Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q12680

- GLT1_YEAST

UniProt

Q12680 - GLT1_YEAST

Protein

Glutamate synthase [NADH]

Gene

GLT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (05 Sep 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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-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

    Pathwayi

    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

    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

    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 – 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.

    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.
    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.
    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

    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:
    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

    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: October 1, 2014
    This is version 138 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