GLT1_YEAST
ID GLT1_YEAST Reviewed; 2145 AA.
AC Q12680; D6VRI0; Q12290;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Glutamate synthase [NADH];
DE EC=1.4.1.14 {ECO:0000269|PubMed:4362465, ECO:0000269|PubMed:7047525, ECO:0000269|PubMed:7836314};
DE AltName: Full=NADH-GOGAT;
DE Flags: Precursor;
GN Name=GLT1; OrderedLocusNames=YDL171C;
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 96744 / CN36;
RX PubMed=8923741;
RX DOI=10.1002/(sici)1097-0061(199610)12:13<1359::aid-yea3>3.0.co;2-5;
RA Filetici P., Martegani M.P., Valenzuela L., Gonzalez A., Ballario P.;
RT "Sequence of the GLT1 gene from Saccharomyces cerevisiae reveals the domain
RT structure of yeast glutamate synthase.";
RL Yeast 12:1359-1366(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 54-61, SUBUNIT, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 96744 / CN36;
RX PubMed=7836314; DOI=10.1128/jb.177.3.792-798.1995;
RA Cogoni C., Valenzuela L., Gonzalez-Halphen D., Olivera H., Macino G.,
RA Ballario P., Gonzalez A.;
RT "Saccharomyces cerevisiae has a single glutamate synthase gene coding for a
RT plant-like high-molecular-weight polypeptide.";
RL J. Bacteriol. 177:792-798(1995).
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND
RP CATALYTIC ACTIVITY.
RX PubMed=4362465; DOI=10.1128/jb.118.1.89-95.1974;
RA Roon R.J., Even H.L., Larimore F.;
RT "Glutamate synthase: properties of the reduced nicotinamide adenine
RT dinucleotide-dependent enzyme from Saccharomyces cerevisiae.";
RL J. Bacteriol. 118:89-95(1974).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY
RP REGULATION, AND CATALYTIC ACTIVITY.
RX PubMed=7047525; DOI=10.1016/s0021-9258(18)34186-3;
RA Masters D.S. Jr., Meister A.;
RT "Inhibition of homocysteine sulfonamide of glutamate synthase purified from
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 257:8711-8715(1982).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2070, AND IDENTIFICATION BY
RP 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: Forms L-glutamate from L-glutamine and 2-oxoglutarate.
CC Represents an alternative pathway to L-glutamate dehydrogenase for the
CC biosynthesis of L-glutamate. Participates with glutamine synthetase in
CC ammonia assimilation processes. The enzyme is specific for NADH, L-
CC glutamine and 2-oxoglutarate. {ECO:0000269|PubMed:4362465,
CC ECO:0000269|PubMed:7047525}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + L-glutamine +
CC NADH; Xref=Rhea:RHEA:13753, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58359; EC=1.4.1.14; Evidence={ECO:0000269|PubMed:4362465,
CC ECO:0000269|PubMed:7047525, ECO:0000269|PubMed:7836314};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Note=Binds 1 [3Fe-4S] cluster.;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC -!- ACTIVITY REGULATION: Inhibited by homocysteine sulfonamide.
CC {ECO:0000269|PubMed:7047525}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=280 uM for L-glutamine {ECO:0000269|PubMed:4362465,
CC ECO:0000269|PubMed:7047525};
CC KM=40 uM for 2-oxoglutarate {ECO:0000269|PubMed:4362465,
CC ECO:0000269|PubMed:7047525};
CC KM=7 uM for NADH {ECO:0000269|PubMed:4362465,
CC ECO:0000269|PubMed:7047525};
CC pH dependence:
CC Optimum pH is 7-7.5. Active from pH 6 to 9.
CC {ECO:0000269|PubMed:4362465, ECO:0000269|PubMed:7047525};
CC -!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
CC pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NAD(+)
CC route): step 1/1.
CC -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:7836314}.
CC -!- MISCELLANEOUS: Present with 18900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family. {ECO:0000305}.
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DR EMBL; X89221; CAA61505.1; -; Genomic_DNA.
DR EMBL; Z67750; CAA91574.1; -; Genomic_DNA.
DR EMBL; Z74219; CAA98745.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11690.1; -; Genomic_DNA.
DR PIR; S61041; S61041.
DR RefSeq; NP_010110.1; NM_001180231.1.
DR AlphaFoldDB; Q12680; -.
DR SMR; Q12680; -.
DR BioGRID; 31894; 178.
DR DIP; DIP-6490N; -.
DR IntAct; Q12680; 35.
DR MINT; Q12680; -.
DR STRING; 4932.YDL171C; -.
DR iPTMnet; Q12680; -.
DR MaxQB; Q12680; -.
DR PaxDb; Q12680; -.
DR PRIDE; Q12680; -.
DR EnsemblFungi; YDL171C_mRNA; YDL171C; YDL171C.
DR GeneID; 851383; -.
DR KEGG; sce:YDL171C; -.
DR SGD; S000002330; GLT1.
DR VEuPathDB; FungiDB:YDL171C; -.
DR eggNOG; KOG0399; Eukaryota.
DR GeneTree; ENSGT00940000172171; -.
DR HOGENOM; CLU_000422_8_2_1; -.
DR InParanoid; Q12680; -.
DR OMA; TVFRLQH; -.
DR BioCyc; MetaCyc:YDL171C-MON; -.
DR BioCyc; YEAST:YDL171C-MON; -.
DR SABIO-RK; Q12680; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR PRO; PR:Q12680; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12680; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016040; F:glutamate synthase (NADH) activity; IDA:SGD.
DR GO; GO:0015930; F:glutamate synthase activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0019676; P:ammonia assimilation cycle; IEP:SGD.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEP:SGD.
DR GO; GO:0097054; P:L-glutamate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00982; gltB_C; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 1.10.1060.10; -; 1.
DR Gene3D; 2.160.20.60; -; 1.
DR Gene3D; 3.20.20.70; -; 2.
DR Gene3D; 3.50.50.60; -; 2.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR002489; Glu_synth_asu_C.
DR InterPro; IPR036485; Glu_synth_asu_C_sf.
DR InterPro; IPR006982; Glu_synth_centr_N.
DR InterPro; IPR012220; Glu_synth_euk.
DR InterPro; IPR002932; Glu_synthdom.
DR InterPro; IPR006005; Glut_synth_ssu1.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF00310; GATase_2; 1.
DR Pfam; PF04898; Glu_syn_central; 1.
DR Pfam; PF01645; Glu_synthase; 1.
DR Pfam; PF01493; GXGXG; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PIRSF; PIRSF000187; GOGAT; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR SUPFAM; SSF69336; SSF69336; 1.
DR TIGRFAMs; TIGR01317; GOGAT_sm_gam; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 1: Evidence at protein level;
KW 3Fe-4S; Amino-acid biosynthesis; Coiled coil; Direct protein sequencing;
KW FAD; Flavoprotein; FMN; Glutamate biosynthesis; Glutamine amidotransferase;
KW Iron; Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Zymogen.
FT PROPEP 1..53
FT /evidence="ECO:0000269|PubMed:7836314"
FT /id="PRO_0000011612"
FT CHAIN 54..2145
FT /note="Glutamate synthase [NADH]"
FT /id="PRO_0000011613"
FT DOMAIN 54..455
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT COILED 1551..1600
FT /evidence="ECO:0000255"
FT ACT_SITE 54
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT BINDING 1132..1189
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 1185
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1191
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1196
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1928..1942
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT MOD_RES 2070
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 166..173
FT /note="NVPVDSTI -> TSRRFYY (in Ref. 1; CAA61505)"
FT /evidence="ECO:0000305"
FT CONFLICT 450..452
FT /note="FLV -> IPS (in Ref. 1; CAA61505)"
FT /evidence="ECO:0000305"
FT CONFLICT 1753
FT /note="V -> L (in Ref. 1; CAA61505)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2145 AA; 238102 MW; 78184877D2167A0D CRC64;
MPVLKSDNFD PLEEAYEGGT IQNYNDEHHL HKSWANVIPD KRGLYDPDYE HDACGVGFVA
NKHGEQSHKI VTDARYLLVN MTHRGAVSSD GNGDGAGILL GIPHEFMKRE FKLDLDLDIP
EMGKYAVGNV FFKKNEKNNK KNLIKCQKIF EDLAASFNLS VLGWRNVPVD STILGDVALS
REPTILQPLL VPLYDEKQPE FNETKFRTQL YLLRKEASLQ IGLENWFYVC SLNNTTIVYK
GQLTPAQVYN YYPDLTNAHF KSHMALVHSR FSTNTFPSWD RAQPLRWLAH NGEINTLRGN
KNWMRSREGV MNSATFKDEL DKLYPIIEEG GSDSAALDNV LELLTINGTL SLPEAVMMMV
PEAYHKDMDS DLKAWYDWAA CLMEPWDGPA LLTFTDGRYC GAILDRNGLR PCRYYITSDD
RVICASEVGV IPIENSLVVQ KGKLKPGDLF LVDTQLGEMV DTKKLKSQIS KRQDFKSWLS
KVIKLDDLLS KTANLVPKEF ISQDSLSLKV QSDPRLLANG YTFEQVTFLL TPMALTGKEA
LGSMGNDAPL ACLNENPVLL YDYFRQLFAQ VTNPPIDPIR EANVMSLECY VGPQGNLLEM
HSSQCDRLLL KSPILHWNEF QALKNIEAAY PSWSVAEIDI TFDKSEGLLG YTDTIDKITK
LASEAIDDGK KILIITDRKM GANRVSISSL IAISCIHHHL IRNKQRSQVA LILETGEARE
IHHFCVLLGY GCDGVYPYLA METLVRMNRE GLLRNVNNDN DTLEEGQILE NYKHAIDAGI
LKVMSKMGIS TLASYKGAQI FEALGLDNSI VDLCFTGTSS RIRGVTFEYL AQDAFSLHER
GYPSRQTISK SVNLPESGEY HFRDGGYKHV NEPTAIASLQ DTVRNKNDVS WQLYVKKEME
AIRDCTLRGL LELDFENSVS IPLEQVEPWT EIARRFASGA MSYGSISMEA HSTLAIAMNR
LGAKSNCGEG GEDAERSAVQ ENGDTMRSAI KQVASARFGV TSYYLSDADE IQIKIAQGAK
PGEGGELPAH KVSKDIAKTR HSTPNVGLIS PPPHHDIYSI EDLKQLIYDL KCANPRAGIS
VKLVSEVGVG IVASGVAKAK ADHILVSGHD GGTGAARWTS VKYAGLPWEL GLAETHQTLV
LNDLRRNVVV QTDGQLRTGF DIAVAVLLGA ESFTLATVPL IAMGCVMLRR CHLNSCAVGI
ATQDPYLRSK FKGQPEHVIN FFYYLIQDLR QIMAKLGFRT IDEMVGHSEK LKKRDDVNAK
AINIDLSPIL TPAHVIRPGV PTKFTKKQDH KLHTRLDNKL IDEAEVTLDR GLPVNIDASI
INTDRALGST LSYRVSKKFG EDGLPKDTVV VNIEGSAGQS FGAFLASGIT FILNGDANDY
VGKGLSGGII VIKPPKDSKF KSDENVIVGN TCFYGATSGT AFISGSAGER FGVRNSGATI
VVERIKGNNA FEYMTGGRAI VLSQMESLNA FSGATGGIAY CLTSDYDDFV GKINKDTVEL
ESLCDPVEIA FVKNLIQEHW NYTQSDLAAR ILGNFNHYLK DFVKVIPTDY KKVLLKEKAE
AAKAKAKATS EYLKKFRSNQ EVDDEVNTLL IANQKAKEQE KKKSITISNK ATLKEPKVVD
LEDAVPDSKQ LEKNSERIEK TRGFMIHKRR HETHRDPRTR VNDWKEFTNP ITKKDAKYQT
ARCMDCGTPF CLSDTGCPLS NIIPKFNELL FKNQWKLALD KLLETNNFPE FTGRVCPAPC
EGACTLGIIE DPVGIKSVER IIIDNAFKEG WIKPCPPSTR TGFTVGVIGS GPAGLACADM
LNRAGHTVTV YERSDRCGGL LMYGIPNMKL DKAIVQRRID LLSAEGIDFV TNTEIGKTIS
MDELKNKHNA VVYAIGSTIP RDLPIKGREL KNIDFAMQLL ESNTKALLNK DLEIIREKIQ
GKKVIVVGGG DTGNDCLGTS VRHGAASVLN FELLPEPPVE RAKDNPWPQW PRVMRVDYGH
AEVKEHYGRD PREYCILSKE FIGNDEGEVT AIRTVRVEWK KSQSGVWQMV EIPNSEEIFE
ADIILLSMGF VGPELINGND NEVKKTRRGT IATLDDSSYS IDGGKTFACG DCRRGQSLIV
WAIQEGRKCA ASVDKFLMDG TTYLPSNGGI VQRDYKLLKE LASQV
