ID   YM084_YEAS7             Reviewed;         714 AA.
AC   A6ZME2;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=SCY_4254;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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.
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DR   EMBL; AAFW02000020; EDN64472.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZME2; -.
DR   SMR; A6ZME2; -.
DR   EnsemblFungi; EDN64472; EDN64472; SCY_4254.
DR   HOGENOM; CLU_012520_5_2_1; -.
DR   UniPathway; UPA00113; UER00528.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
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:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR   CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR035466; GlmS/AgaS_SIS.
DR   InterPro; IPR035490; GlmS/FrlB_SIS.
DR   InterPro; IPR005855; GlmS_trans.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF53697; SSF53697; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS51464; SIS; 2.
PE   3: Inferred from homology;
KW   Aminotransferase; Glutamine amidotransferase; Repeat; Transferase.
FT   CHAIN           1..714
FT                   /note="Putative glutamine--fructose-6-phosphate
FT                   aminotransferase [isomerizing]"
FT                   /id="PRO_0000377676"
FT   DOMAIN          2..321
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT   DOMAIN          387..526
FT                   /note="SIS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT   DOMAIN          559..704
FT                   /note="SIS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT   REGION          266..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..282
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        2
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
SQ   SEQUENCE   714 AA;  79816 MW;  9E672D9EB22FE108 CRC64;
     MCGIFGYCNF LIEKTRGEII DTLIEGLQAL EYKEYDSSGI SIQGDELKSL NIYKQTGKIS
     SLKEEIDLYN LNKNLPFISH CGIAHTRRAT HGGLRRANCH PHNSDPSNEF VVVHNGVITN
     FANLKALLVA KGYVFKSDTD TECIPKLYKH IYDTSIELGY NLDFHVLTNL VLKELEGSYG
     LLCTSSHFPD EVVAARKGSP LVIGVKGKTD MDVNFVEVEY LDQEEDYLKL NTQTKSSGNV
     LAAAPVKYNT CLRKSPPLRS QYLRNSTTST FNHGSSTETP AENGLPRPME FYLSSDCASL
     ARYVSKVVYL EDNDIAHIYD GELHIHCSKI GSEDFSFRTE LSKIKKGPYD NFMQKEIYEQ
     CETTKNVMRG RVDAFTNRVV LGGLENWLTE LRRAKRIIMI ASKASFHSCL AARPIFEELM
     EVPVNVELAL DFVDRNCCIF RNDVCIFVSR SGETTDTINA LNYCIKKEAV TIGVVNCSGS
     SISRFTHCGV HTNTGPEKGI ATTKSYTSQY IALVMIALWM SEDLVSKIER RKEIIQALTI
     VPSQIKEVLE LEPLIIELCD KKLKQHDTFL LLGRGYQFAS ALEGASKMKE ISYVHSESIL
     TNELGHRVLA VASDNPPIIA FATKDAFSPK IASCIDQIIE RKGNPIIICN KGHKIWEQDK
     QKGNVVTLEV PQTVDCLQGI LNVIPLQLIS YWLAIKKDIG VDLPRDSAMS APDI