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Q12680

- GLT1_YEAST

UniProt

Q12680 - GLT1_YEAST

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Protein

Glutamate synthase [NADH]

Gene
GLT1, YDL171C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Forms L-glutamate from L-glutamine and 2-oxoglutarate. Represents an alternative pathway to L-glutamate dehydrogenase for the biosynthesis of L-glutamate. Participates with glutamine synthetase in ammonia assimilation processes. The enzyme is specific for NADH, L-glutamine and 2-oxoglutarate.2 Publications

Catalytic activityi

2 L-glutamate + NAD+ = L-glutamine + 2-oxoglutarate + NADH.

Cofactori

Binds 1 3Fe-4S cluster.
FAD.
FMN.

Enzyme regulationi

Inhibited by homocysteine sulfonamide.1 Publication

Kineticsi

  1. KM=280 µM for L-glutamine2 Publications
  2. KM=40 µM for 2-oxoglutarate
  3. KM=7 µM for NADH

pH dependencei

Optimum pH is 7-7.5. Active from pH 6 to 9.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 541For GATase activity By similarity
Metal bindingi1185 – 11851Iron-sulfur (3Fe-4S) By similarity
Metal bindingi1191 – 11911Iron-sulfur (3Fe-4S) By similarity
Metal bindingi1196 – 11961Iron-sulfur (3Fe-4S) By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1132 – 118958FMN By similarityAdd
BLAST
Nucleotide bindingi1928 – 194215NAD Reviewed predictionAdd
BLAST

GO - Molecular functioni

  1. 3 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. flavin adenine dinucleotide binding Source: InterPro
  3. FMN binding Source: InterPro
  4. glutamate synthase (NADH) activity Source: SGD
  5. iron ion binding Source: InterPro

GO - Biological processi

  1. ammonia assimilation cycle Source: SGD
  2. glutamate biosynthetic process Source: SGD
  3. L-glutamate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Glutamate biosynthesis

Keywords - Ligandi

3Fe-4S, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13146.
YEAST:YDL171C-MONOMER.
SABIO-RKQ12680.
UniPathwayiUPA00045.
UPA00634; UER00690.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate synthase [NADH] (EC:1.4.1.14)
Alternative name(s):
NADH-GOGAT
Gene namesi
Name:GLT1
Ordered Locus Names:YDL171C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDL171c.
SGDiS000002330. GLT1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 5353PRO_0000011612Add
BLAST
Chaini54 – 21452092Glutamate synthase [NADH]PRO_0000011613Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2070 – 20701Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein, Zymogen

Proteomic databases

MaxQBiQ12680.
PaxDbiQ12680.
PeptideAtlasiQ12680.
PRIDEiQ12680.

Expressioni

Gene expression databases

GenevestigatoriQ12680.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

BioGridi31894. 56 interactions.
DIPiDIP-6490N.
IntActiQ12680. 34 interactions.
MINTiMINT-647261.

Structurei

3D structure databases

ProteinModelPortaliQ12680.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 455402Glutamine amidotransferase type-2Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1551 – 160050 Reviewed predictionAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Glutamine amidotransferase

Phylogenomic databases

eggNOGiCOG0493.
GeneTreeiENSGT00500000044896.
HOGENOMiHOG000031559.
KOiK00264.
OMAiMMPADLP.
OrthoDBiEOG7TN012.

Family and domain databases

Gene3Di2.160.20.60. 1 hit.
3.20.20.70. 2 hits.
3.40.50.720. 2 hits.
3.60.20.10. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR028261. DPD_II.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR002489. Glu_synth_asu_C.
IPR006982. Glu_synth_centr_N.
IPR012220. Glu_synth_euk.
IPR002932. Glu_synthdom.
IPR006005. Glut_synth_ssu1.
IPR009051. Helical_ferredxn.
IPR016040. NAD(P)-bd_dom.
IPR029055. Ntn_hydrolases_N.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamiPF14691. Fer4_20. 1 hit.
PF00310. GATase_2. 1 hit.
PF04898. Glu_syn_central. 1 hit.
PF01645. Glu_synthase. 1 hit.
PF01493. GXGXG. 1 hit.
PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000187. GOGAT. 1 hit.
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF56235. SSF56235. 1 hit.
SSF69336. SSF69336. 1 hit.
TIGRFAMsiTIGR01317. GOGAT_sm_gam. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q12680-1 [UniParc]FASTAAdd to Basket

« Hide

MPVLKSDNFD PLEEAYEGGT IQNYNDEHHL HKSWANVIPD KRGLYDPDYE     50
HDACGVGFVA NKHGEQSHKI VTDARYLLVN MTHRGAVSSD GNGDGAGILL 100
GIPHEFMKRE FKLDLDLDIP EMGKYAVGNV FFKKNEKNNK KNLIKCQKIF 150
EDLAASFNLS VLGWRNVPVD STILGDVALS REPTILQPLL VPLYDEKQPE 200
FNETKFRTQL YLLRKEASLQ IGLENWFYVC SLNNTTIVYK GQLTPAQVYN 250
YYPDLTNAHF KSHMALVHSR FSTNTFPSWD RAQPLRWLAH NGEINTLRGN 300
KNWMRSREGV MNSATFKDEL DKLYPIIEEG GSDSAALDNV LELLTINGTL 350
SLPEAVMMMV PEAYHKDMDS DLKAWYDWAA CLMEPWDGPA LLTFTDGRYC 400
GAILDRNGLR PCRYYITSDD RVICASEVGV IPIENSLVVQ KGKLKPGDLF 450
LVDTQLGEMV DTKKLKSQIS KRQDFKSWLS KVIKLDDLLS KTANLVPKEF 500
ISQDSLSLKV QSDPRLLANG YTFEQVTFLL TPMALTGKEA LGSMGNDAPL 550
ACLNENPVLL YDYFRQLFAQ VTNPPIDPIR EANVMSLECY VGPQGNLLEM 600
HSSQCDRLLL KSPILHWNEF QALKNIEAAY PSWSVAEIDI TFDKSEGLLG 650
YTDTIDKITK LASEAIDDGK KILIITDRKM GANRVSISSL IAISCIHHHL 700
IRNKQRSQVA LILETGEARE IHHFCVLLGY GCDGVYPYLA METLVRMNRE 750
GLLRNVNNDN DTLEEGQILE NYKHAIDAGI LKVMSKMGIS TLASYKGAQI 800
FEALGLDNSI VDLCFTGTSS RIRGVTFEYL AQDAFSLHER GYPSRQTISK 850
SVNLPESGEY HFRDGGYKHV NEPTAIASLQ DTVRNKNDVS WQLYVKKEME 900
AIRDCTLRGL LELDFENSVS IPLEQVEPWT EIARRFASGA MSYGSISMEA 950
HSTLAIAMNR LGAKSNCGEG GEDAERSAVQ ENGDTMRSAI KQVASARFGV 1000
TSYYLSDADE IQIKIAQGAK PGEGGELPAH KVSKDIAKTR HSTPNVGLIS 1050
PPPHHDIYSI EDLKQLIYDL KCANPRAGIS VKLVSEVGVG IVASGVAKAK 1100
ADHILVSGHD GGTGAARWTS VKYAGLPWEL GLAETHQTLV LNDLRRNVVV 1150
QTDGQLRTGF DIAVAVLLGA ESFTLATVPL IAMGCVMLRR CHLNSCAVGI 1200
ATQDPYLRSK FKGQPEHVIN FFYYLIQDLR QIMAKLGFRT IDEMVGHSEK 1250
LKKRDDVNAK AINIDLSPIL TPAHVIRPGV PTKFTKKQDH KLHTRLDNKL 1300
IDEAEVTLDR GLPVNIDASI INTDRALGST LSYRVSKKFG EDGLPKDTVV 1350
VNIEGSAGQS FGAFLASGIT FILNGDANDY VGKGLSGGII VIKPPKDSKF 1400
KSDENVIVGN TCFYGATSGT AFISGSAGER FGVRNSGATI VVERIKGNNA 1450
FEYMTGGRAI VLSQMESLNA FSGATGGIAY CLTSDYDDFV GKINKDTVEL 1500
ESLCDPVEIA FVKNLIQEHW NYTQSDLAAR ILGNFNHYLK DFVKVIPTDY 1550
KKVLLKEKAE AAKAKAKATS EYLKKFRSNQ EVDDEVNTLL IANQKAKEQE 1600
KKKSITISNK ATLKEPKVVD LEDAVPDSKQ LEKNSERIEK TRGFMIHKRR 1650
HETHRDPRTR VNDWKEFTNP ITKKDAKYQT ARCMDCGTPF CLSDTGCPLS 1700
NIIPKFNELL FKNQWKLALD KLLETNNFPE FTGRVCPAPC EGACTLGIIE 1750
DPVGIKSVER IIIDNAFKEG WIKPCPPSTR TGFTVGVIGS GPAGLACADM 1800
LNRAGHTVTV YERSDRCGGL LMYGIPNMKL DKAIVQRRID LLSAEGIDFV 1850
TNTEIGKTIS MDELKNKHNA VVYAIGSTIP RDLPIKGREL KNIDFAMQLL 1900
ESNTKALLNK DLEIIREKIQ GKKVIVVGGG DTGNDCLGTS VRHGAASVLN 1950
FELLPEPPVE RAKDNPWPQW PRVMRVDYGH AEVKEHYGRD PREYCILSKE 2000
FIGNDEGEVT AIRTVRVEWK KSQSGVWQMV EIPNSEEIFE ADIILLSMGF 2050
VGPELINGND NEVKKTRRGT IATLDDSSYS IDGGKTFACG DCRRGQSLIV 2100
WAIQEGRKCA ASVDKFLMDG TTYLPSNGGI VQRDYKLLKE LASQV 2145
Length:2,145
Mass (Da):238,102
Last modified:September 5, 2006 - v2
Checksum:i78184877D2167A0D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti166 – 1738NVPVDSTI → TSRRFYY in CAA61505. 1 Publication
Sequence conflicti450 – 4523FLV → IPS in CAA61505. 1 Publication
Sequence conflicti1753 – 17531V → L in CAA61505. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X89221 Genomic DNA. Translation: CAA61505.1.
Z67750 Genomic DNA. Translation: CAA91574.1.
Z74219 Genomic DNA. Translation: CAA98745.1.
BK006938 Genomic DNA. Translation: DAA11690.1.
PIRiS61041.
RefSeqiNP_010110.1. NM_001180231.1.

Genome annotation databases

EnsemblFungiiYDL171C; YDL171C; YDL171C.
GeneIDi851383.
KEGGisce:YDL171C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X89221 Genomic DNA. Translation: CAA61505.1 .
Z67750 Genomic DNA. Translation: CAA91574.1 .
Z74219 Genomic DNA. Translation: CAA98745.1 .
BK006938 Genomic DNA. Translation: DAA11690.1 .
PIRi S61041.
RefSeqi NP_010110.1. NM_001180231.1.

3D structure databases

ProteinModelPortali Q12680.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31894. 56 interactions.
DIPi DIP-6490N.
IntActi Q12680. 34 interactions.
MINTi MINT-647261.

Proteomic databases

MaxQBi Q12680.
PaxDbi Q12680.
PeptideAtlasi Q12680.
PRIDEi Q12680.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDL171C ; YDL171C ; YDL171C .
GeneIDi 851383.
KEGGi sce:YDL171C.

Organism-specific databases

CYGDi YDL171c.
SGDi S000002330. GLT1.

Phylogenomic databases

eggNOGi COG0493.
GeneTreei ENSGT00500000044896.
HOGENOMi HOG000031559.
KOi K00264.
OMAi MMPADLP.
OrthoDBi EOG7TN012.

Enzyme and pathway databases

UniPathwayi UPA00045 .
UPA00634 ; UER00690 .
BioCyci MetaCyc:MONOMER-13146.
YEAST:YDL171C-MONOMER.
SABIO-RK Q12680.

Miscellaneous databases

NextBioi 968525.
PROi Q12680.

Gene expression databases

Genevestigatori Q12680.

Family and domain databases

Gene3Di 2.160.20.60. 1 hit.
3.20.20.70. 2 hits.
3.40.50.720. 2 hits.
3.60.20.10. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR028261. DPD_II.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR002489. Glu_synth_asu_C.
IPR006982. Glu_synth_centr_N.
IPR012220. Glu_synth_euk.
IPR002932. Glu_synthdom.
IPR006005. Glut_synth_ssu1.
IPR009051. Helical_ferredxn.
IPR016040. NAD(P)-bd_dom.
IPR029055. Ntn_hydrolases_N.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view ]
Pfami PF14691. Fer4_20. 1 hit.
PF00310. GATase_2. 1 hit.
PF04898. Glu_syn_central. 1 hit.
PF01645. Glu_synthase. 1 hit.
PF01493. GXGXG. 1 hit.
PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF000187. GOGAT. 1 hit.
SUPFAMi SSF46548. SSF46548. 1 hit.
SSF56235. SSF56235. 1 hit.
SSF69336. SSF69336. 1 hit.
TIGRFAMsi TIGR01317. GOGAT_sm_gam. 1 hit.
PROSITEi PS51278. GATASE_TYPE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of the GLT1 gene from Saccharomyces cerevisiae reveals the domain structure of yeast glutamate synthase."
    Filetici P., Martegani M.P., Valenzuela L., Gonzalez A., Ballario P.
    Yeast 12:1359-1366(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96744 / CN36.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Saccharomyces cerevisiae has a single glutamate synthase gene coding for a plant-like high-molecular-weight polypeptide."
    Cogoni C., Valenzuela L., Gonzalez-Halphen D., Olivera H., Macino G., Ballario P., Gonzalez A.
    J. Bacteriol. 177:792-798(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 54-61, SUBUNIT.
    Strain: ATCC 96744 / CN36.
  5. "Glutamate synthase: properties of the reduced nicotinamide adenine dinucleotide-dependent enzyme from Saccharomyces cerevisiae."
    Roon R.J., Even H.L., Larimore F.
    J. Bacteriol. 118:89-95(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
  6. "Inhibition of homocysteine sulfonamide of glutamate synthase purified from Saccharomyces cerevisiae."
    Masters D.S. Jr., Meister A.
    J. Biol. Chem. 257:8711-8715(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ENZYME REGULATION.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2070, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGLT1_YEAST
AccessioniPrimary (citable) accession number: Q12680
Secondary accession number(s): D6VRI0, Q12290
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 5, 2006
Last modified: September 3, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 18900 molecules/cell in log phase SD medium.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

Similar proteinsi