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Protein

Glutamate synthase [NADH]

Gene

GLT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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

Protein has several cofactor binding sites:

Enzyme regulationi

Inhibited by homocysteine sulfonamide.1 Publication

Kineticsi

  1. KM=280 µM for L-glutamine2 Publications
  2. KM=40 µM for 2-oxoglutarate2 Publications
  3. KM=7 µM for NADH2 Publications

    pH dependencei

    Optimum pH is 7-7.5. Active from pH 6 to 9.2 Publications

    Pathway: L-glutamate biosynthesis via GLT pathway

    This protein is involved in step 1 of the subpathway that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine (NAD(+) route).
    Proteins known to be involved in this subpathway in this organism are:
    1. Glutamate synthase [NADH] (GLT1)
    This subpathway is part of the pathway L-glutamate biosynthesis via GLT pathway, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine (NAD(+) route), the pathway L-glutamate biosynthesis via GLT pathway and in Amino-acid biosynthesis.

    Pathway: nitrogen metabolism

    This protein is involved in the pathway nitrogen metabolism, which is part of Energy metabolism.
    View all proteins of this organism that are known to be involved in the pathway nitrogen metabolism and in Energy metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei54 – 541For GATase activityBy 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 – 118958FMNBy similarityAdd
    BLAST
    Nucleotide bindingi1928 – 194215NADSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    GO - Biological processi

    • ammonia assimilation cycle Source: SGD
    • glutamate biosynthetic process Source: SGD
    • 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.

    Protein family/group databases

    MEROPSiC44.003.

    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 Componenti: Chromosome IV

    Organism-specific databases

    CYGDiYDL171c.
    EuPathDBiFungiDB:YDL171C.
    SGDiS000002330. GLT1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 53531 PublicationPRO_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.

    Interactioni

    Subunit structurei

    Homotrimer.1 Publication

    Protein-protein interaction databases

    BioGridi31894. 58 interactions.
    DIPiDIP-6490N.
    IntActiQ12680. 34 interactions.
    MINTiMINT-647261.
    STRINGi4932.YDL171C.

    Structurei

    3D structure databases

    ProteinModelPortaliQ12680.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1551 – 160050Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glutamate synthase family.Curated
    Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Glutamine amidotransferase

    Phylogenomic databases

    eggNOGiCOG0493.
    GeneTreeiENSGT00500000044896.
    HOGENOMiHOG000031559.
    InParanoidiQ12680.
    KOiK00264.
    OMAiVYPWVAK.
    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

            10         20         30         40         50
    MPVLKSDNFD PLEEAYEGGT IQNYNDEHHL HKSWANVIPD KRGLYDPDYE
    60 70 80 90 100
    HDACGVGFVA NKHGEQSHKI VTDARYLLVN MTHRGAVSSD GNGDGAGILL
    110 120 130 140 150
    GIPHEFMKRE FKLDLDLDIP EMGKYAVGNV FFKKNEKNNK KNLIKCQKIF
    160 170 180 190 200
    EDLAASFNLS VLGWRNVPVD STILGDVALS REPTILQPLL VPLYDEKQPE
    210 220 230 240 250
    FNETKFRTQL YLLRKEASLQ IGLENWFYVC SLNNTTIVYK GQLTPAQVYN
    260 270 280 290 300
    YYPDLTNAHF KSHMALVHSR FSTNTFPSWD RAQPLRWLAH NGEINTLRGN
    310 320 330 340 350
    KNWMRSREGV MNSATFKDEL DKLYPIIEEG GSDSAALDNV LELLTINGTL
    360 370 380 390 400
    SLPEAVMMMV PEAYHKDMDS DLKAWYDWAA CLMEPWDGPA LLTFTDGRYC
    410 420 430 440 450
    GAILDRNGLR PCRYYITSDD RVICASEVGV IPIENSLVVQ KGKLKPGDLF
    460 470 480 490 500
    LVDTQLGEMV DTKKLKSQIS KRQDFKSWLS KVIKLDDLLS KTANLVPKEF
    510 520 530 540 550
    ISQDSLSLKV QSDPRLLANG YTFEQVTFLL TPMALTGKEA LGSMGNDAPL
    560 570 580 590 600
    ACLNENPVLL YDYFRQLFAQ VTNPPIDPIR EANVMSLECY VGPQGNLLEM
    610 620 630 640 650
    HSSQCDRLLL KSPILHWNEF QALKNIEAAY PSWSVAEIDI TFDKSEGLLG
    660 670 680 690 700
    YTDTIDKITK LASEAIDDGK KILIITDRKM GANRVSISSL IAISCIHHHL
    710 720 730 740 750
    IRNKQRSQVA LILETGEARE IHHFCVLLGY GCDGVYPYLA METLVRMNRE
    760 770 780 790 800
    GLLRNVNNDN DTLEEGQILE NYKHAIDAGI LKVMSKMGIS TLASYKGAQI
    810 820 830 840 850
    FEALGLDNSI VDLCFTGTSS RIRGVTFEYL AQDAFSLHER GYPSRQTISK
    860 870 880 890 900
    SVNLPESGEY HFRDGGYKHV NEPTAIASLQ DTVRNKNDVS WQLYVKKEME
    910 920 930 940 950
    AIRDCTLRGL LELDFENSVS IPLEQVEPWT EIARRFASGA MSYGSISMEA
    960 970 980 990 1000
    HSTLAIAMNR LGAKSNCGEG GEDAERSAVQ ENGDTMRSAI KQVASARFGV
    1010 1020 1030 1040 1050
    TSYYLSDADE IQIKIAQGAK PGEGGELPAH KVSKDIAKTR HSTPNVGLIS
    1060 1070 1080 1090 1100
    PPPHHDIYSI EDLKQLIYDL KCANPRAGIS VKLVSEVGVG IVASGVAKAK
    1110 1120 1130 1140 1150
    ADHILVSGHD GGTGAARWTS VKYAGLPWEL GLAETHQTLV LNDLRRNVVV
    1160 1170 1180 1190 1200
    QTDGQLRTGF DIAVAVLLGA ESFTLATVPL IAMGCVMLRR CHLNSCAVGI
    1210 1220 1230 1240 1250
    ATQDPYLRSK FKGQPEHVIN FFYYLIQDLR QIMAKLGFRT IDEMVGHSEK
    1260 1270 1280 1290 1300
    LKKRDDVNAK AINIDLSPIL TPAHVIRPGV PTKFTKKQDH KLHTRLDNKL
    1310 1320 1330 1340 1350
    IDEAEVTLDR GLPVNIDASI INTDRALGST LSYRVSKKFG EDGLPKDTVV
    1360 1370 1380 1390 1400
    VNIEGSAGQS FGAFLASGIT FILNGDANDY VGKGLSGGII VIKPPKDSKF
    1410 1420 1430 1440 1450
    KSDENVIVGN TCFYGATSGT AFISGSAGER FGVRNSGATI VVERIKGNNA
    1460 1470 1480 1490 1500
    FEYMTGGRAI VLSQMESLNA FSGATGGIAY CLTSDYDDFV GKINKDTVEL
    1510 1520 1530 1540 1550
    ESLCDPVEIA FVKNLIQEHW NYTQSDLAAR ILGNFNHYLK DFVKVIPTDY
    1560 1570 1580 1590 1600
    KKVLLKEKAE AAKAKAKATS EYLKKFRSNQ EVDDEVNTLL IANQKAKEQE
    1610 1620 1630 1640 1650
    KKKSITISNK ATLKEPKVVD LEDAVPDSKQ LEKNSERIEK TRGFMIHKRR
    1660 1670 1680 1690 1700
    HETHRDPRTR VNDWKEFTNP ITKKDAKYQT ARCMDCGTPF CLSDTGCPLS
    1710 1720 1730 1740 1750
    NIIPKFNELL FKNQWKLALD KLLETNNFPE FTGRVCPAPC EGACTLGIIE
    1760 1770 1780 1790 1800
    DPVGIKSVER IIIDNAFKEG WIKPCPPSTR TGFTVGVIGS GPAGLACADM
    1810 1820 1830 1840 1850
    LNRAGHTVTV YERSDRCGGL LMYGIPNMKL DKAIVQRRID LLSAEGIDFV
    1860 1870 1880 1890 1900
    TNTEIGKTIS MDELKNKHNA VVYAIGSTIP RDLPIKGREL KNIDFAMQLL
    1910 1920 1930 1940 1950
    ESNTKALLNK DLEIIREKIQ GKKVIVVGGG DTGNDCLGTS VRHGAASVLN
    1960 1970 1980 1990 2000
    FELLPEPPVE RAKDNPWPQW PRVMRVDYGH AEVKEHYGRD PREYCILSKE
    2010 2020 2030 2040 2050
    FIGNDEGEVT AIRTVRVEWK KSQSGVWQMV EIPNSEEIFE ADIILLSMGF
    2060 2070 2080 2090 2100
    VGPELINGND NEVKKTRRGT IATLDDSSYS IDGGKTFACG DCRRGQSLIV
    2110 2120 2130 2140
    WAIQEGRKCA ASVDKFLMDG TTYLPSNGGI VQRDYKLLKE LASQV
    Length:2,145
    Mass (Da):238,102
    Last modified:September 5, 2006 - v2
    Checksum:i78184877D2167A0D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti166 – 1738NVPVDSTI → TSRRFYY in CAA61505 (PubMed:8923741).Curated
    Sequence conflicti450 – 4523FLV → IPS in CAA61505 (PubMed:8923741).Curated
    Sequence conflicti1753 – 17531V → L in CAA61505 (PubMed:8923741).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    ProteinModelPortaliQ12680.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi31894. 58 interactions.
    DIPiDIP-6490N.
    IntActiQ12680. 34 interactions.
    MINTiMINT-647261.
    STRINGi4932.YDL171C.

    Protein family/group databases

    MEROPSiC44.003.

    Proteomic databases

    MaxQBiQ12680.
    PaxDbiQ12680.
    PeptideAtlasiQ12680.
    PRIDEiQ12680.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CYGDiYDL171c.
    EuPathDBiFungiDB:YDL171C.
    SGDiS000002330. GLT1.

    Phylogenomic databases

    eggNOGiCOG0493.
    GeneTreeiENSGT00500000044896.
    HOGENOMiHOG000031559.
    InParanoidiQ12680.
    KOiK00264.
    OMAiVYPWVAK.
    OrthoDBiEOG7TN012.

    Enzyme and pathway databases

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

    Miscellaneous databases

    NextBioi968525.
    PROiQ12680.

    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]
    ProtoNetiSearch...

    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: June 24, 2015
    This is version 145 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.1 Publication

    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

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.