" FT /evidence="ECO:0000259|PROSITE:PS51464" SQ SEQUENCE 699 AA; 77337 MW; 9473C50488D96200 CRC64; MCGIFGYCSF LKEKTRREVL EVLCNGLARQ EYRGYDSAGL CVDGDKAGEV IYFKEVGKVA GLRQKIAASS IDVNKTSISQ VSIAHTRWAT HGPPSEINCH PLRSDPQSEF CVVHNGIVTN SAELRLVLQK RGYKFESETD TEAVAILTKY LYDSRTEKHM TFSDLVKLVL KELEGSFAFV FKSKHFPNEV VTARRGSPLL VGVKTDKKLK VDFVDVEFAG QDSNDTRVDS LQPNSPSALL SPPSANPKVL RTQSRAFMSE DGLPQPIEFF IASDAAAIIE YTKRVLYLED DDIAHIAEGE LHIHRLRRKE EGDQTPGQIA TTRTIETLEL ELAAIMKGKF DTFMQKEIYE QPESVVNTMR GRVNFDENRI TLGGLRAYLP IIRRGRRIVF IACGTSYHSC LATRAIFEEL TEIPVSVELA SDFLDRKTPI FRDDVCVFLS QSGETADTIL ALRYCLERGA LCVGVVNTVG STLSRETHCG VHINAGPEVG VASTKAYTSQ YVALLMIALQ LSEDRISFTE RRNQIINGLH ALPGQIKKVL DLDKALQQLA ADISGNKSLL IMGRGYQHAT CLEGALKIKE ISYMHSEGIL AGELKHGPLA LIDENMPVII IMTQDSLYPK VQSAFAQITA RKAQPIVLCN EDDTGIPAGA KTIRVPKTVD CLQGLLNIIP LQLLSYHLAV RNGCDVDFPR NLAKSVTVE //