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Entry version 129 (23 Feb 2022)
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

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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
189518.LA_2350

<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...

Protein-protein interaction databases

STRINGi189518.LA_2350

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

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: February 23, 2022
This is version 129 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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