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Entry version 130 (08 May 2019)
Sequence version 1 (01 Oct 2001)
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Protein

Enolase

Gene

eno

Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
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

Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. Binds plasminogen when expressed at the bacterial cell surface, potentially allowing the bacterium to acquire surface-associated proteolytic activity, which in turn contributes to the degradation of the extracellular matrix and transmigration of the bacteria.UniRule annotation3 Publications

<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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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 ‘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

Catalytically active also when expressed on the bacterial cell surface.
  1. KM=4.5 mM for 2-phospho-D-glycerate1 Publication
  1. Vmax=2.792 µmol/min/mg enzyme1 Publication

<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)
  3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
  4. Enolase (eno)
  5. Pyruvate kinase (pyk)
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 <a href="http://www.uniprot.org/help/function_section">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 sitei155SubstrateUniRule annotation1
Binding sitei164SubstrateUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi242MagnesiumUniRule annotation1
Metal bindingi291MagnesiumUniRule annotation1
Binding sitei291SubstrateUniRule annotation1
Metal bindingi318MagnesiumUniRule annotation1
Binding sitei318SubstrateUniRule annotation1
Active sitei343Proton acceptorUniRule annotation1
Binding sitei343Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei394SubstrateUniRule 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 functionLyase
Biological processGlycolysis, Virulence
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
SPNE170187:G1FZB-1152-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q97QS2

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

More...
UniPathwayi
UPA00109;UER00187

Protein family/group databases

MoonProt database of moonlighting proteins

More...
MoonProti
Q97QS2

<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:enoUniRule annotation
Ordered Locus Names:SP_1128
<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>OrganismiStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
<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 identifieri170187 [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 lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
<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
  • UP000000585 <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: 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

  • Cytoplasm
  • Secreted
  • Cell surface
  • 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, probably in complex with plasminogen.

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Secreted

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi251K → L: Great decrease in ability to bind plasminogen. Decrease in virulence; when associated with G-252 and L-254. 1 Publication1
Mutagenesisi252E → G: Great decrease in ability to bind plasminogen. Decrease in virulence; when associated with L-251 and L-254. 1 Publication1
Mutagenesisi254K → L: Great decrease in ability to bind plasminogen. Decrease in virulence; when associated with L-251 and G-252. 1 Publication1
Mutagenesisi433K → L: Decrease in ability to bind plasminogen under denaturing conditions. No effect on ability to bind plasminogen under non-denaturing conditions. Loss of ability to form homooctamers. Decrease in virulence; when associated with L-434. 2 Publications1
Mutagenesisi434K → L: Decrease in ability to bind plasminogen under denaturing conditions. No effect on ability to bind plasminogen under non-denaturing conditions. 2 Publications1
Mutagenesisi434K → L: Decrease in ability to bind plasminogen under denaturing conditions. No effect on ability to bind plasminogen under non-denaturing conditions. Loss of ability to form homooctamers. Decrease in virulence; when associated with L-433. 2 Publications1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001339801 – 434EnolaseAdd BLAST434

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homooctamer.

Forms a ring-shaped structure.

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
Q97QS2, 14 interactors

STRING: functional protein association networks

More...
STRINGi
170187.SP_1128

<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

Secondary structure

1434
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q97QS2

Database of comparative protein structure models

More...
ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q97QS2

<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>Regioni55 – 63Antigenic epitope9
Regioni370 – 373Substrate bindingUniRule annotation4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi248 – 256Plasminogen-binding9

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C70 Bacteria
COG0148 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000072174

KEGG Orthology (KO)

More...
KOi
K01689

Identification of Orthologs from Complete Genome Data

More...
OMAi
EFMIIPV

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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

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

Q97QS2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSIITDVYAR EVLDSRGNPT LEVEVYTESG AFGRGMVPSG ASTGEHEAVE
60 70 80 90 100
LRDGDKSRYG GLGTQKAVDN VNNIIAEAII GYDVRDQQAI DRAMIALDGT
110 120 130 140 150
PNKGKLGANA ILGVSIAVAR AAADYLEIPL YSYLGGFNTK VLPTPMMNII
160 170 180 190 200
NGGSHSDAPI AFQEFMILPV GAPTFKEALR YGAEIFHALK KILKSRGLET
210 220 230 240 250
AVGDEGGFAP RFEGTEDGVE TILAAIEAAG YVPGKDVFIG FDCASSEFYD
260 270 280 290 300
KERKVYDYTK FEGEGAAVRT SAEQIDYLEE LVNKYPIITI EDGMDENDWD
310 320 330 340 350
GWKALTERLG KKVQLVGDDF FVTNTDYLAR GIQEGAANSI LIKVNQIGTL
360 370 380 390 400
TETFEAIEMA KEAGYTAVVS HRSGETEDST IADIAVATNA GQIKTGSLSR
410 420 430
TDRIAKYNQL LRIEDQLGEV AEYRGLKSFY NLKK
Length:434
Mass (Da):47,103
Last modified:October 1, 2001 - 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:i0D64F8F04BBB99C4
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 conflicti2Missing AA sequence (PubMed:11442827).Curated1
Sequence conflicti20T → P AA sequence (PubMed:11442827).Curated1
Sequence conflicti24E → G AA sequence (PubMed:12435062).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
AE005672 Genomic DNA Translation: AAK75238.1

Protein sequence database of the Protein Information Resource

More...
PIRi
E95130

NCBI Reference Sequences

More...
RefSeqi
WP_000022813.1, NZ_AKVY01000001.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAK75238; AAK75238; SP_1128

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
31536454

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
spn:SP_1128

<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
AE005672 Genomic DNA Translation: AAK75238.1
PIRiE95130
RefSeqiWP_000022813.1, NZ_AKVY01000001.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W6TX-ray2.10A/B1-434[»]
SMRiQ97QS2
ModBaseiSearch...

Protein-protein interaction databases

IntActiQ97QS2, 14 interactors
STRINGi170187.SP_1128

Protein family/group databases

MoonProtiQ97QS2

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK75238; AAK75238; SP_1128
GeneIDi31536454
KEGGispn:SP_1128

Phylogenomic databases

eggNOGiENOG4105C70 Bacteria
COG0148 LUCA
HOGENOMiHOG000072174
KOiK01689
OMAiEFMIIPV

Enzyme and pathway databases

UniPathwayiUPA00109;UER00187
BioCyciSPNE170187:G1FZB-1152-MONOMER
SABIO-RKiQ97QS2

Miscellaneous databases

EvolutionaryTraceiQ97QS2

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...

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 nameiENO_STRPN
<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: Q97QS2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: October 1, 2001
Last modified: May 8, 2019
This is version 130 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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