YM084_YEAS8
ID YM084_YEAS8 Reviewed; 305 AA.
AC C8ZET7;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Putative glutamine--fructose-6-phosphate aminotransferase [isomerizing];
DE Short=GFAT;
DE EC=2.6.1.16;
DE AltName: Full=D-fructose-6-phosphate amidotransferase;
DE AltName: Full=Hexosephosphate aminotransferase;
GN ORFNames=EC1118_1M3_2520g;
OS Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=643680;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lalvin EC1118 / Prise de mousse;
RX PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC -!- FUNCTION: Involved in amino sugar synthesis (formation of chitin,
CC supplies the amino sugars of asparagine-linked oligosaccharides of
CC glycoproteins). {ECO:0000250}.
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 -!- 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.
CC -!- CAUTION: This is a truncated version of a putative glutamine--fructose-
CC 6-phosphate aminotransferase. Strain Lalvin EC1118 has a frameshift in
CC position 258, which disrupts the gene coding for this protein and
CC produces two ORFs. A contiguous sequence for this protein can be found
CC in strain YJM789 (AC A6ZME2). {ECO:0000305}.
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DR EMBL; FN393082; CAY81903.1; -; Genomic_DNA.
DR AlphaFoldDB; C8ZET7; -.
DR SMR; C8ZET7; -.
DR EnsemblFungi; CAY81903; CAY81903; EC1118_1M3_2520g.
DR HOGENOM; CLU_012520_6_2_1; -.
DR UniPathway; UPA00113; UER00528.
DR Proteomes; UP000000286; Chromosome XIII, Scaffold EC1118_1M3.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Glutamine amidotransferase; Transferase.
FT CHAIN 1..305
FT /note="Putative glutamine--fructose-6-phosphate
FT aminotransferase [isomerizing]"
FT /id="PRO_0000393383"
FT DOMAIN 2..305
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT ACT_SITE 2
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
SQ SEQUENCE 305 AA; 34232 MW; 1E04B62B5CFA6BD7 CRC64;
MCGIFGYCNF LIEKTRGEII DTLIEGLQAL EYKEYDSSGI SIQGDELKSL NIYKQTGKIS
SLKEEIDLYN LNKNLPFISH CGITHTRRAT HGGLRRANCH PHNSDPSNEF VVVHNGVITN
FANLKALLVA KGYVFKSDTD TECIPKLYKH IYDTSIELGY NLDFHVLTNL VLKELEGSYG
LLCTSSHFPD EVVAARKGSP LVIGVKGKTD MDVNFVEVEY LDQEEDYLKL NTQTKSSGNV
LAAAPVKYNT CLRKSPPPSF TIPEKLYNFY IQSWLIHRNA SRERLAATHG ILFVIRLCIT
SAVCE
