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Protein

Aconitate hydratase B

Gene

acnB

Organism
Escherichia coli (strain K12)
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

Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnB functions as a RNA-binding regulatory protein. During oxidative stress inactive AcnB apo-enzyme without iron sulfur clusters binds the acnB mRNA 3' UTRs (untranslated regions), stabilizes acnB mRNA and increases AcnB synthesis, thus mediating a post-transcriptional positive autoregulatory switch. AcnB also decreases the stability of the sodA transcript.7 Publications

Miscellaneous

AcnB is sensitive to oxidation in vivo.1 Publication

<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

[4Fe-4S] cluster1 PublicationNote: Binds 1 [4Fe-4S] cluster per subunit.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=11 mM for citrate2 Publications
  2. KM=0.016 mM for cis-aconitate2 Publications
  3. KM=0.051 mM for isocitrate (using 0.01-0.8 mM substrate)2 Publications
  4. KM=19.7 mM for isocitrate (using 0.8-40 mM substrate)2 Publications
  5. KM=0.21 mM for (2R,3S)-2-methylisocitrate2 Publications
  1. Vmax=23.8 µmol/min/mg enzyme with citrate as substrate2 Publications
  2. Vmax=39.1 µmol/min/mg enzyme with cis-aconitate as substrate2 Publications
  3. Vmax=5.92 µmol/min/mg enzyme using 0.01-0.8 mM isocitrate as substrate2 Publications
  4. Vmax=57.8 µmol/min/mg enzyme using 0.8-40 mM isocitrate as substrate2 Publications

pH dependencei

Optimum pH is 7.4.2 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: propanoate degradation

This protein is involved in the pathway propanoate degradation, which is part of Organic acid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway propanoate degradation and in Organic acid metabolism.

Pathwayi: tricarboxylic acid cycle

This protein is involved in step 2 of the subpathway that synthesizes isocitrate from oxaloacetate.1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. 2-methylcitrate synthase (prpC), Citrate synthase (gltA)
  2. 2-methylcitrate dehydratase (prpD), Aconitate hydratase B (acnB), Aconitate hydratase A (acnA)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isocitrate from oxaloacetate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

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 sitei191Substrate1 Publication1
Binding sitei498Substrate1 Publication1
<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 bindingi710Iron-sulfur (4Fe-4S)1 Publication1
Metal bindingi769Iron-sulfur (4Fe-4S)1 Publication1
Metal bindingi772Iron-sulfur (4Fe-4S)1 Publication1
Binding sitei791Substrate1 Publication1
Binding sitei796Substrate1 Publication1

<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

  • glyoxylate cycle Source: EcoliWiki
  • propionate catabolic process, 2-methylcitrate cycle Source: EcoCyc
  • regulation of translation Source: EcoCyc
  • tricarboxylic acid cycle Source: GO_Central

<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, RNA-binding
Biological processTricarboxylic acid cycle
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:ACONITATEDEHYDRB-MONOMER
MetaCyc:ACONITATEDEHYDRB-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.2.1.3 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P36683

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

More...
UniPathwayi
UPA00223;UER00718

UPA00946

<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:
Aconitate hydratase B1 Publication (EC:4.2.1.31 Publication)
Short name:
ACN1 Publication
Short name:
Aconitase1 Publication
Alternative name(s):
(2R,3S)-2-methylisocitrate dehydratase1 Publication
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase1 Publication
2-methyl-cis-aconitate hydratase1 Publication (EC:4.2.1.991 Publication)
Iron-responsive protein-like1 Publication
Short name:
IRP-like1 Publication
RNA-binding protein1 Publication
<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:acnB1 Publication
Synonyms:yacI, yacJ
Ordered Locus Names:b0118, JW0114
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG12316 acnB

<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

Cells lacking this gene are more sensitive to peroxide stress. The acnAB double mutant does not grow on unsupplemented glucose minimal medium and does not respond under aerobic conditions to glutamate. The acnAB double mutant retains a low but significant aconitase activity.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi769C → S: Inhibits the dimer formation. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB04351 Aconitate Ion

<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_00000766751 – 865Aconitate hydratase BAdd BLAST865

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P36683

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

More...
PaxDbi
P36683

PRoteomics IDEntifications database

More...
PRIDEi
P36683

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P36683

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P36683

<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

Monomer. AcnB can also form a homodimer. The monomer-homodimer transition is dependent on iron availability and the carboxymethylation of C-273 inhibits the dimer formation.3 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4261902, 105 interactors
849264, 1 interactor

Database of interacting proteins

More...
DIPi
DIP-9044N

Protein interaction database and analysis system

More...
IntActi
P36683, 15 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_0098

<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

1865
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P36683

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

More...
SMRi
P36683

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P36683

<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>Regioni244 – 246Substrate binding1 Publication3
Regioni414 – 416Substrate binding1 Publication3

<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.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4107QIJ Bacteria
COG1049 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000205991

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P36683

KEGG Orthology (KO)

More...
KOi
K01682

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P36683

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01576 AcnB_Swivel, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.25.40.310, 1 hit
3.20.19.10, 1 hit
3.30.499.10, 2 hits
3.40.1060.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR015931 Acnase/IPM_dHydase_lsu_aba_1/3
IPR001030 Acoase/IPM_deHydtase_lsu_aba
IPR015928 Aconitase/3IPM_dehydase_swvl
IPR018136 Aconitase_4Fe-4S_BS
IPR036008 Aconitase_4Fe-4S_dom
IPR004406 Aconitase_B
IPR015933 Aconitase_B_HEAT-like_dom
IPR036288 Aconitase_B_HEAT-like_dom_sf
IPR015929 Aconitase_B_swivel
IPR015932 Aconitase_dom2

The PANTHER Classification System

More...
PANTHERi
PTHR43160:SF1 PTHR43160:SF1, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00330 Aconitase, 1 hit
PF06434 Aconitase_2_N, 1 hit
PF11791 Aconitase_B_N, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF036687 AcnB, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53732 SSF53732, 1 hit
SSF74778 SSF74778, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00117 acnB, 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_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.

P36683-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLEEYRKHVA ERAAEGIAPK PLDANQMAAL VELLKNPPAG EEEFLLDLLT
60 70 80 90 100
NRVPPGVDEA AYVKAGFLAA IAKGEAKSPL LTPEKAIELL GTMQGGYNIH
110 120 130 140 150
PLIDALDDAK LAPIAAKALS HTLLMFDNFY DVEEKAKAGN EYAKQVMQSW
160 170 180 190 200
ADAEWFLNRP ALAEKLTVTV FKVTGETNTD DLSPAPDAWS RPDIPLHALA
210 220 230 240 250
MLKNAREGIE PDQPGVVGPI KQIEALQQKG FPLAYVGDVV GTGSSRKSAT
260 270 280 290 300
NSVLWFMGDD IPHVPNKRGG GLCLGGKIAP IFFNTMEDAG ALPIEVDVSN
310 320 330 340 350
LNMGDVIDVY PYKGEVRNHE TGELLATFEL KTDVLIDEVR AGGRIPLIIG
360 370 380 390 400
RGLTTKAREA LGLPHSDVFR QAKDVAESDR GFSLAQKMVG RACGVKGIRP
410 420 430 440 450
GAYCEPKMTS VGSQDTTGPM TRDELKDLAC LGFSADLVMQ SFCHTAAYPK
460 470 480 490 500
PVDVNTHHTL PDFIMNRGGV SLRPGDGVIH SWLNRMLLPD TVGTGGDSHT
510 520 530 540 550
RFPIGISFPA GSGLVAFAAA TGVMPLDMPE SVLVRFKGKM QPGITLRDLV
560 570 580 590 600
HAIPLYAIKQ GLLTVEKKGK KNIFSGRILE IEGLPDLKVE QAFELTDASA
610 620 630 640 650
ERSAAGCTIK LNKEPIIEYL NSNIVLLKWM IAEGYGDRRT LERRIQGMEK
660 670 680 690 700
WLANPELLEA DADAEYAAVI DIDLADIKEP ILCAPNDPDD ARPLSAVQGE
710 720 730 740 750
KIDEVFIGSC MTNIGHFRAA GKLLDAHKGQ LPTRLWVAPP TRMDAAQLTE
760 770 780 790 800
EGYYSVFGKS GARIEIPGCS LCMGNQARVA DGATVVSTST RNFPNRLGTG
810 820 830 840 850
ANVFLASAEL AAVAALIGKL PTPEEYQTYV AQVDKTAVDT YRYLNFNQLS
860
QYTEKADGVI FQTAV
Length:865
Mass (Da):93,498
Last modified:November 1, 1997 - v3
<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:iFEC8AA5D2A9DD2BD
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC73229.1
AP009048 Genomic DNA Translation: BAB96692.2
U41560 Genomic DNA Translation: AAC43710.1

Protein sequence database of the Protein Information Resource

More...
PIRi
F64734

NCBI Reference Sequences

More...
RefSeqi
NP_414660.1, NC_000913.3
WP_001307570.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73229; AAC73229; b0118
BAB96692; BAB96692; BAB96692

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
944864

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0114
eco:b0118

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2164

<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
U00096 Genomic DNA Translation: AAC73229.1
AP009048 Genomic DNA Translation: BAB96692.2
U41560 Genomic DNA Translation: AAC43710.1
PIRiF64734
RefSeqiNP_414660.1, NC_000913.3
WP_001307570.1, NZ_LN832404.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L5JX-ray2.40A/B1-865[»]
ProteinModelPortaliP36683
SMRiP36683
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261902, 105 interactors
849264, 1 interactor
DIPiDIP-9044N
IntActiP36683, 15 interactors
STRINGi316385.ECDH10B_0098

Chemistry databases

DrugBankiDB04351 Aconitate Ion

PTM databases

CarbonylDBiP36683

2D gel databases

SWISS-2DPAGEiP36683

Proteomic databases

EPDiP36683
PaxDbiP36683
PRIDEiP36683

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73229; AAC73229; b0118
BAB96692; BAB96692; BAB96692
GeneIDi944864
KEGGiecj:JW0114
eco:b0118
PATRICifig|1411691.4.peg.2164

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB2222
EcoGeneiEG12316 acnB

Phylogenomic databases

eggNOGiENOG4107QIJ Bacteria
COG1049 LUCA
HOGENOMiHOG000205991
InParanoidiP36683
KOiK01682
PhylomeDBiP36683

Enzyme and pathway databases

UniPathwayi
UPA00223;UER00718

UPA00946

BioCyciEcoCyc:ACONITATEDEHYDRB-MONOMER
MetaCyc:ACONITATEDEHYDRB-MONOMER
BRENDAi4.2.1.3 2026
SABIO-RKiP36683

Miscellaneous databases

EvolutionaryTraceiP36683

Protein Ontology

More...
PROi
PR:P36683

Family and domain databases

CDDicd01576 AcnB_Swivel, 1 hit
Gene3Di1.25.40.310, 1 hit
3.20.19.10, 1 hit
3.30.499.10, 2 hits
3.40.1060.10, 1 hit
InterProiView protein in InterPro
IPR015931 Acnase/IPM_dHydase_lsu_aba_1/3
IPR001030 Acoase/IPM_deHydtase_lsu_aba
IPR015928 Aconitase/3IPM_dehydase_swvl
IPR018136 Aconitase_4Fe-4S_BS
IPR036008 Aconitase_4Fe-4S_dom
IPR004406 Aconitase_B
IPR015933 Aconitase_B_HEAT-like_dom
IPR036288 Aconitase_B_HEAT-like_dom_sf
IPR015929 Aconitase_B_swivel
IPR015932 Aconitase_dom2
PANTHERiPTHR43160:SF1 PTHR43160:SF1, 1 hit
PfamiView protein in Pfam
PF00330 Aconitase, 1 hit
PF06434 Aconitase_2_N, 1 hit
PF11791 Aconitase_B_N, 1 hit
PIRSFiPIRSF036687 AcnB, 1 hit
SUPFAMiSSF53732 SSF53732, 1 hit
SSF74778 SSF74778, 1 hit
TIGRFAMsiTIGR00117 acnB, 1 hit
PROSITEiView protein in PROSITE
PS00450 ACONITASE_1, 1 hit
PS01244 ACONITASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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<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 nameiACNB_ECOLI
<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: P36683
Secondary accession number(s): P36648, P75652, Q59382
<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: June 1, 1994
Last sequence update: November 1, 1997
Last modified: December 5, 2018
This is version 169 of the entry and version 3 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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