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Protein

Enolase

Gene

eno_3

Organism
Chlamydia trachomatis
Status
Unreviewed-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

Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.UniRule annotation

<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

Mg2+UniRule annotation

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein.UniRule annotation

<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: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk_5), Phosphoglycerate kinase (pgk_3), Phosphoglycerate kinase (pgk_4), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk_2), Phosphoglycerate kinase (pgk_2), Phosphoglycerate kinase (pgk_1), Phosphoglycerate kinase (pgk_2), Phosphoglycerate kinase (pgk_3), Phosphoglycerate kinase (pgk_2), Phosphoglycerate kinase (pgk_1), Phosphoglycerate kinase (pgk_2), Phosphoglycerate kinase (pgk_4), Phosphoglycerate kinase (pgk_6), Phosphoglycerate kinase (pgk_2), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk_3), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk_2), Phosphoglycerate kinase (pgk_1), Phosphoglycerate kinase (pgk_2)
  3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA_8), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), Phosphoglycerate mutase (2,3-diphosphoglycerate-independent) (gpmI_2), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA_9), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA_2), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA_2), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA_2), Phosphoglycerate mutase (2,3-diphosphoglycerate-independent) (gpmI_1), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA_6), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA_2), Phosphoglyceromutase (gpmA_12), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), Phosphoglycerate mutase (2,3-diphosphoglycerate-independent) (gpmI_1), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA_5), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA_2), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA_4), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA_2), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA_1), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA_4), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA_3), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA_1), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA_1)
  4. Enolase (eno_3), Enolase (eno_3), Enolase (eno_4), Enolase (eno_2), Enolase (eno_1), Enolase (eno_1), Enolase (eno_1), Enolase (eno), Enolase (eno_1), Enolase (eno_3), Enolase (eno_2), Enolase (eno_2)
  5. Pyruvate kinase (pykF), Pyruvate kinase (pykF), Pyruvate kinase (pykF), Pyruvate kinase (pykF), Pyruvate kinase (pykF), Pyruvate kinase (pykF_3), Pyruvate kinase (pykF_3), Pyruvate kinase (pykF_1), Pyruvate kinase (pykF_2), Pyruvate kinase (pykF_2), Pyruvate kinase (pykF_1), Pyruvate kinase (pykF_3), Pyruvate kinase (pykF_2), Pyruvate kinase (pykF_2), Pyruvate kinase (pykF_1), Pyruvate kinase (pykF_2), Pyruvate kinase (pykF_1), Pyruvate kinase (pykF_1)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei155SubstrateUniRule annotation1
Binding sitei164SubstrateUniRule annotation1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei205Proton donorUniRule annotation1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi243MagnesiumUniRule annotation1
Metal bindingi292MagnesiumUniRule annotation1
Binding sitei292SubstrateUniRule annotation1
Metal bindingi319MagnesiumUniRule annotation1
Binding sitei319SubstrateUniRule annotation1
Active sitei344Proton acceptorUniRule annotation1
Binding sitei344Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei395SubstrateUniRule 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

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 functionLyaseUniRule annotationImported
Biological processGlycolysisUniRule annotation
LigandMagnesiumUniRule annotation, Metal-bindingUniRule annotation, PyruvateImported

Enzyme and pathway databases

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

More...
UniPathwayi
UPA00109;UER00187

<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:
EnolaseUniRule annotation (EC:4.2.1.11UniRule annotation)
Alternative name(s):
2-phospho-D-glycerate hydro-lyaseUniRule annotation
2-phosphoglycerate dehydrataseUniRule annotation
<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:eno_3Imported
Synonyms:enoUniRule annotation
ORF Names:ERS133248_03182Imported
<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>OrganismiChlamydia trachomatisImported
<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 identifieri813 [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 lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000049116 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unassembled WGS sequence

<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

  • Cytoplasm UniRule annotation
  • Secreted UniRule annotation
  • Cell surface UniRule annotation
  • Note: Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the cell surface.UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

CytoplasmUniRule annotation, SecretedUniRule annotation

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini4 – 134Enolase_NInterPro annotationAdd BLAST131
Domaini139 – 432Enolase_CInterPro annotationAdd BLAST294

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>Regioni371 – 374Substrate bindingUniRule annotation4

<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 enolase family.UniRule annotation

Family and domain databases

Conserved Domains Database

More...
CDDi
cd03313 enolase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.120, 1 hit
3.30.390.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00318 Enolase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000941 Enolase
IPR036849 Enolase-like_C_sf
IPR029017 Enolase-like_N
IPR020810 Enolase_C
IPR020809 Enolase_CS
IPR020811 Enolase_N

The PANTHER Classification System

More...
PANTHERi
PTHR11902 PTHR11902, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00113 Enolase_C, 1 hit
PF03952 Enolase_N, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001400 Enolase, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00148 ENOLASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01192 Enolase_C, 1 hit
SM01193 Enolase_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51604 SSF51604, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01060 eno, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00164 ENOLASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

A0A0E9G889-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSIITDVYAR EVLDSRGNPT LEVEVYTESG AFGRGMVPSG ASTGEHEAVE
60 70 80 90 100
LRDGDKSRYL GLGTQKAVDN VNNVIADAII GYDVRDQQAI DRAMIALDDT
110 120 130 140 150
PNKGKLGANA ILGVSIAVAR AAADYLEVPL YNYLGGFNAK VLPTPMMNII
160 170 180 190 200
NGGSHSDAPI AFQEFMIVPV GAPTFKEGLR WGAEVFHNLK KILKARGLVT
210 220 230 240 250
AVGDEGGFAP KFEGTEDGVE TIIEAIEAAG YVAGENGIMI GFDCASSEFY
260 270 280 290 300
DKEKGLYDYT KFEGEGAAIR TSAEQIDYLE ELVNKYPIIT IEDGMDENDW
310 320 330 340 350
DGWKALTERL GGRVQLVGDD FFVTNTDYLV RGIKENAANS ILIKVNQIGT
360 370 380 390 400
LTETFEAIEM AKEAGYTAVV SHRSGETEDS TIADIAVATN AGQIKTGSLS
410 420 430
RTDRIAKYNQ LLRIEDQLGE VAAYKGLQSF YNLKK
Length:435
Mass (Da):47,094
Last modified:June 24, 2015 - 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:i39816313D930F03B
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
CVOC01000189 Genomic DNA Translation: CRH90608.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CRH90608; CRH90608; ERS133248_03182

<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
CVOC01000189 Genomic DNA Translation: CRH90608.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCRH90608; CRH90608; ERS133248_03182

Enzyme and pathway databases

UniPathwayi
UPA00109;UER00187

Family and domain databases

CDDicd03313 enolase, 1 hit
Gene3Di3.20.20.120, 1 hit
3.30.390.10, 1 hit
HAMAPiMF_00318 Enolase, 1 hit
InterProiView protein in InterPro
IPR000941 Enolase
IPR036849 Enolase-like_C_sf
IPR029017 Enolase-like_N
IPR020810 Enolase_C
IPR020809 Enolase_CS
IPR020811 Enolase_N
PANTHERiPTHR11902 PTHR11902, 1 hit
PfamiView protein in Pfam
PF00113 Enolase_C, 1 hit
PF03952 Enolase_N, 1 hit
PIRSFiPIRSF001400 Enolase, 1 hit
PRINTSiPR00148 ENOLASE
SMARTiView protein in SMART
SM01192 Enolase_C, 1 hit
SM01193 Enolase_N, 1 hit
SUPFAMiSSF51604 SSF51604, 1 hit
TIGRFAMsiTIGR01060 eno, 1 hit
PROSITEiView protein in PROSITE
PS00164 ENOLASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiA0A0E9G889_CHLTH
<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: A0A0E9G889
<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/TrEMBL: June 24, 2015
Last sequence update: June 24, 2015
Last modified: December 5, 2018
This is version 17 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 statusiUnreviewed (UniProtKB/TrEMBL)

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteomeImported
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Main funding by: National Institutes of Health

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