GFA1_YEAST
ID GFA1_YEAST Reviewed; 717 AA.
AC P14742; D6VXI4;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=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 Name=GFA1; OrderedLocusNames=YKL104C; ORFNames=YKL457;
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 [GENOMIC DNA].
RC STRAIN=ATCC 26786 / X2180-1A;
RX PubMed=2656689; DOI=10.1016/s0021-9258(18)81857-9;
RA Watzele G., Tanner W.;
RT "Cloning of the glutamine:fructose-6-phosphate amidotransferase gene from
RT yeast. Pheromonal regulation of its transcription.";
RL J. Biol. Chem. 264:8753-8758(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8109175; DOI=10.1002/yea.320091113;
RA Cheret G., Pallier C., Valens M., Daignan-Fornier B., Fukuhara H.,
RA Bolotin-Fukuhara M., Sor F.;
RT "The DNA sequence analysis of the HAP4-LAP4 region on chromosome XI of
RT Saccharomyces cerevisiae suggests the presence of a second aspartate
RT aminotransferase gene in yeast.";
RL Yeast 9:1259-1265(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [4]
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 [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP CLEAVAGE OF INITIATOR METHIONINE, ACTIVE SITE, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=15699032; DOI=10.1074/jbc.m501059200;
RA Dummitt B., Micka W.S., Chang Y.H.;
RT "Yeast glutamine-fructose-6-phosphate aminotransferase (Gfa1) requires
RT methionine aminopeptidase activity for proper function.";
RL J. Biol. Chem. 280:14356-14360(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND THR-334, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-336, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Involved in amino sugar synthesis (formation of chitin,
CC supplies the amino sugars of asparagine-linked oligosaccharides of
CC glycoproteins). {ECO:0000269|PubMed:15699032}.
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 Evidence={ECO:0000269|PubMed:15699032};
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 -!- INDUCTION: The activity of this enzyme increases in presence of mating
CC pheromone (transcriptional regulation).
CC -!- MISCELLANEOUS: Present with 14300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; J04719; AAA34643.1; -; Genomic_DNA.
DR EMBL; X71133; CAA50453.1; -; Genomic_DNA.
DR EMBL; Z28104; CAA81944.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09054.1; -; Genomic_DNA.
DR PIR; S37931; XNBYGM.
DR RefSeq; NP_012818.1; NM_001179670.1.
DR AlphaFoldDB; P14742; -.
DR SMR; P14742; -.
DR BioGRID; 34030; 233.
DR DIP; DIP-5224N; -.
DR IntAct; P14742; 144.
DR MINT; P14742; -.
DR STRING; 4932.YKL104C; -.
DR iPTMnet; P14742; -.
DR MaxQB; P14742; -.
DR PaxDb; P14742; -.
DR PRIDE; P14742; -.
DR EnsemblFungi; YKL104C_mRNA; YKL104C; YKL104C.
DR GeneID; 853757; -.
DR KEGG; sce:YKL104C; -.
DR SGD; S000001587; GFA1.
DR VEuPathDB; FungiDB:YKL104C; -.
DR eggNOG; KOG1268; Eukaryota.
DR GeneTree; ENSGT00940000173234; -.
DR HOGENOM; CLU_012520_5_2_1; -.
DR InParanoid; P14742; -.
DR OMA; ASEYRYA; -.
DR BioCyc; YEAST:YKL104C-MON; -.
DR BRENDA; 2.6.1.16; 984.
DR Reactome; R-SCE-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR UniPathway; UPA00113; UER00528.
DR PRO; PR:P14742; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P14742; protein.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IDA:SGD.
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; IGI:SGD.
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; 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; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
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 1: Evidence at protein level;
KW Aminotransferase; Glutamine amidotransferase; Phosphoprotein;
KW Reference proteome; Repeat; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15699032"
FT CHAIN 2..717
FT /note="Glutamine--fructose-6-phosphate aminotransferase
FT [isomerizing]"
FT /id="PRO_0000135289"
FT DOMAIN 2..318
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT DOMAIN 390..529
FT /note="SIS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 562..707
FT /note="SIS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT ACT_SITE 2
FT /note="For GATase activity"
FT /evidence="ECO:0000269|PubMed:15699032"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 334
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 453..454
FT /note="QS -> HC (in Ref. 1; AAA34643)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="Missing (in Ref. 1; AAA34643)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 717 AA; 80047 MW; 27E5F0D24BDC451A CRC64;
MCGIFGYCNY LVERSRGEII DTLVDGLQRL EYRGYDSTGI AIDGDEADST FIYKQIGKVS
ALKEEITKQN PNRDVTFVSH CGIAHTRWAT HGRPEQVNCH PQRSDPEDQF VVVHNGIITN
FRELKTLLIN KGYKFESDTD TECIAKLYLH LYNTNLQNGH DLDFHELTKL VLLELEGSYG
LLCKSCHYPN EVIATRKGSP LLIGVKSEKK LKVDFVDVEF PEENAGQPEI PLKSNNKSFG
LGPKKAREFE AGSQNANLLP IAANEFNLRH SQSRAFLSED GSPTPVEFFV SSDAASVVKH
TKKVLFLEDD DLAHIYDGEL HIHRSRREVG ASMTRSIQTL EMELAQIMKG PYDHFMQKEI
YEQPESTFNT MRGRIDYENN KVILGGLKAW LPVVRRARRL IMIACGTSYH SCLATRAIFE
ELSDIPVSVE LASDFLDRKC PVFRDDVCVF VSQSGETADT MLALNYCLER GALTVGIVNS
VGSSISRVTH CGVHINAGPE IGVASTKAYT SQYIALVMFA LSLSDDRVSK IDRRIEIIQG
LKLIPGQIKQ VLKLEPRIKK LCATELKDQK SLLLLGRGYQ FAAALEGALK IKEISYMHSE
GVLAGELKHG VLALVDENLP IIAFGTRDSL FPKVVSSIEQ VTARKGHPII ICNENDEVWA
QKSKSIDLQT LEVPQTVDCL QGLINIIPLQ LMSYWLAVNK GIDVDFPRNL AKSVTVE
