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UniProtKB - P07342 (ILVB_YEAST)

Entry version 226 (25 May 2022)
Sequence version 1 (01 Apr 1988)
Previous versions | rss
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Protein

Acetolactate synthase catalytic subunit, mitochondrial

Gene

ILV2

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

Catalytic subunit of mitochondrial acetolactate synthase, which catalyzes the first of a series of common steps in the biosynthesis of the branched-chain amino acids. Catalyzes the irreversible decarboxylation of pyruvate to a bound hydroxyethyl group that then condenses with either a second pyruvate molecule to form 2-acetolactate (AL) or with 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate (AHB). The first product is the precursor for valine and leucine biosynthesis, while the second leads to isoleucine.

1 Publication

Miscellaneous

Contains 1 molecule of FAD per monomer. The role of this cofactor is not clear considering that the reaction does not involve redox chemistry.
Present with 31900 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

The regulatory subunit ILV6 stimulates enzymatic activity seven- to tenfold and confers sensitivity to inhibition by valine and activation by ATP.1 Publication

<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=8.6 mM for pyruvate (catalytic subunit only)1 Publication
  2. KM=18.1 mM for pyruvate (reconstituted into the acetolactate synthase complex with the regulatory subunit)1 Publication

pH dependencei

Optimum pH is 7-7.5.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.1 Publication This subpathway is part of the pathway L-isoleucine biosynthesis, 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-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-valine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-valine from pyruvate.1 Publication This subpathway is part of the pathway L-valine biosynthesis, 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-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei139Thiamine pyrophosphate1
Binding sitei241FAD1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi550Magnesium1
Metal bindingi577Magnesium1
Metal bindingi579Magnesium; via carbonyl oxygen1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi355 – 376FAD1 PublicationAdd BLAST22
Nucleotide bindingi407 – 426FAD1 PublicationAdd BLAST20

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionTransferase
Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesis
LigandMagnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.2.1.6, 984

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

More...UniPathwayi		UPA00047;UER00055
UPA00049;UER00059

<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%5Fand%5Ftaxonomy%5Fsection">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:
Acetolactate synthase catalytic subunit, mitochondrialCurated (EC:2.2.1.61 Publication)
Alternative name(s):
Acetohydroxy-acid synthase catalytic subunit1 Publication
Short name:
AHAS
Short name:
ALS
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:ILV2
Synonyms:SMR1
Ordered Locus Names:YMR108W
ORF Names:YM9718.07
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 XIII

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000004714, ILV2

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YMR108W

<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

Mitochondrion

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1075095

<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 'PTM / Processing' section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 90MitochondrionSequence analysisAdd BLAST90
<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_000003566491 – 687Acetolactate synthase catalytic subunit, mitochondrialAdd BLAST597

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P07342

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

More...PaxDbi		P07342

PRoteomics IDEntifications database

More...PRIDEi		P07342

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P07342

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P07342

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer. The acetolactate synthase complex contains the catalytic subunit ILV2 and the regulatory small subunit ILV6.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		35284, 79 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3034, Acetolactate synthase complex

Database of interacting proteins

More...DIPi		DIP-1104N

Protein interaction database and analysis system

More...IntActi		P07342, 73 interactors

Molecular INTeraction database

More...MINTi		P07342

STRING: functional protein association networks

More...STRINGi		4932.YMR108W

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P07342

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P07342, 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

1687
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P07342

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

More...SMRi		P07342

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		P07342

<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>Regioni43 – 68DisorderedSequence analysisAdd BLAST26
Regioni499 – 579Thiamine pyrophosphate bindingAdd BLAST81

<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 TPP enzyme family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG4166, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000176650

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_013748_1_2_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P07342

Identification of Orthologs from Complete Genome Data

More...OMAi		CFGTSGP

Family and domain databases

Conserved Domains Database

More...CDDi		cd02015, TPP_AHAS, 1 hit

Database of protein disorder

More...DisProti		DP00398

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR012846, Acetolactate_synth_lsu
IPR039368, AHAS_TPP
IPR029035, DHS-like_NAD/FAD-binding_dom
IPR029061, THDP-binding
IPR012000, Thiamin_PyroP_enz_cen_dom
IPR012001, Thiamin_PyroP_enz_TPP-bd_dom
IPR000399, TPP-bd_CS
IPR045229, TPP_enz
IPR011766, TPP_enzyme-bd_C

The PANTHER Classification System

More...PANTHERi		PTHR18968, PTHR18968, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02775, TPP_enzyme_C, 1 hit
PF00205, TPP_enzyme_M, 1 hit
PF02776, TPP_enzyme_N, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52467, SSF52467, 1 hit
SSF52518, SSF52518, 2 hits

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00118, acolac_lg, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00187, TPP_ENZYMES, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P07342-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIRQSTLKNF AIKRCFQHIA YRNTPAMRSV ALAQRFYSSS SRYYSASPLP 
        60         70         80         90        100
ASKRPEPAPS FNVDPLEQPA EPSKLAKKLR AEPDMDTSFV GLTGGQIFNE 
       110        120        130        140        150
MMSRQNVDTV FGYPGGAILP VYDAIHNSDK FNFVLPKHEQ GAGHMAEGYA 
       160        170        180        190        200
RASGKPGVVL VTSGPGATNV VTPMADAFAD GIPMVVFTGQ VPTSAIGTDA 
       210        220        230        240        250
FQEADVVGIS RSCTKWNVMV KSVEELPLRI NEAFEIATSG RPGPVLVDLP 
       260        270        280        290        300
KDVTAAILRN PIPTKTTLPS NALNQLTSRA QDEFVMQSIN KAADLINLAK 
       310        320        330        340        350
KPVLYVGAGI LNHADGPRLL KELSDRAQIP VTTTLQGLGS FDQEDPKSLD 
       360        370        380        390        400
MLGMHGCATA NLAVQNADLI IAVGARFDDR VTGNISKFAP EARRAAAEGR 
       410        420        430        440        450
GGIIHFEVSP KNINKVVQTQ IAVEGDATTN LGKMMSKIFP VKERSEWFAQ 
       460        470        480        490        500
INKWKKEYPY AYMEETPGSK IKPQTVIKKL SKVANDTGRH VIVTTGVGQH 
       510        520        530        540        550
QMWAAQHWTW RNPHTFITSG GLGTMGYGLP AAIGAQVAKP ESLVIDIDGD 
       560        570        580        590        600
ASFNMTLTEL SSAVQAGTPV KILILNNEEQ GMVTQWQSLF YEHRYSHTHQ 
       610        620        630        640        650
LNPDFIKLAE AMGLKGLRVK KQEELDAKLK EFVSTKGPVL LEVEVDKKVP 
       660        670        680 
VLPMVAGGSG LDEFINFDPE VERQQTELRH KRTGGKH
Length:687
Mass (Da):74,937
Last modified:April 1, 1988 - v1
<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:iB03C4D0F38AA1362
GO

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
X02549 Genomic DNA Translation: CAA26400.1
Z49702 Genomic DNA Translation: CAA89744.1
AY692995 Genomic DNA Translation: AAT93014.1
BK006946 Genomic DNA Translation: DAA10005.1

Protein sequence database of the Protein Information Resource

More...PIRi		A23808, YCBYI

NCBI Reference Sequences

More...RefSeqi		NP_013826.1, NM_001182608.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YMR108W_mRNA; YMR108W; YMR108W

Database of genes from NCBI RefSeq genomes

More...GeneIDi		855135

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YMR108W

<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
X02549 Genomic DNA Translation: CAA26400.1
Z49702 Genomic DNA Translation: CAA89744.1
AY692995 Genomic DNA Translation: AAT93014.1
BK006946 Genomic DNA Translation: DAA10005.1
PIRiA23808, YCBYI
RefSeqiNP_013826.1, NM_001182608.1

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
1JSCX-ray2.60A/B58-687[»]
1N0HX-ray2.80A/B58-687[»]
1T9AX-ray2.59A/B58-687[»]
1T9BX-ray2.20A/B58-687[»]
1T9CX-ray2.34A/B58-687[»]
1T9DX-ray2.30A/B/C/D58-687[»]
5FEMX-ray2.17A/B58-687[»]
5IMSX-ray1.98A/B58-687[»]
5WKCX-ray2.33A/B/D/E58-687[»]
6BD3X-ray2.28A/B58-687[»]
6BD9X-ray1.98A/B58-687[»]
6U9DX-ray3.19A/B/E/F/I/J/M/N/Q/R/U/V58-687[»]
AlphaFoldDBiP07342
SMRiP07342
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi35284, 79 interactors
ComplexPortaliCPX-3034, Acetolactate synthase complex
DIPiDIP-1104N
IntActiP07342, 73 interactors
MINTiP07342
STRINGi4932.YMR108W

Chemistry databases

BindingDBiP07342
ChEMBLiCHEMBL1075095

PTM databases

CarbonylDBiP07342
iPTMnetiP07342

Proteomic databases

MaxQBiP07342
PaxDbiP07342
PRIDEiP07342

Genome annotation databases

EnsemblFungiiYMR108W_mRNA; YMR108W; YMR108W
GeneIDi855135
KEGGisce:YMR108W

Organism-specific databases

SGDiS000004714, ILV2
VEuPathDBiFungiDB:YMR108W

Phylogenomic databases

eggNOGiKOG4166, Eukaryota
GeneTreeiENSGT00940000176650
HOGENOMiCLU_013748_1_2_1
InParanoidiP07342
OMAiCFGTSGP

Enzyme and pathway databases

UniPathwayiUPA00047;UER00055
UPA00049;UER00059
BRENDAi2.2.1.6, 984

Miscellaneous databases

EvolutionaryTraceiP07342

Protein Ontology

More...PROi		PR:P07342
RNActiP07342, protein

Family and domain databases

CDDicd02015, TPP_AHAS, 1 hit
DisProtiDP00398
InterProiView protein in InterPro
IPR012846, Acetolactate_synth_lsu
IPR039368, AHAS_TPP
IPR029035, DHS-like_NAD/FAD-binding_dom
IPR029061, THDP-binding
IPR012000, Thiamin_PyroP_enz_cen_dom
IPR012001, Thiamin_PyroP_enz_TPP-bd_dom
IPR000399, TPP-bd_CS
IPR045229, TPP_enz
IPR011766, TPP_enzyme-bd_C
PANTHERiPTHR18968, PTHR18968, 1 hit
PfamiView protein in Pfam
PF02775, TPP_enzyme_C, 1 hit
PF00205, TPP_enzyme_M, 1 hit
PF02776, TPP_enzyme_N, 1 hit
SUPFAMiSSF52467, SSF52467, 1 hit
SSF52518, SSF52518, 2 hits
TIGRFAMsiTIGR00118, acolac_lg, 1 hit
PROSITEiView protein in PROSITE
PS00187, TPP_ENZYMES, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiILVB_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: P07342
Secondary accession number(s): D6VZT1
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: May 25, 2022
This is version 226 of the entry and version 1 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, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: 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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