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UniProtKB - Q8NQ98 (ACNA_CORGL)

Entry version 118 (10 Feb 2021)
Sequence version 2 (07 Feb 2006)
Previous versions | rss
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Protein

Aconitate hydratase A

Gene

acn

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025)
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 probably via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate (PubMed:21984793, PubMed:20647021). 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).By similarity2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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

[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

kcat is 19.6 sec(-1) for aconitase activity with citrate as substrate (at pH 8). kcat is 28.9 sec(-1) for aconitase activity with isocitrate as substrate (at pH 8). kcat is 71 sec(-1) for aconitase activity with cis-aconitate as substrate (at pH 8).1 Publication
  1. KM=18.5 µM for cis-aconitate (at pH 8)1 Publication
  2. KM=480 µM for citrate (at pH 8)1 Publication
  3. KM=552 µM for isocitrate (at pH 8)1 Publication
  1. Vmax=11.2 µmol/min/mg enzyme with citrate as substrate (at pH 8)1 Publication
  2. Vmax=16.5 µmol/min/mg enzyme with isocitrate as substrate (at pH 8)1 Publication
  3. Vmax=40.6 µmol/min/mg enzyme with cis-aconitate as substrate (at pH 8)1 Publication

pH dependencei

Optimum pH is between 7.5 and 7.75.1 Publication

Temperature dependencei

Optimum temperature is 50 degrees Celsius.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: 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 dehydratase 2 (prpD2), 2-methylcitrate synthase 2 (prpC2), Citrate synthase (gltA)
  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.1 Publication
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%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 bindingi475Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi541Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi544Iron-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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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
LigandIron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		CORYNE:G18NG-11125-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%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:
Aconitate hydratase A1 Publication (EC:4.2.1.31 Publication)
Short name:
ACN1 Publication
Short name:
Aconitase1 Publication
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%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:acn
Ordered Locus Names:Cgl1540, cg1737
<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>OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025)
<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 identifieri196627 [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 lineageiBacteria › Actinobacteria › Corynebacteriales › Corynebacteriaceae › Corynebacterium ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000582 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<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 glutamate auxotrophic in glucose minimal medium, show a strong growth defect, and secret large amounts of acetate. Deletion causes a strong selection pressure for secondary mutations within the gltA gene, which might be caused by a growth-inhibitory level of cytoplasmic citrate.1 Publication

<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_00000766571 – 939Aconitate hydratase AAdd BLAST939

2D gel databases

The World-2DPAGE database

More...World-2DPAGEi		0001:Q8NQ98

<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

Repressed by AcnR, RipA, GlxR and activated by RamA. Repression by RipA is part of iron homeostasis and serves to reduce the iron demand under iron limitation. The activation of acn transcription by RamA serves to allow the increased carbon flux through the TCA cycle during growth on acetate. GlxR is a global regulator that binds to the acn promoter and presumably represses its transcription in the presence of cyclic AMP (cAMP).4 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%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

Monomer.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		196627.cg1737

<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		Q8NQ98

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		COG1048, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_013476_2_1_11

Identification of Orthologs from Complete Genome Data

More...OMAi		NGGIMQY

Family and domain databases

Conserved Domains Database

More...CDDi		cd01580, AcnA_IRP_Swivel, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.20.19.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR044137, AcnA_IRP_Swivel
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

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.

Q8NQ98-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTESKNSFNA KSTLEVGDKS YDYFALSAVP GMEKLPYSLK VLGENLLRTE 
        60         70         80         90        100
DGANITNEHI EAIANWDASS DPSIEIQFTP ARVLMQDFTG VPCVVDLATM 
       110        120        130        140        150
REAVAALGGD PNDVNPLNPA EMVIDHSVIV EAFGRPDALA KNVEIEYERN 
       160        170        180        190        200
EERYQFLRWG SESFSNFRVV PPGTGIVHQV NIEYLARVVF DNEGLAYPDT 
       210        220        230        240        250
CIGTDSHTTM ENGLGILGWG VGGIEAEAAM LGQPVSMLIP RVVGFKLTGE 
       260        270        280        290        300
IPVGVTATDV VLTITEMLRD HGVVQKFVEF YGSGVKAVPL ANRATIGNMS 
       310        320        330        340        350
PEFGSTCAMF PIDEETTKYL RLTGRPEEQV ALVEAYAKAQ GMWLDEDTVE 
       360        370        380        390        400
AEYSEYLELD LSTVVPSIAG PKRPQDRILL SEAKEQFRKD LPTYTDDAVS 
       410        420        430        440        450
VDTSIPATRM VNEGGGQPEG GVEADNYNAS WAGSGESLAT GAEGRPSKPV 
       460        470        480        490        500
TVASPQGGEY TIDHGMVAIA SITSCTNTSN PSVMIGAGLI ARKAAEKGLK 
       510        520        530        540        550
SKPWVKTICA PGSQVVDGYY QRADLWKDLE AMGFYLSGFG CTTCIGNSGP 
       560        570        580        590        600
LPEEISAAIN EHDLTATAVL SGNRNFEGRI SPDVKMNYLA SPIMVIAYAI 
       610        620        630        640        650
AGTMDFDFEN EALGQDQDGN DVFLKDIWPS TEEIEDTIQQ AISRELYEAD 
       660        670        680        690        700
YADVFKGDKQ WQELDVPTGD TFEWDENSTY IRKAPYFDGM PVEPVAVTDI 
       710        720        730        740        750
QGARVLAKLG DSVTTDHISP ASSIKPGTPA AQYLDEHGVE RHDYNSLGSR 
       760        770        780        790        800
RGNHEVMMRG TFANIRLQNQ LVDIAGGYTR DFTQEGAPQA FIYDASVNYK 
       810        820        830        840        850
AAGIPLVVLG GKEYGTGSSR DWAAKGTNLL GIRAVITESF ERIHRSNLIG 
       860        870        880        890        900
MGVVPLQFPA GESHESLGLD GTETFDITGL TALNEGETPK TVKVTATKEN 
       910        920        930 
GDVVEFDAVV RIDTPGEADY YRHGGILQYV LRQMAASSK
Length:939
Mass (Da):101,726
Last modified:February 7, 2006 - v2
<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:i3488BCA190A07F13
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAB98933 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence CAF21548 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

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 conflicti71D → N in BAA76717 (Ref. 1) Curated1
Sequence conflicti122M → V in BAA76717 (Ref. 1) Curated1
Sequence conflicti555I → Y in BAA76717 (Ref. 1) Curated1
Sequence conflicti745N → Y in BAA76717 (Ref. 1) Curated1
Sequence conflicti888T → I in BAA76717 (Ref. 1) 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
AB025424 Genomic DNA Translation: BAA76717.1
BA000036 Genomic DNA Translation: BAB98933.1 Different initiation.
BX927152 Genomic DNA Translation: CAF21548.1 Different initiation.

NCBI Reference Sequences

More...RefSeqi		NP_600755.1, NC_003450.3

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		BAB98933; BAB98933; BAB98933
CAF21548; CAF21548; cg1737

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		cgb:cg1737
cgl:NCgl1482

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|196627.13.peg.1507

<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
AB025424 Genomic DNA Translation: BAA76717.1
BA000036 Genomic DNA Translation: BAB98933.1 Different initiation.
BX927152 Genomic DNA Translation: CAF21548.1 Different initiation.
RefSeqiNP_600755.1, NC_003450.3

3D structure databases

SMRiQ8NQ98
ModBaseiSearch...

Protein-protein interaction databases

STRINGi196627.cg1737

2D gel databases

World-2DPAGEi0001:Q8NQ98

Genome annotation databases

EnsemblBacteriaiBAB98933; BAB98933; BAB98933
CAF21548; CAF21548; cg1737
KEGGicgb:cg1737
cgl:NCgl1482
PATRICifig|196627.13.peg.1507

Phylogenomic databases

eggNOGiCOG1048, Bacteria
HOGENOMiCLU_013476_2_1_11
OMAiNGGIMQY

Enzyme and pathway databases

UniPathwayiUPA00223;UER00718
UPA00946
BioCyciCORYNE:G18NG-11125-MONOMER

Family and domain databases

CDDicd01580, AcnA_IRP_Swivel, 1 hit
Gene3Di3.20.19.10, 1 hit
InterProiView protein in InterPro
IPR044137, AcnA_IRP_Swivel
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
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_CORGL
<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: Q8NQ98
Secondary accession number(s): Q6M550, Q9WXJ0
<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: February 7, 2006
Last sequence update: February 7, 2006
Last modified: February 10, 2021
This is version 118 of the entry and version 2 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

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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