ID   YM084_YEAS2             Reviewed;         720 AA.
AC   C7GL41;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   25-MAY-2022, entry version 48.
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=C1Q_01026;
OS   Saccharomyces cerevisiae (strain JAY291) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=574961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAY291;
RX   PubMed=19812109; DOI=10.1101/gr.091777.109;
RA   Argueso J.L., Carazzolle M.F., Mieczkowski P.A., Duarte F.M., Netto O.V.C.,
RA   Missawa S.K., Galzerani F., Costa G.G.L., Vidal R.O., Noronha M.F.,
RA   Dominska M., Andrietta M.G.S., Andrietta S.R., Cunha A.F., Gomes L.H.,
RA   Tavares F.C.A., Alcarde A.R., Dietrich F.S., McCusker J.H., Petes T.D.,
RA   Pereira G.A.G.;
RT   "Genome structure of a Saccharomyces cerevisiae strain widely used in
RT   bioethanol production.";
RL   Genome Res. 19:2258-2270(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   -!- SEQUENCE CAUTION:
CC       Sequence=EEU08477.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; ACFL01000033; EEU08477.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; C7GL41; -.
DR   SMR; C7GL41; -.
DR   UniPathway; UPA00113; UER00528.
DR   Proteomes; UP000008073; 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..720
FT                   /note="Putative glutamine--fructose-6-phosphate
FT                   aminotransferase [isomerizing]"
FT                   /id="PRO_0000393411"
FT   DOMAIN          2..321
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT   DOMAIN          393..532
FT                   /note="SIS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT   DOMAIN          565..710
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   720 AA;  80561 MW;  FCDCAB9E434094A6 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 EDNDTAHIYD GELHIHCSKI GSEDFSFRTV QKLELELSKI KKGPYDNFMQ
     KEIYEQCETT KNVMRGRVDA FTNRVVLGGL ENWLTELRRA KRIIMIASKS SFHSCLAARP
     IFEELMEVPV NVELALDFVD RNCCIFRNDV CIFVSRSGET TDTINALNYC IKKEAVTIGV
     VNCSGSSISR FTHCGVHTNT GPEKGIATTK SYTSQYIALV MIALWMSEDL VSKIERRKEI
     IQALTIVPSQ IKEVLELEPL IIELCDKKLK QHDTFLLLGR GYQFASALEG ASKMKEISYV
     HSESILTDEL GHRVLAVTSD NPPIIAFATK DAFSPKIASC IDQIIERKGN PIIICNKGHK
     IWEQDKQKGN VVTLEVPQTV DCLQGILNVI PLQLISYWLA IKKDIGVDLP RDSAMSAPDI