ID Q875Y2 PRELIMINARY; PRT; 724 AA. AC Q875Y2; DT 01-JUN-2003 (TrEMBLrel. 24, Created) DT 01-JUN-2003 (TrEMBLrel. 24, Last sequence update) DT 01-MAR-2004 (TrEMBLrel. 26, Last annotation update) DE GFA1. OS Saccharomyces castellii (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Naumovia. OX NCBI_TaxID=27288; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CBS4309; 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 RT of duplicated genes."; RL Nature 421:848-852(2003). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CBS4309; RA Langkjaer R.B., Cliften P.F., Johnston M., Piskur J.; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Controls the flux of glucose into the hexosamine CC pathway. Most likely involved in regulating the availability of CC precursors for N- and O-linked glycosylation of proteins (By CC similarity). CC -!- CATALYTIC ACTIVITY: L-glutamine + D-fructose 6-phosphate = L- CC glutamate + D-glucosamine 6-phosphate. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SIMILARITY: In the C-terminal section; belongs to the SIS family. CC GFAT subfamily. 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; -. DR HSSP; P17169; 1MOQ. DR MEROPS; C44.971; -. DR GO; GO:0005737; C:cytoplasm; IEA. DR GO; GO:0030288; C:periplasmic space (sensu Gram-negative Bact...; IEA. DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase...; IEA. DR GO; GO:0005529; F:sugar binding; IEA. DR GO; GO:0005215; F:transporter activity; IEA. DR GO; GO:0016051; P:carbohydrate biosynthesis; IEA. DR GO; GO:0008152; P:metabolism; IEA. DR GO; GO:0006810; P:transport; IEA. DR InterPro; IPR000583; GATase_2. DR InterPro; IPR005855; GlmS_trans. DR InterPro; IPR001638; SBP_bac_3. DR InterPro; IPR001347; SIS. DR Pfam; PF00310; GATase_2; 1. DR Pfam; PF01380; SIS; 2. DR TIGRFAMs; TIGR01135; glmS; 1. DR PROSITE; PS00443; GATASE_TYPE_II; UNKNOWN_1. DR PROSITE; PS01039; SBP_BACTERIAL_3; 1. KW Aminotransferase; Glutamine amidotransferase; Transferase. SQ SEQUENCE 724 AA; 80712 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 //