ID Q875Y2_NAUCA Unreviewed; 724 AA. AC Q875Y2; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 02-OCT-2024, entry version 86. 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}; OS Naumovozyma castellii (Yeast) (Saccharomyces castellii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Naumovozyma. OX NCBI_TaxID=27288 {ECO:0000313|EMBL:AAO32496.1}; RN [1] {ECO:0000313|EMBL:AAO32496.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CBS4309 {ECO:0000313|EMBL:AAO32496.1}; RA Langkjaer R.B., Cliften P.F., Johnston M., Piskur J.; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAO32496.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CBS4309 {ECO:0000313|EMBL:AAO32496.1}; RX PubMed=12594514; DOI=10.1038/nature01419; RA Langkjaer R.B., Cliften P.F., Johnston M., Piskur J.; RT "Yeast genome duplication was followed by asynchronous differentiation of RT duplicated genes."; RL Nature 421:848-852(2003). 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 --------------------------------------------------------------------------- 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; AY144933; AAO32496.1; -; Genomic_DNA. DR AlphaFoldDB; Q875Y2; -. DR OMA; ASEYRYA; -. DR UniPathway; UPA00113; UER00528. DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro. DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-EC. 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:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway. 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; 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 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 Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 2..325 FT /note="Glutamine amidotransferase type-2" FT /evidence="ECO:0000259|PROSITE:PS51278" FT DOMAIN 397..536 FT /note="SIS" FT /evidence="ECO:0000259|PROSITE:PS51464" FT DOMAIN 569..714 FT /note="SIS" FT /evidence="ECO:0000259|PROSITE:PS51464" SQ SEQUENCE 724 AA; 80713 MW; 5883A8BFDDD0E3DF CRC64; MCGIFGYCNF LVERSRGEII DTLVEGLERL EYRGYDSTGI AIDGDELDST MIFRQIGKVA ALKEEIKKQN PNRDVTFVSH CGIAHTRWAT HGEPKQVNCH PQRSDPLNSF VIVHNGIITN FRELRTLLVN KGFKFESDTD TECIAKLFKH LYDTNLQNGN ELDFHELTKL VLLELEGSYG LLCKSIHYPN EVIATRKGSP LLIGVKSEKK LKVDFVDVEF PDDNNLGKPE TPLGSATDST VDGITVNGKK HPRSYGVDEA QSSNLLPIAA NEFNLRHSQS RAFLSEDGTP NPVEFFLSSD AASVIKHTKK VLFLEDDDIA HIYDGELHIH RSRREVGASM TRSIQTLEME LAQIMKGPYK HFMQKEIYEQ PESTLNTMRG RIDFENNTLM LGGLKAWLPA IRRARRLIMI ACGTSYHSCL ATRAIFEELS EIPVSVELAS DFLDRKSPVF RDDICVFVSQ SGETADTMLA LNYCLERGAL TVGIVNSVGS SLSRATHCGV HINAGPEIGV ASTKAYTSQY IALVMFALSL SDDRLSKLER RKDIIQGLKL IPGQIKQVLQ LEKKIKKLCE NELKDQKSLL LLGRGYQFAS ALEGALKIKE ISYMHSEGVL AGELKHGVLA LVDENLPIIA FGTRDSLFPK VVSSIEQVTA RKGHPIVICN ENDEVWAKKA ESIHLVTLEV PQTVDCLQGL LNIIPLQLMS YWLAVNKGID VDFPRNLAKS VTVE //