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Protein

Aconitate hydratase A

Gene

acnA

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

Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA-binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3' UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post-transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript.6 Publications

Miscellaneous

The AcnA activity over a broad pH range might be a useful adaptation for specifically expression in the stationary phase, where the intracellular pH may vary over a wider range. AcnA is resistant to oxidation in vivo.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

[4Fe-4S] cluster2 PublicationsNote: Binds 1 [4Fe-4S] cluster per subunit.2 Publications

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

  1. KM=1.16 mM for citrate1 Publication
  2. KM=0.058 mM for cis-aconitate1 Publication
  3. KM=0.014 mM for isocitrate (using 0.01-0.8 mM substrate)1 Publication
  4. KM=1.77 mM for isocitrate (using 0.8-40 mM substrate)1 Publication
  1. Vmax=6.13 µmol/min/mg enzyme with citrate as substrate1 Publication
  2. Vmax=14.5 µmol/min/mg enzyme with cis-aconitate as substrate1 Publication
  3. Vmax=3.57 µmol/min/mg enzyme using 0.01-0.8 mM isocitrate as substrate1 Publication
  4. Vmax=14.7 µmol/min/mg enzyme using 0.8-40 mM isocitrate as substrate1 Publication

pH dependencei

Optimum pH is 7.4. It retains a high specific activity over a broad pH range.1 Publication

<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: tricarboxylic acid cycle

This protein is involved in step 2 of the subpathway that synthesizes isocitrate from oxaloacetate.Curated
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 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 bindingi435Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi501Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi504Iron-sulfur (4Fe-4S)By similarity1

<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

  • 4 iron, 4 sulfur cluster binding Source: EcoliWiki
  • aconitate hydratase activity Source: EcoliWiki
  • iron ion binding Source: EcoliWiki
  • metal ion binding Source: EcoliWiki
  • mRNA 3'-UTR binding Source: EcoCyc
  • mRNA binding Source: EcoliWiki

GO - Biological processi

  • anaerobic respiration Source: EcoliWiki
  • citrate metabolic process Source: GO_Central
  • glyoxylate cycle Source: EcoliWiki
  • response to oxidative stress Source: EcoliWiki
  • 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:ACONITASE-MONOMER
MetaCyc:ACONITASE-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.2.1.3 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P25516

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

More...
UniPathwayi
UPA00223;UER00718

<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 A1 Publication (EC:4.2.1.31 Publication)
Short name:
ACN1 Publication
Short name:
Aconitase1 Publication
Alternative name(s):
Iron-responsive protein-like1 Publication
Short name:
IRP-like1 Publication
RNA-binding protein1 Publication
Stationary phase enzyme1 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:acnA1 Publication
Synonyms:acn
Ordered Locus Names:b1276, JW1268
<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
EG11325 acnA

<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.4 Publications

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00000766612 – 891Aconitate hydratase AAdd BLAST890

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P25516

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

More...
PaxDbi
P25516

PRoteomics IDEntifications database

More...
PRIDEi
P25516

<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

Induced upon entry into stationary phase by iron, oxidative and salt stress under aerobic conditions. AcnA is subject to CRP-mediated catabolite repression and ArcA-mediated anaerobic repression. AcnA is negatively regulated by ryhB RNA.5 Publications

<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.1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4260134, 23 interactors
851065, 1 interactor

Database of interacting proteins

More...
DIPi
DIP-9043N

Protein interaction database and analysis system

More...
IntActi
P25516, 13 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_1393

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P25516

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

More...
SMRi
P25516

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<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
ENOG4107QM5 Bacteria
COG1048 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000025704

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P25516

KEGG Orthology (KO)

More...
KOi
K01681

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P25516

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.19.10, 1 hit
3.30.499.10, 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
IPR006249 Aconitase/IRP2
IPR018136 Aconitase_4Fe-4S_BS
IPR036008 Aconitase_4Fe-4S_dom
IPR000573 AconitaseA/IPMdHydase_ssu_swvl

The PANTHER Classification System

More...
PANTHERi
PTHR11670 PTHR11670, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00330 Aconitase, 1 hit
PF00694 Aconitase_C, 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
TIGR01341 aconitase_1, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P25516-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSTLREASK DTLQAKDKTY HYYSLPLAAK SLGDITRLPK SLKVLLENLL
60 70 80 90 100
RWQDGNSVTE EDIHALAGWL KNAHADREIA YRPARVLMQD FTGVPAVVDL
110 120 130 140 150
AAMREAVKRL GGDTAKVNPL SPVDLVIDHS VTVDRFGDDE AFEENVRLEM
160 170 180 190 200
ERNHERYVFL KWGKQAFSRF SVVPPGTGIC HQVNLEYLGK AVWSELQDGE
210 220 230 240 250
WIAYPDTLVG TDSHTTMING LGVLGWGVGG IEAEAAMLGQ PVSMLIPDVV
260 270 280 290 300
GFKLTGKLRE GITATDLVLT VTQMLRKHGV VGKFVEFYGD GLDSLPLADR
310 320 330 340 350
ATIANMSPEY GATCGFFPID AVTLDYMRLS GRSEDQVELV EKYAKAQGMW
360 370 380 390 400
RNPGDEPIFT STLELDMNDV EASLAGPKRP QDRVALPDVP KAFAASNELE
410 420 430 440 450
VNATHKDRQP VDYVMNGHQY QLPDGAVVIA AITSCTNTSN PSVLMAAGLL
460 470 480 490 500
AKKAVTLGLK RQPWVKASLA PGSKVVSDYL AKAKLTPYLD ELGFNLVGYG
510 520 530 540 550
CTTCIGNSGP LPDPIETAIK KSDLTVGAVL SGNRNFEGRI HPLVKTNWLA
560 570 580 590 600
SPPLVVAYAL AGNMNINLAS EPIGHDRKGD PVYLKDIWPS AQEIARAVEQ
610 620 630 640 650
VSTEMFRKEY AEVFEGTAEW KGINVTRSDT YGWQEDSTYI RLSPFFDEMQ
660 670 680 690 700
ATPAPVEDIH GARILAMLGD SVTTDHISPA GSIKPDSPAG RYLQGRGVER
710 720 730 740 750
KDFNSYGSRR GNHEVMMRGT FANIRIRNEM VPGVEGGMTR HLPDSDVVSI
760 770 780 790 800
YDAAMRYKQE QTPLAVIAGK EYGSGSSRDW AAKGPRLLGI RVVIAESFER
810 820 830 840 850
IHRSNLIGMG ILPLEFPQGV TRKTLGLTGE EKIDIGDLQN LQPGATVPVT
860 870 880 890
LTRADGSQEV VPCRCRIDTA TELTYYQNDG ILHYVIRNML K
Length:891
Mass (Da):97,677
Last modified:January 15, 2008 - 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:iEB47E5B3C3F9C56C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti522S → G in CAA42834 (PubMed:1541275).Curated1
Sequence conflicti522S → G in BAA14828 (PubMed:16738553).Curated1

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
X60293 Genomic DNA Translation: CAA42834.1
U00096 Genomic DNA Translation: AAC74358.1
AP009048 Genomic DNA Translation: BAA14828.1

Protein sequence database of the Protein Information Resource

More...
PIRi
G64875

NCBI Reference Sequences

More...
RefSeqi
NP_415792.1, NC_000913.3
WP_000099535.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74358; AAC74358; b1276
BAA14828; BAA14828; BAA14828

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
946724

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW1268
eco:b1276

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|511145.12.peg.1327

<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
X60293 Genomic DNA Translation: CAA42834.1
U00096 Genomic DNA Translation: AAC74358.1
AP009048 Genomic DNA Translation: BAA14828.1
PIRiG64875
RefSeqiNP_415792.1, NC_000913.3
WP_000099535.1, NZ_LN832404.1

3D structure databases

ProteinModelPortaliP25516
SMRiP25516
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260134, 23 interactors
851065, 1 interactor
DIPiDIP-9043N
IntActiP25516, 13 interactors
STRINGi316385.ECDH10B_1393

Proteomic databases

EPDiP25516
PaxDbiP25516
PRIDEiP25516

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74358; AAC74358; b1276
BAA14828; BAA14828; BAA14828
GeneIDi946724
KEGGiecj:JW1268
eco:b1276
PATRICifig|511145.12.peg.1327

Organism-specific databases

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

More...
EchoBASEi
EB1301
EcoGeneiEG11325 acnA

Phylogenomic databases

eggNOGiENOG4107QM5 Bacteria
COG1048 LUCA
HOGENOMiHOG000025704
InParanoidiP25516
KOiK01681
PhylomeDBiP25516

Enzyme and pathway databases

UniPathwayi
UPA00223;UER00718

BioCyciEcoCyc:ACONITASE-MONOMER
MetaCyc:ACONITASE-MONOMER
BRENDAi4.2.1.3 2026
SABIO-RKiP25516

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P25516

Family and domain databases

Gene3Di3.20.19.10, 1 hit
3.30.499.10, 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
IPR006249 Aconitase/IRP2
IPR018136 Aconitase_4Fe-4S_BS
IPR036008 Aconitase_4Fe-4S_dom
IPR000573 AconitaseA/IPMdHydase_ssu_swvl
PANTHERiPTHR11670 PTHR11670, 1 hit
PfamiView protein in Pfam
PF00330 Aconitase, 1 hit
PF00694 Aconitase_C, 1 hit
PRINTSiPR00415 ACONITASE
SUPFAMiSSF53732 SSF53732, 1 hit
TIGRFAMsiTIGR01341 aconitase_1, 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...

<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 nameiACNA_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: P25516
Secondary accession number(s): P78060, P78148
<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: May 1, 1992
Last sequence update: January 15, 2008
Last modified: December 5, 2018
This is version 157 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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