ID   YM084_YEAS1             Reviewed;         720 AA.
AC   B3LLX6;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 55.
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=SCRG_01975;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; CH408047; EDV11579.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LLX6; -.
DR   SMR; B3LLX6; -.
DR   EnsemblFungi; EDV11579; EDV11579; SCRG_01975.
DR   HOGENOM; CLU_012520_5_2_1; -.
DR   UniPathway; UPA00113; UER00528.
DR   Proteomes; UP000008335; 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_0000377747"
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;  80557 MW;  D68AA1B784162DD9 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 GSEDFSFRTV QKLELELSKI KKGPYDNFMQ
     KEIYEQCETT KNVMRGRVDA FTNRVVLGGL ENWLTELRRA KRIIMIASKS SFHSCLAARP
     IFEELMEVPV NVELALDFVD RNCCIFRNDV CIFVSRSGET TDTINALNYC IKKEAVTIGV
     VNCSGSSISR FTHCGVHTNT GPEKGIATTK SYTSQYIALV MIALWMSEDL VSKIERRKEI
     IQALTIIPSQ IKEVLELEPL IIELCDKKLK QHDTFLLLGR GYQFASALEG ASKMKEISYV
     HSESILTDEL GHRVLAVASD NPPIIAFATK DAFSPKIASC IDQIIERKGN PIIICNKGHK
     IWEQDKQKGN VVTLEVPQTV DCLQGILNVI PLQLISYWLA IKKDIGVDLP RDSAMSAPDI