Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Due to a server migration, the UniProt 'ID mapping', 'Peptide search' and 'community bibliography submission' tools will not be available on the 19th April 2021 during the morning (EST).

UniProtKB - Q39FB9 (ISPF_BURL3)

Entry version 86 (10 Feb 2021)
Sequence version 1 (22 Nov 2005)
Previous versions | rss
Add a publicationFeedback
Protein

2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase

Gene

ispF

Organism
Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383)
Status
Reviewed-Annotation score:

Annotation score:3 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 biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).UniRule annotation

<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

a divalent metal cationUniRule annotationNote: Binds 1 divalent metal cation per subunit.UniRule annotation

<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: isopentenyl diphosphate biosynthesis via DXP pathway

This protein is involved in step 4 of the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate.UniRule annotation
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr), 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr), 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr), 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr), 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr), 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr), 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr), 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr), 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr), 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr), 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr), 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr), 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr), 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr)
  2. 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (ispD), 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (ispD), 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (ispD), 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (ispD), 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (ispD), 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (ispD), 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (ispD), 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (ispD)
  3. 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE), 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE), 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE), 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE), 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE), 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE), 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE), 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE), 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE), 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE), 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE), 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE), 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE), 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE)
  4. 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ispF), 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ispF), 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ispF), 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ispF), 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ispF), 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ispF), 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ispF), 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ispF), 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ispF), 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ispF), 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ispF)
  5. 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) (ispG), 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) (ispG), 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) (ispG), 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) (ispG), 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) (ispG), 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) (ispG)
  6. 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH), 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH), 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH), 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH), 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH), 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH)
This subpathway is part of the pathway isopentenyl diphosphate biosynthesis via DXP pathway, which is itself part of Isoprenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate, the pathway isopentenyl diphosphate biosynthesis via DXP pathway and in Isoprenoid biosynthesis.

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 bindingi10Divalent metal cationUniRule annotation1
Metal bindingi12Divalent metal cationUniRule annotation1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei36Transition state stabilizerUniRule annotation1
Metal bindingi44Divalent metal cationUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei67Substrate; via carbonyl oxygenUniRule annotation1
Sitei135Transition state stabilizerUniRule annotation1
Binding sitei144SubstrateUniRule annotation1

<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
Biological processIsoprene biosynthesis
LigandMetal-binding

Enzyme and pathway databases

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

More...UniPathwayi		UPA00056;UER00095

<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:
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthaseUniRule annotation (EC:4.6.1.12UniRule annotation)
Short name:
MECDP-synthaseUniRule annotation
Short name:
MECPP-synthaseUniRule annotation
Short name:
MECPSUniRule annotation
<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:ispFUniRule annotation
Ordered Locus Names:Bcep18194_A5253
<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>OrganismiBurkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383)
<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 identifieri482957 [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 › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex
<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
  • UP000002705 <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 1

<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_00002377111 – 1612-C-methyl-D-erythritol 2,4-cyclodiphosphate synthaseAdd BLAST161

<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

Homotrimer.

UniRule annotation

<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		Q39FB9

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni10 – 12Substrate bindingUniRule annotation3
Regioni36 – 37Substrate bindingUniRule annotation2
Regioni40 – 48Substrate bindingUniRule annotation9
Regioni58 – 60Substrate bindingUniRule annotation3
Regioni63 – 67Substrate bindingUniRule annotation5

<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 IspF family.UniRule annotation

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_084630_2_0_4

Identification of Orthologs from Complete Genome Data

More...OMAi		PEWSGAS

Database of Orthologous Groups

More...OrthoDBi		1716560at2

Family and domain databases

Conserved Domains Database

More...CDDi		cd00554, MECDP_synthase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.1330.50, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00107, IspF, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003526, MECDP_synthase
IPR020555, MECDP_synthase_CS
IPR036571, MECDP_synthase_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02542, YgbB, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF69765, SSF69765, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00151, ispF, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS01350, ISPF, 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.

Q39FB9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDFRIGQGYD VHQLVEGRPL IIGGVTIPYE RGLLGHSDAD VLLHAITDAL 
        60         70         80         90        100
FGAAALGDIG RHFSDTDAAF KGADSRVLLR ECVARINAAG FTIQNVDSTV 
       110        120        130        140        150
IAQAPKLAPH IDGMRANIAA DLGLPLDRVN VKAKTNEKLG YLGRGEGIEA 
       160 
QAAALLVKQG G
Length:161
Mass (Da):16,937
Last modified:November 22, 2005 - 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:i8A8F8D40B0811237
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
CP000151 Genomic DNA Translation: ABB08847.1

NCBI Reference Sequences

More...RefSeqi		WP_011352389.1, NZ_CADFCT010000008.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		ABB08847; ABB08847; Bcep18194_A5253

Database of genes from NCBI RefSeq genomes

More...GeneIDi		45095130

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		bur:Bcep18194_A5253

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|482957.22.peg.2199

<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
CP000151 Genomic DNA Translation: ABB08847.1
RefSeqiWP_011352389.1, NZ_CADFCT010000008.1

3D structure databases

SMRiQ39FB9
ModBaseiSearch...

Genome annotation databases

EnsemblBacteriaiABB08847; ABB08847; Bcep18194_A5253
GeneIDi45095130
KEGGibur:Bcep18194_A5253
PATRICifig|482957.22.peg.2199

Phylogenomic databases

HOGENOMiCLU_084630_2_0_4
OMAiPEWSGAS
OrthoDBi1716560at2

Enzyme and pathway databases

UniPathwayiUPA00056;UER00095

Family and domain databases

CDDicd00554, MECDP_synthase, 1 hit
Gene3Di3.30.1330.50, 1 hit
HAMAPiMF_00107, IspF, 1 hit
InterProiView protein in InterPro
IPR003526, MECDP_synthase
IPR020555, MECDP_synthase_CS
IPR036571, MECDP_synthase_sf
PfamiView protein in Pfam
PF02542, YgbB, 1 hit
SUPFAMiSSF69765, SSF69765, 1 hit
TIGRFAMsiTIGR00151, ispF, 1 hit
PROSITEiView protein in PROSITE
PS01350, ISPF, 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 nameiISPF_BURL3
<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: Q39FB9
<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: May 30, 2006
Last sequence update: November 22, 2005
Last modified: February 10, 2021
This is version 86 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. 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

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