ID   YM084_YEAST             Reviewed;         262 AA.
AC   A2P2R3; D6VZQ7; E9P8R5; Q3E7C0; Q6B308; Q6WV01;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-NOV-2023, entry version 101.
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   OrderedLocusNames=YMR084W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 246-262, AND CONFIRMATION OF
RP   FRAMESHIFT.
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA   Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA   Gates K., Gaffney T.D., Philippsen P.;
RT   "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT   comparison to the genome of a related fungus: Ashbya gossypii.";
RL   Genome Biol. 4:R45.1-R45.13(2003).
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 S288c has a frameshift in position
CC       258, which disrupts the gene coding for this protein and produces two
CC       ORFs YMR084W and YMR085W. A contiguous sequence for this protein can be
CC       found in strain YJM789 (AC A6ZME2). {ECO:0000305}.
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DR   EMBL; Z49259; CAA89230.1; -; Genomic_DNA.
DR   EMBL; AY692572; AAT92591.1; -; Genomic_DNA.
DR   EMBL; AY268137; AAR26283.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09981.1; -; Genomic_DNA.
DR   PIR; S54459; S54459.
DR   RefSeq; NP_013801.1; NM_001182583.1.
DR   AlphaFoldDB; A2P2R3; -.
DR   SMR; A2P2R3; -.
DR   BioGRID; 35259; 80.
DR   STRING; 4932.YMR084W; -.
DR   PaxDb; 4932-YMR084W; -.
DR   EnsemblFungi; YMR084W_mRNA; YMR084W; YMR084W.
DR   GeneID; 855108; -.
DR   KEGG; sce:YMR084W; -.
DR   AGR; SGD:S000004689; -.
DR   SGD; S000004689; YMR084W.
DR   VEuPathDB; FungiDB:YMR084W; -.
DR   eggNOG; KOG1268; Eukaryota.
DR   GeneTree; ENSGT00940000173234; -.
DR   HOGENOM; CLU_012520_6_2_1; -.
DR   InParanoid; A2P2R3; -.
DR   OrthoDB; 1705390at2759; -.
DR   BioCyc; YEAST:G3O-32784-MONOMER; -.
DR   UniPathway; UPA00113; UER00528.
DR   BioGRID-ORCS; 855108; 1 hit in 10 CRISPR screens.
DR   PRO; PR:A2P2R3; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; A2P2R3; Protein.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IBA:GO_Central.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central.
DR   CDD; cd00714; GFAT; 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; IPR029055; Ntn_hydrolases_N.
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   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Glutamine amidotransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..262
FT                   /note="Putative glutamine--fructose-6-phosphate
FT                   aminotransferase [isomerizing]"
FT                   /id="PRO_0000269757"
FT   DOMAIN          2..262
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   262 AA;  29272 MW;  CAEC5457BEB33DFD CRC64;
     MCGIFGYCNF LIEKTRGEII DTLIEGLQAL EYKEYDSSGI SIQGDELESL NIYKQTGKIS
     SLKEEIDLYN LNKNLPFISH CGIAHTRRAT HGGLRRANCH PHNSDPSNEF VVVHNGVITN
     FANLKALLMA KGYVFKSDTD TECIPKLYKH IYDTSIELGY NLDFHVLTNL VLKELEGSYG
     LLCTSSHFPD EVVAARKGSP LVIGVKGKTD MDVNFVEVEY LDQEEDYLKL NTQTKSSGNV
     LAAAPVKYNT CLRKSPPFVH NT
//