Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 81 (16 Oct 2019)
Sequence version 1 (04 Apr 2006)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Aconitate hydratase A

Gene

acn

Organism
Francisella tularensis subsp. holarctica (strain LVS)
Status
Reviewed-Annotation score:

Annotation score:4 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

Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Could catalyze the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnA functions as a RNA-binding regulatory protein.By similarity

<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] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster per subunit.By similarity

<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.By similarity
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Aconitate hydratase A (acn)
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.

Pathwayi: propanoate degradation

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi439Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi505Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi508Iron-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

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, 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
FTUL376619:G1G1L-1772-MONOMER

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 ABy similarity (EC:4.2.1.3By similarity)
Short name:
ACNBy similarity
Short name:
AconitaseBy similarity
Alternative name(s):
(2R,3S)-2-methylisocitrate dehydrataseBy similarity
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydrataseBy similarity
Iron-responsive protein-likeBy similarity
Short name:
IRP-likeBy similarity
Probable 2-methyl-cis-aconitate hydrataseBy similarity (EC:4.2.1.99By similarity)
RNA-binding proteinBy similarity
<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:acn
Ordered Locus Names:FTL_1772
<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>OrganismiFrancisella tularensis subsp. holarctica (strain LVS)
<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 identifieri376619 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

<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_00002351661 – 937Aconitate hydratase AAdd BLAST937

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q2A1K3

<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.

By similarity

<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

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

More...
SMRi
Q2A1K3

Database of comparative protein structure models

More...
ModBasei
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
ENOG4108I0Z Bacteria
COG1048 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000025703

KEGG Orthology (KO)

More...
KOi
K01681

Identification of Orthologs from Complete Genome Data

More...
OMAi
REIQYRP

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>. 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_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.

Q2A1K3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSDIKNITKL QIEDKGKKYS LYSLKKLSQE LGKDVTRLPY SIRVLLENQL
60 70 80 90 100
RNIDGYKVKE DDMHKVLDWD AKASSRPEIP HMPARVVMQD FTGVPAVVDL
110 120 130 140 150
AAMRKAIKDA GGDADKINPL VDTAMVIDHS VQVDFYGTKT ALAQNVAKEF
160 170 180 190 200
ERNGERYSLL KWAQKAFDDF IVVPPGMGII HQVNLEYLAK DALVKNINGE
210 220 230 240 250
DVIYPDTLVG TDSHTTMING VGAVGWGVGG IEAEAVMLGQ PYYMVLPDVV
260 270 280 290 300
GVKFTGKLKT GVTATDLVLK VTEVLRKHGV VGKFVEYYGE GLESLSLPDR
310 320 330 340 350
ATIANMTPEY GATIGFFPVD EVTLDFFNNT NRSELVDAAR EMYKEQLLFR
360 370 380 390 400
ENPAEEPEYS NIVEIDLSEV ESNLAGPKRP QDRVAFHDMK KAFAEALVHE
410 420 430 440 450
QGLHGFGLTD EQLQKSAEVK GLNERITHGS VAIAAITSCT NTSNPSLLLG
460 470 480 490 500
AGLLAKKANE KGLKVKPFVK TSLAPGSQVV TQYLEKANLL PELENLGFNL
510 520 530 540 550
VGYGCTTCIG NSGPLDEPVV EAINEADLIV ASVSSGNRNF EGRINPHIKA
560 570 580 590 600
NYLASPIHVV AYALAGTVDF DPVEDAIGKD AEGNDVYLAD IWPTTEEIAA
610 620 630 640 650
IQSHVINSDM FKKAYATVLD GTEEWQKLKA PEGKLYEFDS SSTYIQCPNF
660 670 680 690 700
FEKFAEGNDD LDIKGARTLL MLGDSVTTDH ISPAGAIPEE YPAGQYLKSH
710 720 730 740 750
GVEKKDFNSY GSRRGNHEVM MRGTFANIRI RNLLLDNVEG GFTKYHLDGS
760 770 780 790 800
QQYVFDAAMK YKEKGIPLVI LAGKEYGTGS SRDWAAKGTF LLGVKAVIAE
810 820 830 840 850
SYERIHRSNL VGMGVLPLEY VNGQNAKTLG LDGTEMFNIK NLNNIKPRQI
860 870 880 890 900
VIVEAVHPKT AHTTTFEALA RLDADVDVDY LKNGGILQTV LKDIMGDKKE
910 920 930
SKSTQSTTSK GCGSADTSSE TSCPFAKIAN FFKKLFK
Length:937
Mass (Da):102,704
Last modified:April 4, 2006 - 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:i3784B39F6F6980C9
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
AM233362 Genomic DNA Translation: CAJ80211.1

NCBI Reference Sequences

More...
RefSeqi
WP_003017291.1, NZ_CP009694.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAJ80211; CAJ80211; FTL_1772

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ftl:FTL_1772

<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
AM233362 Genomic DNA Translation: CAJ80211.1
RefSeqiWP_003017291.1, NZ_CP009694.1

3D structure databases

SMRiQ2A1K3
ModBaseiSearch...

Proteomic databases

PRIDEiQ2A1K3

Genome annotation databases

EnsemblBacteriaiCAJ80211; CAJ80211; FTL_1772
KEGGiftl:FTL_1772

Phylogenomic databases

eggNOGiENOG4108I0Z Bacteria
COG1048 LUCA
HOGENOMiHOG000025703
KOiK01681
OMAiREIQYRP

Enzyme and pathway databases

UniPathwayiUPA00223;UER00718
UPA00946
BioCyciFTUL376619:G1G1L-1772-MONOMER

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...

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 nameiACNA_FRATH
<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: Q2A1K3
<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 16, 2006
Last sequence update: April 4, 2006
Last modified: October 16, 2019
This is version 81 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. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again