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Entry version 174 (08 May 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Saccharopine dehydrogenase [NAD(+), L-lysine-forming]

Gene

LYS1

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the NAD+-dependent cleavage of saccharopine to L-lysine and 2-oxoglutarate, the final step in the alpha-aminoadipate (AAA) pathway for lysin biosynthesis.2 Publications

Miscellaneous

Present with 111934 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by p-chloromercuribenzoate and iodoacetate by modification of the active site cysteine residue. Inhibited by diethyl pyrocarbonate by modification of histidine residues. Inhibited by pyridoxal 5'-phosphate by modification of an essential lysine residue.4 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.089 mM for NADH (at pH 6.8 and 22 degrees Celsius)1 Publication
  2. KM=0.1 mM for NAD+ (at pH 6.8 and 22 degrees Celsius)1 Publication
  3. KM=1.67 mM for saccharopine (at pH 6.8 and 22 degrees Celsius)1 Publication
  4. KM=0.55 mM for 2-oxoglutarate (at pH 6.8 and 22 degrees Celsius)1 Publication
  5. KM=2.0 mM for L-lysine (at pH 6.8 and 22 degrees Celsius)1 Publication
  6. KM=0.019 mM for NADH (at pH 7 and 25 degrees Celsius)1 Publication
  7. KM=0.9 mM for NAD+ (at pH 7 and 25 degrees Celsius)1 Publication
  8. KM=6.7 mM for saccharopine (at pH 7 and 25 degrees Celsius)1 Publication
  9. KM=0.11 mM for 2-oxoglutarate (at pH 7 and 25 degrees Celsius)1 Publication
  10. KM=1.1 mM for L-lysine (at pH 7 and 25 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 10 for the forward reaction, and 6.5-7 for the reverse reaction.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-lysine biosynthesis via AAA pathway

    This protein is involved in step 3 of the subpathway that synthesizes L-lysine from L-alpha-aminoadipate (fungal route).1 Publication
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. L-2-aminoadipate reductase (LYS2)
    2. Saccharopine dehydrogenase [NADP(+), L-glutamate-forming] (LYS9)
    3. Saccharopine dehydrogenase [NAD(+), L-lysine-forming] (LYS1)
    This subpathway is part of the pathway L-lysine biosynthesis via AAA 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-lysine from L-alpha-aminoadipate (fungal route), the pathway L-lysine biosynthesis via AAA pathway and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei18L-saccharopineCombined sources1 Publication1 Publication1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei77Proton acceptor1 Publication1 Publication1
    Binding sitei77L-saccharopineCombined sources1 Publication1 Publication1
    Active sitei96Proton donor1 Publication1 Publication1
    Binding sitei101L-saccharopineCombined sources1
    Binding sitei130NADCombined sources1
    Binding sitei131L-saccharopineCombined sources1 Publication1 Publication1
    Binding sitei135L-saccharopine; via amide nitrogenCombined sources1
    Binding sitei227NADCombined sources1 Publication1 Publication1
    Binding sitei231NADCombined sources1 Publication1 Publication1
    Binding sitei251NADCombined sources1
    Binding sitei278NAD; via carbonyl oxygenCombined sources1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi203 – 204NADCombined sources1 Publication1 Publication2
    Nucleotide bindingi318 – 321NADCombined sources1 Publication4

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    • lysine biosynthetic process Source: SGD
    • lysine biosynthetic process via aminoadipic acid Source: SGD

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionOxidoreductase
    Biological processAmino-acid biosynthesis, Lysine biosynthesis
    LigandNAD

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    YEAST:YIR034C-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.5.1.7 984

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P38998

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00033;UER00034

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Saccharopine dehydrogenase [NAD(+), L-lysine-forming] (EC:1.5.1.7)
    Short name:
    SDH
    Alternative name(s):
    Lysine--2-oxoglutarate reductase
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:LYS1
    Ordered Locus Names:YIR034C
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome IX

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    FungiDB:YIR034C

    Saccharomyces Genome Database

    More...
    SGDi
    S000001473 LYS1

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Peroxisome

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi77K → M: Decreases the turnover number 145-fold. Decreases the turnover number 700-fold; when associated with GLN-96. 1 Publication1
    Mutagenesisi96H → Q: Decreases the turnover number 28-fold. Decreases the turnover number 700-fold; when associated with MET-77. 1 Publication1
    Mutagenesisi205C → S: Prevents disulfide formation. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001990162 – 373Saccharopine dehydrogenase [NAD(+), L-lysine-forming]Add BLAST372

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanine; partial1 Publication1
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi205 ↔ 249Combined sources2 Publications

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P38998

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P38998

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P38998

    PTM databases

    CarbonylDB database of protein carbonylation sites

    More...
    CarbonylDBi
    P38998

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Induced by alpha-aminoadipate semialdehyde in a LYS14-dependent manner. Repressed by lysine.1 Publication

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Monomer.1 Publication

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    RSP5P399403EBI-10264,EBI-16219

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    35025, 25 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-5291N

    Protein interaction database and analysis system

    More...
    IntActi
    P38998, 11 interactors

    Molecular INTeraction database

    More...
    MINTi
    P38998

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YIR034C

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1373
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2Q99X-ray1.64A1-373[»]
    2QRJX-ray1.60A1-373[»]
    2QRKX-ray1.75A1-373[»]
    2QRLX-ray1.60A1-373[»]
    3UGKX-ray2.01A1-373[»]
    3UH1X-ray2.17A1-373[»]
    3UHAX-ray2.30A/B1-373[»]

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P38998

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P38998

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni279 – 281L-saccharopine bindingCombined sources3

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi371 – 373Microbody targeting signalSequence analysis1 Publication3

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the AlaDH/PNT family.Curated

    Phylogenomic databases

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000143704

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P38998

    KEGG Orthology (KO)

    More...
    KOi
    K00290

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    YFFFSHT

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd12188 SDH, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR007886 AlaDH/PNT_N
    IPR007698 AlaDH/PNT_NAD(H)-bd
    IPR027281 Lys1
    IPR036291 NAD(P)-bd_dom_sf

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11133:SF15 PTHR11133:SF15, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF05222 AlaDh_PNT_N, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF018250 Saccharopine_DH_Lys, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM01002 AlaDh_PNT_C, 1 hit
    SM01003 AlaDh_PNT_N, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51735 SSF51735, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P38998-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAAVTLHLRA ETKPLEARAA LTPTTVKKLI AKGFKIYVED SPQSTFNINE
    60 70 80 90 100
    YRQAGAIIVP AGSWKTAPRD RIIIGLKEMP ETDTFPLVHE HIQFAHCYKD
    110 120 130 140 150
    QAGWQNVLMR FIKGHGTLYD LEFLENDQGR RVAAFGFYAG FAGAALGVRD
    160 170 180 190 200
    WAFKQTHSDD EDLPAVSPYP NEKALVKDVT KDYKEALATG ARKPTVLIIG
    210 220 230 240 250
    ALGRCGSGAI DLLHKVGIPD ANILKWDIKE TSRGGPFDEI PQADIFINCI
    260 270 280 290 300
    YLSKPIAPFT NMEKLNNPNR RLRTVVDVSA DTTNPHNPIP IYTVATVFNK
    310 320 330 340 350
    PTVLVPTTAG PKLSVISIDH LPSLLPREAS EFFSHDLLPS LELLPQRKTA
    360 370
    PVWVRAKKLF DRHCARVKRS SRL
    Length:373
    Mass (Da):41,465
    Last modified:January 23, 2007 - v3
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i7E3A810876C1DC41
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti209A → AL AA sequence (PubMed:6769500).Curated1
    Sequence conflicti309A → V in CAA54551 (Ref. 1) Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    X77362 Genomic DNA Translation: CAA54551.1
    Z38061 Genomic DNA Translation: CAA86194.1
    BK006942 Genomic DNA Translation: DAA08581.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S48496

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_012300.3, NM_001179556.3

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    YIR034C_mRNA; YIR034C_mRNA; YIR034C

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    854852

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sce:YIR034C

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X77362 Genomic DNA Translation: CAA54551.1
    Z38061 Genomic DNA Translation: CAA86194.1
    BK006942 Genomic DNA Translation: DAA08581.1
    PIRiS48496
    RefSeqiNP_012300.3, NM_001179556.3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2Q99X-ray1.64A1-373[»]
    2QRJX-ray1.60A1-373[»]
    2QRKX-ray1.75A1-373[»]
    2QRLX-ray1.60A1-373[»]
    3UGKX-ray2.01A1-373[»]
    3UH1X-ray2.17A1-373[»]
    3UHAX-ray2.30A/B1-373[»]
    SMRiP38998
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi35025, 25 interactors
    DIPiDIP-5291N
    IntActiP38998, 11 interactors
    MINTiP38998
    STRINGi4932.YIR034C

    PTM databases

    CarbonylDBiP38998

    Proteomic databases

    MaxQBiP38998
    PaxDbiP38998
    PRIDEiP38998

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYIR034C_mRNA; YIR034C_mRNA; YIR034C
    GeneIDi854852
    KEGGisce:YIR034C

    Organism-specific databases

    EuPathDBiFungiDB:YIR034C
    SGDiS000001473 LYS1

    Phylogenomic databases

    HOGENOMiHOG000143704
    InParanoidiP38998
    KOiK00290
    OMAiYFFFSHT

    Enzyme and pathway databases

    UniPathwayi
    UPA00033;UER00034

    BioCyciYEAST:YIR034C-MONOMER
    BRENDAi1.5.1.7 984
    SABIO-RKiP38998

    Miscellaneous databases

    EvolutionaryTraceiP38998

    Protein Ontology

    More...
    PROi
    PR:P38998

    Family and domain databases

    CDDicd12188 SDH, 1 hit
    InterProiView protein in InterPro
    IPR007886 AlaDH/PNT_N
    IPR007698 AlaDH/PNT_NAD(H)-bd
    IPR027281 Lys1
    IPR036291 NAD(P)-bd_dom_sf
    PANTHERiPTHR11133:SF15 PTHR11133:SF15, 1 hit
    PfamiView protein in Pfam
    PF05222 AlaDh_PNT_N, 1 hit
    PIRSFiPIRSF018250 Saccharopine_DH_Lys, 1 hit
    SMARTiView protein in SMART
    SM01002 AlaDh_PNT_C, 1 hit
    SM01003 AlaDh_PNT_N, 1 hit
    SUPFAMiSSF51735 SSF51735, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLYS1_YEAST
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P38998
    Secondary accession number(s): D6VVW5
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: January 23, 2007
    Last modified: May 8, 2019
    This is version 174 of the entry and version 3 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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