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Entry version 128 (02 Jun 2021)
Sequence version 1 (01 Mar 2003)
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Protein

(R)-citramalate synthase CimA

Gene

cimA

Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
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 condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate (PubMed:15292141, PubMed:18498255, PubMed:19351325).

Shows strict substrate specificity for pyruvate. Cannot use alpha-ketoisovalerate, alpha-ketobutyrate, alpha-ketoisocaproate, alpha-ketoglutarate or glyoxylate (PubMed:15292141, PubMed:18498255).

3 Publications

<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

Mn2+1 PublicationNote: Mn2+ is the most effective activator, followed by Co2+, Ca2+, Mg2+ and Ni2+.1 Publication

<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

Regulated by the end-product isoleucine via a feedback inhibition. The binding of isoleucine has inhibitory effects on the binding of both pyruvate and acetyl-CoA. May act via conformational change of the dimer interface of the regulatory domain, leading to inhibition of the catalytic reaction.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

kcat is 2.41 sec(-1) (PubMed:15292141). kcat is 10.3 sec(-1) with acetyl-CoA as substrate (PubMed:18498255). kcat is 9.13 sec(-1) with pyruvate as substrate (PubMed:18498255).2 Publications
  1. KM=43 µM for pyruvate1 Publication
  2. KM=60 µM for pyruvate1 Publication
  3. KM=1118 µM for acetyl-CoA1 Publication

    Temperature dependencei

    Optimum temperature is 35-40 degrees Celsius.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 2-oxobutanoate from pyruvate.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 2-oxobutanoate from pyruvate, the pathway L-isoleucine 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 is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei16Proton donor1 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 bindingi17Manganese2 Publications1
    <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 sitei144Pyruvate1 Publication1
    Active sitei146Proton acceptor1 Publication1
    Binding sitei179Pyruvate1 Publication1
    Metal bindingi207Manganese; via tele nitrogen2 Publications1
    Metal bindingi209Manganese; via tele nitrogen2 Publications1

    <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 functionLyase, Transferase
    Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesis, Isoleucine biosynthesis
    LigandManganese, Metal-binding, Pyruvate

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    LINT189518:G1GL4-1907-MONOMER
    MetaCyc:MONOMER-11894

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

    More...
    UniPathwayi
    UPA00047;UER00066

    <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:
    (R)-citramalate synthase CimACurated (EC:2.3.1.1823 Publications)
    Alternative name(s):
    LiCMS1 Publication
    <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:cimA1 Publication
    Ordered Locus Names:LA_2350Imported
    <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>OrganismiLeptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
    <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 identifieri189518 [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 lineageiBacteriaSpirochaetesLeptospiralesLeptospiraceaeLeptospira
    <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
    • UP000001408 <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 I

    <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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi16R → K or Q: Loss of activity. 1 Publication1
    Mutagenesisi17D → A: 34-fold increase in Km for pyruvate and 315-fold decrease in kcat. 1 Publication1
    Mutagenesisi17D → N: 4.4-fold increase in Km for pyruvate and 480-fold decrease in kcat. 1 Publication1
    Mutagenesisi81L → A: 4.7-fold increase in Km for pyruvate and 15.7-fold decrease in kcat. 1 Publication1
    Mutagenesisi81L → V: 3.3-fold increase in Km for pyruvate and 10.1-fold decrease in kcat. 1 Publication1
    Mutagenesisi83F → A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat. 1 Publication1
    Mutagenesisi104L → V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat. 1 Publication1
    Mutagenesisi144Y → L: 259-fold increase in Km for pyruvate and 76-fold decrease in kcat. 1 Publication1
    Mutagenesisi144Y → V: 114-fold increase in Km for pyruvate and 5.3-fold decrease in kcat. 1 Publication1
    Mutagenesisi146E → D or Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat. 1 Publication1
    Mutagenesisi179T → A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat. 1 Publication1
    Mutagenesisi302H → A or N: Loss of activity. 1 Publication1
    Mutagenesisi304D → A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat. 1 Publication1
    Mutagenesisi310N → A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat. 1 Publication1
    Mutagenesisi311L → A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat. 1 Publication1
    Mutagenesisi312Y → A: Loss of activity. 1 Publication1
    Mutagenesisi430Y → L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine. 1 Publication1
    Mutagenesisi431D → A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat. 1 Publication1
    Mutagenesisi451L → V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat. 1 Publication1
    Mutagenesisi454Y → A: 1.4 decrease in Km for acetyl-CoA and 17-fold decrease in kcat. Still inhibited by isoleucine and weakly inhibited by leucine. 1 Publication1
    Mutagenesisi458I → A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine. 1 Publication1
    Mutagenesisi464T → A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat. 1 Publication1
    Mutagenesisi468V → A: No change in Km for acetyl-CoA and 2-fold decrease in kcat. Increases inhibition by isoleucine and leucine becomes an effective inhibitor. 1 Publication1
    Mutagenesisi493P → A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat. 1 Publication1
    Mutagenesisi495Q → A: 1.6-fold decrease in Km for acetyl-CoA and 2.8-fold decrease in kcat. 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 '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_00004494241 – 516(R)-citramalate synthase CimAAdd BLAST516

    <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

    Expression is repressed by isoleucine but not by leucine.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%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.

    2 Publications

    <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

    1516
    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
    Q8F3Q1

    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
    Q8F3Q1

    <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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini8 – 269Pyruvate carboxyltransferasePROSITE-ProRule annotationAdd BLAST262

    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>Regioni16 – 17Pyruvate binding1 Publication2

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    Contains a catalytic N-terminal domain and a C-terminal regulatory domain, linked together by a flexible region (PubMed:18498255, PubMed:19351325). The catalytic domain consists of a TIM barrel flanked by an extended C-terminal region. The active site is located at the center of the TIM barrel near the C-terminal ends of the beta-strands and is composed of conserved residues of the beta-strands of one subunit and the C-terminal region of the other (PubMed:18498255).2 Publications

    <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

    Phylogenomic databases

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_022158_0_1_12

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    DWSNGMR

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.20.20.70, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR013709, 2-isopropylmalate_synth_dimer
    IPR002034, AIPM/Hcit_synth_CS
    IPR013785, Aldolase_TIM
    IPR036230, LeuA_allosteric_dom_sf
    IPR000891, PYR_CT

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00682, HMGL-like, 1 hit
    PF08502, LeuA_dimer, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00917, LeuA_dimer, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF110921, SSF110921, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00815, AIPM_HOMOCIT_SYNTH_1, 1 hit
    PS50991, PYR_CT, 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.

    Q8F3Q1-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTKVETRLEI LDVTLRDGEQ TRGVSFSTSE KLNIAKFLLQ KLNVDRVEIA
    60 70 80 90 100
    SARVSKGELE TVQKIMEWAA TEQLTERIEI LGFVDGNKTV DWIKDSGAKV
    110 120 130 140 150
    LNLLTKGSLH HLEKQLGKTP KEFFTDVSFV IEYAIKSGLK INVYLEDWSN
    160 170 180 190 200
    GFRNSPDYVK SLVEHLSKEH IERIFLPDTL GVLSPEETFQ GVDSLIQKYP
    210 220 230 240 250
    DIHFEFHGHN DYDLSVANSL QAIRAGVKGL HASINGLGER AGNTPLEALV
    260 270 280 290 300
    TTIHDKSNSK TNINEIAITE ASRLVEVFSG KRISANRPIV GEDVFTQTAG
    310 320 330 340 350
    VHADGDKKGN LYANPILPER FGRKRSYALG KLAGKASISE NVKQLGMVLS
    360 370 380 390 400
    EVVLQKVLER VIELGDQNKL VTPEDLPFII ADVSGRTGEK VLTIKSCNIH
    410 420 430 440 450
    SGIGIRPHAQ IELEYQGKIH KEISEGDGGY DAFMNALTKI TNRLGISIPK
    460 470 480 490 500
    LIDYEVRIPP GGKTDALVET RITWNKSLDL EEDQTFKTMG VHPDQTVAAV
    510
    HATEKMLNQI LQPWQI
    Length:516
    Mass (Da):57,319
    Last modified:March 1, 2003 - 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:i4F0DE93214537124
    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
    AE010300 Genomic DNA Translation: AAN49549.1

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_712531.1, NC_004342.2
    WP_000169689.1, NC_004342.2

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAN49549; AAN49549; LA_2350

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    lil:LA_2350

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|189518.3.peg.2333

    <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
    AE010300 Genomic DNA Translation: AAN49549.1
    RefSeqiNP_712531.1, NC_004342.2
    WP_000169689.1, NC_004342.2

    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
    3BLEX-ray2.00A1-325[»]
    3BLFX-ray2.60A1-325[»]
    3BLIX-ray2.50A1-325[»]
    3F6GX-ray2.00A/B390-516[»]
    3F6HX-ray2.70A/B390-516[»]
    SMRiQ8F3Q1
    ModBaseiSearch...
    PDBe-KBiSearch...

    Genome annotation databases

    EnsemblBacteriaiAAN49549; AAN49549; LA_2350
    KEGGilil:LA_2350
    PATRICifig|189518.3.peg.2333

    Phylogenomic databases

    HOGENOMiCLU_022158_0_1_12
    OMAiDWSNGMR

    Enzyme and pathway databases

    UniPathwayiUPA00047;UER00066
    BioCyciLINT189518:G1GL4-1907-MONOMER
    MetaCyc:MONOMER-11894

    Miscellaneous databases

    EvolutionaryTraceiQ8F3Q1

    Family and domain databases

    Gene3Di3.20.20.70, 1 hit
    InterProiView protein in InterPro
    IPR013709, 2-isopropylmalate_synth_dimer
    IPR002034, AIPM/Hcit_synth_CS
    IPR013785, Aldolase_TIM
    IPR036230, LeuA_allosteric_dom_sf
    IPR000891, PYR_CT
    PfamiView protein in Pfam
    PF00682, HMGL-like, 1 hit
    PF08502, LeuA_dimer, 1 hit
    SMARTiView protein in SMART
    SM00917, LeuA_dimer, 1 hit
    SUPFAMiSSF110921, SSF110921, 1 hit
    PROSITEiView protein in PROSITE
    PS00815, AIPM_HOMOCIT_SYNTH_1, 1 hit
    PS50991, PYR_CT, 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 nameiCIMA_LEPIN
    <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: Q8F3Q1
    <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 22, 2020
    Last sequence update: March 1, 2003
    Last modified: June 2, 2021
    This is version 128 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

    3D-structure, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
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