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UniProtKB - P09339 (ACNA_BACSU)

Entry version 152 (02 Dec 2020)
Sequence version 4 (23 Jan 2007)
Previous versions | rss
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Protein

Aconitate/2-methylaconitate hydratase

Gene

citB

Organism
Bacillus subtilis (strain 168)
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 both the tricarboxylic acid (TCA) and methylcitric acid cycles (PubMed:28956599). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate (PubMed:3110133, PubMed:23354745). Also catalyzes the rehydration of 2-methyl-cis-aconitate to produce 2-methylisocitrate (PubMed:28956599). The apo form of AcnA functions as a RNA-binding regulatory protein which plays a role in the regulation of citrate concentration and in the sporulation. To prevent the accumulation of excessive levels of citrate, it binds near the 5' end of the citZ mRNA, decreasing its stability and thereby limiting the concentration of citrate synthase in the cell. Aconitase also binds to the gerE transcript late in sporulation and stabilizes it for translation, thereby increasing the rate and level of GerE protein accumulation (PubMed:10468622, PubMed:16923907, PubMed:23354745, PubMed:9393699).6 Publications

Miscellaneous

Whether aconitase is active as an enzyme or an RNA-binding protein is determined by the status of an iron-sulfur (4Fe-4S) cluster that is essential for the catalytic activity of all aconitases. Citrate is both cotransported with iron and a chelator of divalent cations, including iron. If the intracellular citrate level becomes excessive, iron will be sequestered away from iron-containing proteins, including aconitase. Since excess citrate greatly stimulates aconitase synthesis via the positive regulatory effect of CcpC, the cell will gain the ability to metabolize citrate at a higher rate. If so much iron has been sequestered that aconitase loses enzymatic activity, the cell will acquire a high concentration of enzymatically inactive but RNA-binding-competent aconitase molecules. These aconitase proteins can bind to the citZ mRNA and reduce the rate of citrate accumulation by restricting the synthesis of citrate synthase protein.2 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 <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. Citrate synthase 2 (citZ), Citrate synthase 1 (citA), Citrate/2-methylcitrate synthase (mmgD)
  2. Aconitate hydratase (acnA), Aconitate/2-methylaconitate hydratase (citB)
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 <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 bindingi450Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi516Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi519Iron-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		BSUB:BSU18000-MONOMER

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%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/2-methylaconitate hydratase1 Publication (EC:4.2.1.-1 Publication, EC:4.2.1.31 Publication)
Alternative name(s):
Aconitate hydratase A1 Publication
Short name:
ACN1 Publication
Short name:
Aconitase1 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%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:citB
Ordered Locus Names:BSU18000
<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>OrganismiBacillus subtilis (strain 168)
<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 identifieri224308 [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 › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›
<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
  • UP000001570 <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 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

Complete GO annotation on QuickGO ...

<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 show a dramatic increase in the concentration of citrate. This accumulation of citrate prevents sporulation due to chelation by citrate of divalent cations required for proper functioning of the Spo0A-initiated phosphorelay.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi450C → S: Loss of aconitase activity. It is glutamate auxotroph and accumulates citrate. Exhibits overexpression of the citB promoter and accumulates high levels of inactive aconitase. 1 Publication1
Mutagenesisi741R → E: Same aconitase activity compared to the wild-type. It is glutamate prototroph and accumulates citrate. Exhibits overexpression of the citB promoter and accumulates high levels of active aconitase. 1 Publication1

<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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000766552 – 909Aconitate/2-methylaconitate hydrataseAdd BLAST908

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P09339

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

More...PaxDbi		P09339

PRoteomics IDEntifications database

More...PRIDEi		P09339

<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

By citrate via CcpC. When citrate is absent, CcpC binds to the sites near the citB promoter and blocks expression. When citrate is present, it causes a change in the interaction of CcpC with its binding sites, resulting in derepression of citB. When citrate is very abundant, CcpC activates citB expression, presumably reflecting a change in the interaction of CcpC with RNA polymerase. Also induced by decoyinine and nutrient depletion.1 Publication

<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

Protein interaction database and analysis system

More...IntActi		P09339, 1 interactor

Molecular INTeraction database

More...MINTi		P09339

STRING: functional protein association networks

More...STRINGi		224308.BSU18000

<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		P09339

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 general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Mutagenesis of different positions (F662L, R741F, Q745E, I810T and V853A) on the C-terminal region of citB gene product shows that even B.subtilis mutant has high aconitase catalytic activity, it is defective in sporulation. The defect is at a late stage of sporulation, specifically affecting expression of sigma-K-dependent genes, many of which are important for spore coat assembly and require transcriptional activation by GerE. It strongly suggests that aconitase RNA binding activity may stabilize gerE mRNA in order to allow efficient GerE synthesis and proper timing of spore coat assembly.1 Publication

<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

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P09339

Identification of Orthologs from Complete Genome Data

More...OMAi		NGGIMQY

Database for complete collections of gene phylogenies

More...PhylomeDBi		P09339

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%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.

<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 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.

P09339-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MANEQKTAAK DVFQARKTFT TNGKTYHYYS LKALEDSGIG KVSKLPYSIK 
        60         70         80         90        100
VLLESVLRQV DGFVIKKEHV ENLAKWGTAE LKDIDVPFKP SRVILQDFTG 
       110        120        130        140        150
VPAVVDLASL RKAMAAVGGD PDKINPEIPV DLVIDHSVQV DKAGTEDALA 
       160        170        180        190        200
VNMDLEFERN AERYKFLSWA KKAFNNYQAV PPATGIVHQV NLEFLASVVH 
       210        220        230        240        250
AIEEDGELVT YPDTLVGTDS HTTMINGIGV LGWGVGGIEA EAGMLGQPSY 
       260        270        280        290        300
FPVPEVIGAK LVGKLPNGTT ATDLALKVTQ VLREKGVVGK FVEFFGPGIA 
       310        320        330        340        350
ELPLADRATI ANMAPEYGAT CGFFPVDEEA LNYLRLTGRD PEHIDVVEAY 
       360        370        380        390        400
CRSNGLFYTP DAEDPQFTDV VEIDLSQIEA NLSGPKRPQD LIPLSAMQET 
       410        420        430        440        450
FKKQLVSPAG NQGFGLNAEE ENKEIKFKLL NGEETVMKTG AIAIAAITSC 
       460        470        480        490        500
TNTSNPYVLI GAGLVAKKAV ELGLKVPNYV KTSLAPGSKV VTGYLVNSGL 
       510        520        530        540        550
LPYMKELGFN LVGYGCTTCI GNSGPLSPEI EEAVAKNDLL ITSVLSGNRN 
       560        570        580        590        600
FEGRIHPLVK GNYLASPPLV VAYALAGTVN INLKTDPIGV GKDGQNVYFN 
       610        620        630        640        650
DIWPSMDEIN ALVKQTVTPE LFRKEYETVF DDNKRWNEIE TTDEALYKWD 
       660        670        680        690        700
NDSTYIQNPP FFEEMSVEPG KVEPLKGLRV VGKFGDSVTT DHISPAGAIG 
       710        720        730        740        750
KDTPAGKYLQ EKGVSPRDFN SYGSRRGNHE VMMRGTFANI RIKNQIAPGT 
       760        770        780        790        800
EGGFTTYWPT GEVTSIYDAC MKYKEDKTGL VVLAGKDYGM GSSRDWAAKG 
       810        820        830        840        850
TNLLGIRTVI AESFERIHRS NLVFMGVLPL QFKQGENADT LGLTGKEVIE 
       860        870        880        890        900
VDVDETVRPR DLVTVRAINE DGNVTTFEAV VRFDSEVEID YYRHGGILQM 

VLREKMKQS
Length:909
Mass (Da):99,334
Last modified:January 23, 2007 - v4
<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:i9545E734F2BCF735
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 conflicti43 – 45SKL → FEA in AAA22316 (PubMed:3110133).Curated3
Sequence conflicti119G → V no nucleotide entry (Ref. 3) 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
Z73234 Genomic DNA Translation: CAA97599.1
AL009126 Genomic DNA Translation: CAB13684.1
M16776 Genomic DNA Translation: AAA22316.1

Protein sequence database of the Protein Information Resource

More...PIRi		G69599

NCBI Reference Sequences

More...RefSeqi		NP_389683.1, NC_000964.3
WP_003245728.1, NZ_JNCM01000035.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		CAB13684; CAB13684; BSU18000

Database of genes from NCBI RefSeq genomes

More...GeneIDi		938140

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		bsu:BSU18000

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|224308.179.peg.1961

<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
Z73234 Genomic DNA Translation: CAA97599.1
AL009126 Genomic DNA Translation: CAB13684.1
M16776 Genomic DNA Translation: AAA22316.1
PIRiG69599
RefSeqiNP_389683.1, NC_000964.3
WP_003245728.1, NZ_JNCM01000035.1

3D structure databases

SMRiP09339
ModBaseiSearch...

Protein-protein interaction databases

IntActiP09339, 1 interactor
MINTiP09339
STRINGi224308.BSU18000

Proteomic databases

jPOSTiP09339
PaxDbiP09339
PRIDEiP09339

Genome annotation databases

EnsemblBacteriaiCAB13684; CAB13684; BSU18000
GeneIDi938140
KEGGibsu:BSU18000
PATRICifig|224308.179.peg.1961

Phylogenomic databases

eggNOGiCOG1048, Bacteria
InParanoidiP09339
OMAiNGGIMQY
PhylomeDBiP09339

Enzyme and pathway databases

UniPathwayiUPA00223;UER00718
BioCyciBSUB:BSU18000-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_BACSU
<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: P09339
Secondary accession number(s): Q45059
<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: July 1, 1989
Last sequence update: January 23, 2007
Last modified: December 2, 2020
This is version 152 of the entry and version 4 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

Direct protein sequencing, Reference proteome

Documents

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