Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q12680 (GLT1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate synthase [NADH]

EC=1.4.1.14
Alternative name(s):
NADH-GOGAT
Gene names
Name:GLT1
Ordered Locus Names:YDL171C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length2145 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.6

Catalytic activity

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

Cofactor

Binds 1 3Fe-4S cluster.

FAD.

FMN.

Enzyme regulation

Inhibited by homocysteine sulfonamide. Ref.6

Pathway

Amino-acid biosynthesis; L-glutamate biosynthesis via GLT pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NAD(+) route): step 1/1.

Energy metabolism; nitrogen metabolism.

Subunit structure

Homotrimer. Ref.4

Miscellaneous

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

Sequence similarities

Belongs to the glutamate synthase family.

Contains 1 glutamine amidotransferase type-2 domain.

Biophysicochemical properties

Kinetic parameters:

KM=280 µM for L-glutamine Ref.5 Ref.6

KM=40 µM for 2-oxoglutarate

KM=7 µM for NADH

pH dependence:

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 5353
PRO_0000011612
Chain54 – 21452092Glutamate synthase [NADH]
PRO_0000011613

Regions

Domain54 – 455402Glutamine amidotransferase type-2
Nucleotide binding1132 – 118958FMN By similarity
Nucleotide binding1928 – 194215NAD Potential
Coiled coil1551 – 160050 Potential

Sites

Active site541For GATase activity By similarity
Metal binding11851Iron-sulfur (3Fe-4S) By similarity
Metal binding11911Iron-sulfur (3Fe-4S) By similarity
Metal binding11961Iron-sulfur (3Fe-4S) By similarity

Amino acid modifications

Modified residue20701Phosphothreonine Ref.8

Experimental info

Sequence conflict166 – 1738NVPVDSTI → TSRRFYY in CAA61505. Ref.1
Sequence conflict450 – 4523FLV → IPS in CAA61505. Ref.1
Sequence conflict17531V → L in CAA61505. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q12680 [UniParc].

Last modified September 5, 2006. Version 2.
Checksum: 78184877D2167A0D

FASTA2,145238,102
        10         20         30         40         50         60 
MPVLKSDNFD PLEEAYEGGT IQNYNDEHHL HKSWANVIPD KRGLYDPDYE HDACGVGFVA 

        70         80         90        100        110        120 
NKHGEQSHKI VTDARYLLVN MTHRGAVSSD GNGDGAGILL GIPHEFMKRE FKLDLDLDIP 

       130        140        150        160        170        180 
EMGKYAVGNV FFKKNEKNNK KNLIKCQKIF EDLAASFNLS VLGWRNVPVD STILGDVALS 

       190        200        210        220        230        240 
REPTILQPLL VPLYDEKQPE FNETKFRTQL YLLRKEASLQ IGLENWFYVC SLNNTTIVYK 

       250        260        270        280        290        300 
GQLTPAQVYN YYPDLTNAHF KSHMALVHSR FSTNTFPSWD RAQPLRWLAH NGEINTLRGN 

       310        320        330        340        350        360 
KNWMRSREGV MNSATFKDEL DKLYPIIEEG GSDSAALDNV LELLTINGTL SLPEAVMMMV 

       370        380        390        400        410        420 
PEAYHKDMDS DLKAWYDWAA CLMEPWDGPA LLTFTDGRYC GAILDRNGLR PCRYYITSDD 

       430        440        450        460        470        480 
RVICASEVGV IPIENSLVVQ KGKLKPGDLF LVDTQLGEMV DTKKLKSQIS KRQDFKSWLS 

       490        500        510        520        530        540 
KVIKLDDLLS KTANLVPKEF ISQDSLSLKV QSDPRLLANG YTFEQVTFLL TPMALTGKEA 

       550        560        570        580        590        600 
LGSMGNDAPL ACLNENPVLL YDYFRQLFAQ VTNPPIDPIR EANVMSLECY VGPQGNLLEM 

       610        620        630        640        650        660 
HSSQCDRLLL KSPILHWNEF QALKNIEAAY PSWSVAEIDI TFDKSEGLLG YTDTIDKITK 

       670        680        690        700        710        720 
LASEAIDDGK KILIITDRKM GANRVSISSL IAISCIHHHL IRNKQRSQVA LILETGEARE 

       730        740        750        760        770        780 
IHHFCVLLGY GCDGVYPYLA METLVRMNRE GLLRNVNNDN DTLEEGQILE NYKHAIDAGI 

       790        800        810        820        830        840 
LKVMSKMGIS TLASYKGAQI FEALGLDNSI VDLCFTGTSS RIRGVTFEYL AQDAFSLHER 

       850        860        870        880        890        900 
GYPSRQTISK SVNLPESGEY HFRDGGYKHV NEPTAIASLQ DTVRNKNDVS WQLYVKKEME 

       910        920        930        940        950        960 
AIRDCTLRGL LELDFENSVS IPLEQVEPWT EIARRFASGA MSYGSISMEA HSTLAIAMNR 

       970        980        990       1000       1010       1020 
LGAKSNCGEG GEDAERSAVQ ENGDTMRSAI KQVASARFGV TSYYLSDADE IQIKIAQGAK 

      1030       1040       1050       1060       1070       1080 
PGEGGELPAH KVSKDIAKTR HSTPNVGLIS PPPHHDIYSI EDLKQLIYDL KCANPRAGIS 

      1090       1100       1110       1120       1130       1140 
VKLVSEVGVG IVASGVAKAK ADHILVSGHD GGTGAARWTS VKYAGLPWEL GLAETHQTLV 

      1150       1160       1170       1180       1190       1200 
LNDLRRNVVV QTDGQLRTGF DIAVAVLLGA ESFTLATVPL IAMGCVMLRR CHLNSCAVGI 

      1210       1220       1230       1240       1250       1260 
ATQDPYLRSK FKGQPEHVIN FFYYLIQDLR QIMAKLGFRT IDEMVGHSEK LKKRDDVNAK 

      1270       1280       1290       1300       1310       1320 
AINIDLSPIL TPAHVIRPGV PTKFTKKQDH KLHTRLDNKL IDEAEVTLDR GLPVNIDASI 

      1330       1340       1350       1360       1370       1380 
INTDRALGST LSYRVSKKFG EDGLPKDTVV VNIEGSAGQS FGAFLASGIT FILNGDANDY 

      1390       1400       1410       1420       1430       1440 
VGKGLSGGII VIKPPKDSKF KSDENVIVGN TCFYGATSGT AFISGSAGER FGVRNSGATI 

      1450       1460       1470       1480       1490       1500 
VVERIKGNNA FEYMTGGRAI VLSQMESLNA FSGATGGIAY CLTSDYDDFV GKINKDTVEL 

      1510       1520       1530       1540       1550       1560 
ESLCDPVEIA FVKNLIQEHW NYTQSDLAAR ILGNFNHYLK DFVKVIPTDY KKVLLKEKAE 

      1570       1580       1590       1600       1610       1620 
AAKAKAKATS EYLKKFRSNQ EVDDEVNTLL IANQKAKEQE KKKSITISNK ATLKEPKVVD 

      1630       1640       1650       1660       1670       1680 
LEDAVPDSKQ LEKNSERIEK TRGFMIHKRR HETHRDPRTR VNDWKEFTNP ITKKDAKYQT 

      1690       1700       1710       1720       1730       1740 
ARCMDCGTPF CLSDTGCPLS NIIPKFNELL FKNQWKLALD KLLETNNFPE FTGRVCPAPC 

      1750       1760       1770       1780       1790       1800 
EGACTLGIIE DPVGIKSVER IIIDNAFKEG WIKPCPPSTR TGFTVGVIGS GPAGLACADM 

      1810       1820       1830       1840       1850       1860 
LNRAGHTVTV YERSDRCGGL LMYGIPNMKL DKAIVQRRID LLSAEGIDFV TNTEIGKTIS 

      1870       1880       1890       1900       1910       1920 
MDELKNKHNA VVYAIGSTIP RDLPIKGREL KNIDFAMQLL ESNTKALLNK DLEIIREKIQ 

      1930       1940       1950       1960       1970       1980 
GKKVIVVGGG DTGNDCLGTS VRHGAASVLN FELLPEPPVE RAKDNPWPQW PRVMRVDYGH 

      1990       2000       2010       2020       2030       2040 
AEVKEHYGRD PREYCILSKE FIGNDEGEVT AIRTVRVEWK KSQSGVWQMV EIPNSEEIFE 

      2050       2060       2070       2080       2090       2100 
ADIILLSMGF VGPELINGND NEVKKTRRGT IATLDDSSYS IDGGKTFACG DCRRGQSLIV 

      2110       2120       2130       2140 
WAIQEGRKCA ASVDKFLMDG TTYLPSNGGI VQRDYKLLKE LASQV 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X89221 Genomic DNA. Translation: CAA61505.1.
Z67750 Genomic DNA. Translation: CAA91574.1.
Z74219 Genomic DNA. Translation: CAA98745.1.
BK006938 Genomic DNA. Translation: DAA11690.1.
PIRS61041.
RefSeqNP_010110.1. NM_001180231.1.

3D structure databases

ProteinModelPortalQ12680.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31894. 55 interactions.
DIPDIP-6490N.
IntActQ12680. 34 interactions.
MINTMINT-647261.

Proteomic databases

MaxQBQ12680.
PaxDbQ12680.
PeptideAtlasQ12680.
PRIDEQ12680.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL171C; YDL171C; YDL171C.
GeneID851383.
KEGGsce:YDL171C.

Organism-specific databases

CYGDYDL171c.
SGDS000002330. GLT1.

Phylogenomic databases

eggNOGCOG0493.
GeneTreeENSGT00500000044896.
HOGENOMHOG000031559.
KOK00264.
OMAMMPADLP.
OrthoDBEOG7TN012.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13146.
YEAST:YDL171C-MONOMER.
SABIO-RKQ12680.
UniPathwayUPA00045.
UPA00634; UER00690.

Gene expression databases

GenevestigatorQ12680.

Family and domain databases

Gene3D2.160.20.60. 1 hit.
3.20.20.70. 2 hits.
3.40.50.720. 2 hits.
3.60.20.10. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR028261. DPD_II.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR002489. Glu_synth_asu_C.
IPR002932. Glu_synth_centr_C.
IPR006982. Glu_synth_centr_N.
IPR012220. Glu_synth_euk.
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]
PfamPF14691. 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]
PIRSFPIRSF000187. GOGAT. 1 hit.
SUPFAMSSF46548. SSF46548. 1 hit.
SSF56235. SSF56235. 1 hit.
SSF69336. SSF69336. 1 hit.
TIGRFAMsTIGR01317. GOGAT_sm_gam. 1 hit.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968525.
PROQ12680.

Entry information

Entry nameGLT1_YEAST
AccessionPrimary (citable) accession number: Q12680
Secondary accession number(s): D6VRI0, Q12290
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 5, 2006
Last modified: June 11, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways