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Entry version 71 (12 Aug 2020)
Sequence version 1 (14 Oct 2008)
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Protein

3-isopropylmalate dehydratase large subunit

Gene

leuC

Organism
Acidithiobacillus ferrooxidans (strain ATCC 53993) (Leptospirillum ferrooxidans (ATCC 53993))
Status
Reviewed-Annotation score:

Annotation score:3 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>
-Protein inferred from homologyi <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 isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.UniRule annotation

<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

[4Fe-4S] clusterUniRule annotationNote: Binds 1 [4Fe-4S] cluster per subunit.UniRule annotation

<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-leucine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. 3-isopropylmalate dehydratase large subunit (leuC), 3-isopropylmalate dehydratase small subunit (leuD)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
This subpathway is part of the pathway L-leucine 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-leucine from 3-methyl-2-oxobutanoate, the pathway L-leucine 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 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 bindingi348Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi409Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi412Iron-sulfur (4Fe-4S)UniRule annotation1

<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
Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesis, Leucine biosynthesis
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
AFER380394:G1GCL-786-MONOMER

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

More...
UniPathwayi
UPA00048;UER00071

<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:
3-isopropylmalate dehydratase large subunitUniRule annotation (EC:4.2.1.33UniRule annotation)
Alternative name(s):
Alpha-IPM isomeraseUniRule annotation
Short name:
IPMIUniRule annotation
Isopropylmalate isomeraseUniRule annotation
<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:leuCUniRule annotation
Ordered Locus Names:Lferr_0775
<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>OrganismiAcidithiobacillus ferrooxidans (strain ATCC 53993) (Leptospirillum ferrooxidans (ATCC 53993))
<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 identifieri380394 [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 lineageiBacteriaProteobacteriaAcidithiobacilliaAcidithiobacillalesAcidithiobacillaceaeAcidithiobacillus

<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_10001356581 – 4703-isopropylmalate dehydratase large subunitAdd BLAST470

<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

Heterodimer of LeuC and LeuD.

UniRule annotation

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
380394.Lferr_0775

<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

<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 aconitase/IPM isomerase family. LeuC type 1 subfamily.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0065, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_006714_3_4_6

KEGG Orthology (KO)

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KOi
K01703

Identification of Orthologs from Complete Genome Data

More...
OMAi
CNMSIEM

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01583, IPMI, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.499.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01026, LeuC_type1, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004430, 3-IsopropMal_deHydase_lsu
IPR015931, Acnase/IPM_dHydase_lsu_aba_1/3
IPR001030, Acoase/IPM_deHydtase_lsu_aba
IPR018136, Aconitase_4Fe-4S_BS
IPR036008, Aconitase_4Fe-4S_dom
IPR033941, IPMI_cat

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00330, Aconitase, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00415, ACONITASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53732, SSF53732, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00170, leuC, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00450, ACONITASE_1, 1 hit
PS01244, ACONITASE_2, 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.

B5ENJ1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSAKTLYDKL WESHVVHTEQ DGGVLLYIDR QLLHEVTSPQ AFSGLRAAGR
60 70 80 90 100
KAWRIDANIA TADHNVPTTD RAAGIADATS RLQVDTLDRN CAEFGIEEFG
110 120 130 140 150
MHDKRQGIVH VIAPEQGLTL PGMTVVCGDS HTATHGALGA LAFGIGTTEV
160 170 180 190 200
EHVLATQCLW ARKSRSMRIW VEGELGNGVT AKDLVLAIIG RIGTAGGTGY
210 220 230 240 250
AIEFAGPAVH ALSVEGRMTL CNMAIEAGAR SGMVGVDAVT IDYLRGRPYA
260 270 280 290 300
PVGKIWDQAV AVWGELHSDP DAQFDAEIRL EATDVAPQVT WGTSPEMVVD
310 320 330 340 350
ISARVPDPAL EKDPVRRKGW SDALAYMDLA AATPISSIAL DKVFIGSCTN
360 370 380 390 400
ARIEDLRAAA AVARGHHKAA SVKAVLVVPG SGLVKAQAEA EGLDRIFRDA
410 420 430 440 450
GFEWREPGCS MCLAMNADRL EPGERCASTS NRNFEGRQGA GGRTHLVSPA
460 470
MAAAAAIAGH FVDVRDWIMH
Length:470
Mass (Da):50,109
Last modified:October 14, 2008 - 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:iADD01E679CA01E97
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
CP001132 Genomic DNA Translation: ACH83025.1

NCBI Reference Sequences

More...
RefSeqi
WP_012536243.1, NC_011206.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
ACH83025; ACH83025; Lferr_0775

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
afe:Lferr_0775

<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
CP001132 Genomic DNA Translation: ACH83025.1
RefSeqiWP_012536243.1, NC_011206.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

STRINGi380394.Lferr_0775

Genome annotation databases

EnsemblBacteriaiACH83025; ACH83025; Lferr_0775
KEGGiafe:Lferr_0775

Phylogenomic databases

eggNOGiCOG0065, Bacteria
HOGENOMiCLU_006714_3_4_6
KOiK01703
OMAiCNMSIEM

Enzyme and pathway databases

UniPathwayiUPA00048;UER00071
BioCyciAFER380394:G1GCL-786-MONOMER

Family and domain databases

CDDicd01583, IPMI, 1 hit
Gene3Di3.30.499.10, 1 hit
HAMAPiMF_01026, LeuC_type1, 1 hit
InterProiView protein in InterPro
IPR004430, 3-IsopropMal_deHydase_lsu
IPR015931, Acnase/IPM_dHydase_lsu_aba_1/3
IPR001030, Acoase/IPM_deHydtase_lsu_aba
IPR018136, Aconitase_4Fe-4S_BS
IPR036008, Aconitase_4Fe-4S_dom
IPR033941, IPMI_cat
PfamiView protein in Pfam
PF00330, Aconitase, 1 hit
PRINTSiPR00415, ACONITASE
SUPFAMiSSF53732, SSF53732, 1 hit
TIGRFAMsiTIGR00170, leuC, 1 hit
PROSITEiView protein in PROSITE
PS00450, ACONITASE_1, 1 hit
PS01244, ACONITASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiLEUC_ACIF5
<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: B5ENJ1
<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 14, 2009
Last sequence update: October 14, 2008
Last modified: August 12, 2020
This is version 71 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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