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Protein

Acetolactate synthase large subunit IlvB1

Gene

ilvB1

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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 conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine. Also involved in condensing pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate.2 Publications

<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 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:
  • Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity
  • thiamine diphosphateBy similarityNote: Binds 1 thiamine pyrophosphate per subunit.By similarity

<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 valine, sulfometuron methyl (SM), sulfonylureas (SU) and imidazolinones (IM). Pyrazosulfuron ethyl (PSE), promisulfuron methyl (PSM), sulfometuron methyl (SMM), metsulfuron methyl (MSM), and chlorimuron ethyl (CE) inhibited more than 80% of the activity.2 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=2.76 mM for pyruvate (with the catalytic subunit alone at pH 7.5 and at 37 degrees Celsius)2 Publications
  2. KM=1.56 mM for pyruvate (with the catalytic and regulatory subunits at pH 7.5 and at 37 degrees Celsius)2 Publications

    pH dependencei

    Optimum pH is between 6 and 7.2 Publications

    Temperature dependencei

    Optimum temperature is between 35 and 40 degrees Celsius.2 Publications

    <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-isoleucine biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. Acetolactate synthase (LH57_16400), Acetolactate synthase large subunit IlvB1 (ilvB1), Putative acetolactate synthase large subunit IlvB2 (ilvB2), Acetolactate synthase large subunit IlvG (ilvG), Putative acetolactate synthase small subunit (ilvH), Putative acetolactate synthase large subunit IlvX (ilvX)
    2. Ketol-acid reductoisomerase (NADP(+)) (ilvC), Ketol-acid reductoisomerase (NADP(+)) (ilvC)
    3. Dihydroxy-acid dehydratase (ilvD), Dihydroxy-acid dehydratase (ilvD)
    4. Branched-chain-amino-acid aminotransferase (LH57_12040), Branched-chain-amino-acid aminotransferase (ilvE)
    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.
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. Acetolactate synthase (LH57_16400), Acetolactate synthase large subunit IlvB1 (ilvB1), Putative acetolactate synthase large subunit IlvB2 (ilvB2), Acetolactate synthase large subunit IlvG (ilvG), Putative acetolactate synthase small subunit (ilvH), Putative acetolactate synthase large subunit IlvX (ilvX)
    2. Ketol-acid reductoisomerase (NADP(+)) (ilvC), Ketol-acid reductoisomerase (NADP(+)) (ilvC)
    3. Dihydroxy-acid dehydratase (ilvD), Dihydroxy-acid dehydratase (ilvD)
    4. Branched-chain-amino-acid aminotransferase (LH57_12040), Branched-chain-amino-acid aminotransferase (ilvE)
    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 ‘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 sitei85Thiamine pyrophosphateBy similarity1
    Binding sitei187FADBy similarity1
    <p>This subsection of the ‘Function’ 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 bindingi480MagnesiumBy similarity1
    Metal bindingi507MagnesiumBy similarity1

    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 bindingi293 – 314FADBy similarityAdd BLAST22
    Nucleotide bindingi336 – 355FADBy similarityAdd 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

    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 functionTransferase
    Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesis
    LigandFAD, Flavoprotein, Magnesium, Metal-binding, Thiamine pyrophosphate

    Enzyme and pathway databases

    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_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:
    Acetolactate synthase large subunit IlvB1 (EC:2.2.1.6)
    Short name:
    ALS
    Alternative name(s):
    Acetohydroxy-acid synthase large subunit
    Short name:
    AHAS
    <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:ilvB1
    Ordered Locus Names:Rv3003c
    ORF Names:MTV012.17c
    <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>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    <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 identifieri83332 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    <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
    • UP000001584 <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

    Organism-specific databases

    Mycobacterium tuberculosis strain H37Rv genome database

    More...
    TubercuListi
    Rv3003c

    <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

    GO - Cellular componenti

    <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

    <p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Auxotrophic for all of the 3 branched-chain amino acids (isoleucine, leucine and valine), when grown with either C6 or C2 carbon sources. Depletion of these branched chain amino acids in the medium led to loss of viability.1 Publication

    <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 polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000908031 – 618Acetolactate synthase large subunit IlvB1Add BLAST618

    Proteomic databases

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

    More...
    PaxDbi
    P9WG41

    <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

    The expression is high during the mid-exponential phase and low during the stationary phase.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

    Heterodimer of large catalytic subunit and small regulatory subunit.1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    83332.Rv3003c

    <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

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P9WG41

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

    More...
    SMRi
    P9WG41

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <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>Regioni429 – 509Thiamine 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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105C7K Bacteria
    COG0028 LUCA

    KEGG Orthology (KO)

    More...
    KOi
    K01652

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    QGMVRQW

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P9WG41

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd02015 TPP_AHAS, 1 hit

    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
    IPR011766 TPP_enzyme-bd_C

    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_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.

    P9WG41-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSAPTKPHSP TFKPEPHSAA NEPKHPAARP KHVALQQLTG AQAVIRSLEE
    60 70 80 90 100
    LGVDVIFGIP GGAVLPVYDP LFDSKKLRHV LVRHEQGAGH AASGYAHVTG
    110 120 130 140 150
    RVGVCMATSG PGATNLVTPL ADAQMDSIPV VAITGQVGRG LIGTDAFQEA
    160 170 180 190 200
    DISGITMPIT KHNFLVRSGD DIPRVLAEAF HIAASGRPGA VLVDIPKDVL
    210 220 230 240 250
    QGQCTFSWPP RMELPGYKPN TKPHSRQVRE AAKLIAAARK PVLYVGGGVI
    260 270 280 290 300
    RGEATEQLRE LAELTGIPVV TTLMARGAFP DSHRQNLGMP GMHGTVAAVA
    310 320 330 340 350
    ALQRSDLLIA LGTRFDDRVT GKLDSFAPEA KVIHADIDPA EIGKNRHADV
    360 370 380 390 400
    PIVGDVKAVI TELIAMLRHH HIPGTIEMAD WWAYLNGVRK TYPLSYGPQS
    410 420 430 440 450
    DGSLSPEYVI EKLGEIAGPD AVFVAGVGQH QMWAAQFIRY EKPRSWLNSG
    460 470 480 490 500
    GLGTMGFAIP AAMGAKIALP GTEVWAIDGD GCFQMTNQEL ATCAVEGIPV
    510 520 530 540 550
    KVALINNGNL GMVRQWQSLF YAERYSQTDL ATHSHRIPDF VKLAEALGCV
    560 570 580 590 600
    GLRCEREEDV VDVINQARAI NDCPVVIDFI VGADAQVWPM VAAGTSNDEI
    610
    QAARGIRPLF DDITEGHA
    Length:618
    Mass (Da):66,123
    Last modified:April 16, 2014 - 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:i9E0523F4AD6EC6AF
    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
    AL123456 Genomic DNA Translation: CCP45809.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    F70855

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_003415168.1, NZ_NVQJ01000041.1
    YP_177917.1, NC_000962.3

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CCP45809; CCP45809; Rv3003c

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    887286

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mtu:Rv3003c

    <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
    AL123456 Genomic DNA Translation: CCP45809.1
    PIRiF70855
    RefSeqiWP_003415168.1, NZ_NVQJ01000041.1
    YP_177917.1, NC_000962.3

    3D structure databases

    ProteinModelPortaliP9WG41
    SMRiP9WG41
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv3003c

    Proteomic databases

    PaxDbiP9WG41

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCCP45809; CCP45809; Rv3003c
    GeneIDi887286
    KEGGimtu:Rv3003c

    Organism-specific databases

    TubercuListiRv3003c

    Phylogenomic databases

    eggNOGiENOG4105C7K Bacteria
    COG0028 LUCA
    KOiK01652
    OMAiQGMVRQW
    PhylomeDBiP9WG41

    Enzyme and pathway databases

    UniPathwayi
    UPA00047;UER00055

    UPA00049;UER00059

    Family and domain databases

    CDDicd02015 TPP_AHAS, 1 hit
    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
    IPR011766 TPP_enzyme-bd_C
    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

    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 nameiILVB1_MYCTU
    <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: P9WG41
    Secondary accession number(s): L0TCV7, O53250, P0A622
    <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: April 16, 2014
    Last sequence update: April 16, 2014
    Last modified: December 5, 2018
    This is version 25 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 programProkaryotic 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
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