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Entry version 188 (29 Sep 2021)
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 lysine biosynthesis.

2 Publications

Miscellaneous

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

Caution

PubMed:10077615 shows data confirming the peroxisomal localization of the protein, however this study was later retracted as the images were additionally used in other articles for other proteins.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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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 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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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

<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

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]1 Publication (EC:1.5.1.73 Publications)
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:LYS1Imported
Ordered Locus Names:YIR034CImported
<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

Saccharomyces Genome Database

More...
SGDi
S000001473, LYS1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YIR034C

<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

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 or proteolytic cleavage.<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

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
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">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
35025, 26 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

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P38998, protein

<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

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

More...
SMRi
P38998

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0172, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_063085_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P38998

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

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>. The information is filed in different subsections. The current subsections and their content are listed below:<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; 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:

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[»]
SMRiP38998
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi35025, 26 interactors
DIPiDIP-5291N
IntActiP38998, 11 interactors
MINTiP38998
STRINGi4932.YIR034C

PTM databases

CarbonylDBiP38998
iPTMnetiP38998

Proteomic databases

MaxQBiP38998
PaxDbiP38998
PRIDEiP38998

Genome annotation databases

EnsemblFungiiYIR034C_mRNA; YIR034C; YIR034C
GeneIDi854852
KEGGisce:YIR034C

Organism-specific databases

SGDiS000001473, LYS1
VEuPathDBiFungiDB:YIR034C

Phylogenomic databases

eggNOGiKOG0172, Eukaryota
HOGENOMiCLU_063085_0_0_1
InParanoidiP38998
OMAiYFFFSHT

Enzyme and pathway databases

UniPathwayiUPA00033;UER00034
BRENDAi1.5.1.7, 984
SABIO-RKiP38998

Miscellaneous databases

EvolutionaryTraceiP38998

Protein Ontology

More...
PROi
PR:P38998
RNActiP38998, protein

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
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

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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: September 29, 2021
This is version 188 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, Direct protein sequencing, Reference proteome

Documents

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