eno

Functionⁱ

Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.UniRule annotation1 Publication

Catalytic activityⁱ

2-phospho-D-glycerate = phosphoenolpyruvate + H₂O.UniRule annotation1 Publication

Cofactorⁱ

Mg²⁺UniRule annotation1 Publication

Enzyme regulationⁱ

The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein (By similarity). Inhibited by fluoride and phosphate.UniRule annotation1 Publication

Kineticsⁱ

pH dependenceⁱ

Optimum pH is 7.5.1 Publication

Temperature dependenceⁱ

Optimum temperature is 90 degrees Celsius.1 Publication

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:

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 key	Position(s)	DescriptionActions	Length
Binding siteⁱ	156	SubstrateUniRule annotation	1
Binding siteⁱ	165	SubstrateUniRule annotation	1
Active siteⁱ	206	Proton donorUniRule annotation	1
Metal bindingⁱ	243	MagnesiumUniRule annotation	1
Metal bindingⁱ	286	MagnesiumUniRule annotation	1
Binding siteⁱ	286	SubstrateUniRule annotation	1
Metal bindingⁱ	313	MagnesiumUniRule annotation	1
Binding siteⁱ	313	SubstrateUniRule annotation	1
Active siteⁱ	338	Proton acceptorUniRule annotation	1
Binding siteⁱ	338	Substrate (covalent); in inhibited formUniRule annotation	1
Binding siteⁱ	389	SubstrateUniRule annotation	1

GO - Molecular functionⁱ

magnesium ion binding Source: InterPro
phosphopyruvate hydratase activity Source: UniProtKB-EC

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

glycolytic process Source: UniProtKB-UniPathway

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Lyase
Biological process	Glycolysis
Ligand	Magnesium, Metal-binding

Enzyme and pathway databases

UniPathwayⁱ	UPA00109; UER00187

UniPathwayⁱ

UPA00109; UER00187

Names & Taxonomyⁱ

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
Gene namesⁱ	Name:enoUniRule annotation Ordered Locus Names:TM_0877
Organismⁱ	Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifierⁱ	243274 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Thermotogae › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga › Thermotoga maritima
Proteomesⁱ	UP000008183 Componentⁱ: Chromosome

Subcellular locationⁱ

Cytoplasm
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00318
Secreted
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00318
Cell surface
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00318

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

cell surface Source: UniProtKB-SubCell
extracellular region Source: UniProtKB-SubCell
phosphopyruvate hydratase complex Source: InterPro

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cytoplasm, Secreted

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000133994	1 – 429	EnolaseAdd BLAST		429

Proteomic databases

PRIDEⁱ	P42848

PRIDEⁱ

P42848

Interactionⁱ

Subunit structureⁱ

Homooctamer. Forms a ring-shaped particle.1 Publication

Protein-protein interaction databases

STRINGⁱ	243274.TM0877

STRINGⁱ

243274.TM0877

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P42848
SMRⁱ	P42848
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	365 – 368	Substrate bindingUniRule annotation		4

Sequence similaritiesⁱ

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGⁱ	ENOG4105C70 Bacteria COG0148 LUCA
InParanoidⁱ	P42848
KEGG Orthology (KO) More...KOⁱ	K01689
OMAⁱ	EFMIIPV

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd03313 enolase, 1 hit
Gene3Dⁱ	3.20.20.1201 hit 3.30.390.101 hit
HAMAPⁱ	MF_00318 Enolase, 1 hit
InterProⁱ	View protein in InterPro IPR000941 Enolase IPR036849 Enolase-like_C_sf IPR029017 Enolase-like_N IPR034390 Enolase-like_superfamily IPR020810 Enolase_C IPR020809 Enolase_CS IPR020811 Enolase_N
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
PIRSFⁱ	PIRSF001400 Enolase, 1 hit
PRINTSⁱ	PR00148 ENOLASE
SFLDⁱ	SFLDG00178 enolase, 1 hit SFLDS00001 Enolase, 1 hit
SMARTⁱ	View protein in SMART SM01192 Enolase_C, 1 hit SM01193 Enolase_N, 1 hit
SUPFAMⁱ	SSF51604 SSF51604, 1 hit
TIGRFAMsⁱ	TIGR01060 eno, 1 hit
PROSITEⁱ	View protein in PROSITE PS00164 ENOLASE, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P42848-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MYVEIVDVRA REVLDSRGNP TVEAEVVLED GTMGRAIVPS GASTGKFEAL 
        60         70         80         90        100
EIRDKDKKRY LGKGVLKAVE NVNETIAPAL IGMNAFDQPL VDKTLIELDG 
       110        120        130        140        150
TENKSKLGAN AILAVSMAVA RAAANYLGLP LYKYLGGVNA KVLPVPLMNV 
       160        170        180        190        200
INGGQHADNN LDLQEFMIVP AGFDSFREAL RAGAEIFHTL KKILHEAGHV 
       210        220        230        240        250
TAVGDEGGFA PNLSSNEEAI KVLIEAIEKA GYKPGEEVFI ALDCAASSFY 
       260        270        280        290        300
DEEKGVYYVD GEEKSSEVLM GYYEELVAKY PIISIEDPFA EEDWDAFVEF 
       310        320        330        340        350
TKRVGNKVQI VGDDLYVTNV KRLSKGIELK ATNSILIKLN QIGTVTETLD 
       360        370        380        390        400
AVEMAQKNNM TAIISHRSGE SEDTFIADLA VATNAGFIKT GSLSRSERIA 
       410        420 
KYNQLLRIEE ELGKVAEFRG LKSFYSIKR

Length:429

Mass (Da):46,870

Last modified:May 30, 2000 - v2

Checksum:ⁱ35D65899D3AE56CB

GO

Sequence cautionⁱ

The sequence AAD35958 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AE000512 Genomic DNA Translation: AAD35958.1 Different initiation.
PIRⁱ	G72323
NCBI Reference Sequences More...RefSeqⁱ	NP_228685.1, NC_000853.1

Genome annotation databases

EnsemblBacteriaⁱ	AAD35958; AAD35958; TM_0877
GeneIDⁱ	898551
KEGGⁱ	tma:TM0877 tmi:THEMA_00250 tmw:THMA_0899
PATRICⁱ	fig\|243274.18.peg.50

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
P42848	A5IIQ6 A0A101FAR2 A0A124FG49 D2C5C2	Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995) Thermotoga sp. 47_83 Thermotoga naphthophila Thermotoga naphthophila (strain ATCC BAA-489 / DSM 13996 / JCM 10882 / RKU-10)	429	UniRef100_P42848	Cluster: Enolase	5

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
P42848	B9KA91 A5IIQ6 A0A101FAR2 A0A124FG49 D2C5C2 B1LCF4 A0A2N5RJ96 A0A0B5KU21 A0A2N5RGG9 A0A0A6MW32 +3	Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NS-E) Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995) Thermotoga sp. 47_83 Thermotoga naphthophila Thermotoga naphthophila (strain ATCC BAA-489 / DSM 13996 / JCM 10882 / RKU-10) Thermotoga sp. (strain RQ2) Thermotoga sp. KOL6 Thermotoga sp. RQ7 Thermotoga sp. SG1 Thermotoga sp. Mc24 And more	432	UniRef90_B9KA91	Cluster: Enolase	14

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
P42848	Q8KG25 B3QQT2 A0A1D8D3H5 A0A172TW73 UPI000A36A1C7 R5YJB4 R5YTN6 A0A0D6ASF5 UPI00034D1E55 A0A0D6AAL3 +3653	Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum) Chlorobaculum parvum (strain NCIB 8327) (Chlorobium vibrioforme subsp. thiosulfatophilum (strain DSM 263 / NCIB 8327)) Chlorobaculum limnaeum Flavisolibacter tropicus Streptomyces murinus Clostridium sp. CAG:571 Clostridium sp. CAG:492 Geminocystis sp. NIES-3709 Geminocystis herdmanii Geminocystis sp. NIES-3708 And more	437	UniRef50_Q8KG25	Cluster: Enolase 2	3,664

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AE000512 Genomic DNA Translation: AAD35958.1 Different initiation.
PIRⁱ	G72323
NCBI Reference Sequences More...RefSeqⁱ	NP_228685.1, NC_000853.1

3D structure databases

ProteinModelPortalⁱ	P42848
SMRⁱ	P42848
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	243274.TM0877

STRINGⁱ

243274.TM0877

Proteomic databases

PRIDEⁱ	P42848

PRIDEⁱ

P42848

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAD35958; AAD35958; TM_0877
GeneIDⁱ	898551
KEGGⁱ	tma:TM0877 tmi:THEMA_00250 tmw:THMA_0899
PATRICⁱ	fig\|243274.18.peg.50

Phylogenomic databases

eggNOGⁱ	ENOG4105C70 Bacteria COG0148 LUCA
InParanoidⁱ	P42848
KEGG Orthology (KO) More...KOⁱ	K01689
OMAⁱ	EFMIIPV

Enzyme and pathway databases

UniPathwayⁱ	UPA00109; UER00187

UniPathwayⁱ

UPA00109; UER00187

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd03313 enolase, 1 hit
Gene3Dⁱ	3.20.20.1201 hit 3.30.390.101 hit
HAMAPⁱ	MF_00318 Enolase, 1 hit
InterProⁱ	View protein in InterPro IPR000941 Enolase IPR036849 Enolase-like_C_sf IPR029017 Enolase-like_N IPR034390 Enolase-like_superfamily IPR020810 Enolase_C IPR020809 Enolase_CS IPR020811 Enolase_N
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
PIRSFⁱ	PIRSF001400 Enolase, 1 hit
PRINTSⁱ	PR00148 ENOLASE
SFLDⁱ	SFLDG00178 enolase, 1 hit SFLDS00001 Enolase, 1 hit
SMARTⁱ	View protein in SMART SM01192 Enolase_C, 1 hit SM01193 Enolase_N, 1 hit
SUPFAMⁱ	SSF51604 SSF51604, 1 hit
TIGRFAMsⁱ	TIGR01060 eno, 1 hit
PROSITEⁱ	View protein in PROSITE PS00164 ENOLASE, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ENO_THEMA
Accessionⁱ	P42848Primary (citable) accession number: P42848
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
	Last sequence update:	May 30, 2000
	Last modified:	February 28, 2018
	This is version 138 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Direct protein sequencing, Reference proteome

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P42848 (ENO_THEMA)

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Enolase

Select a section on the left to see content.

<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

<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi

<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

<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>pH dependencei

<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

Sites

<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

<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 - Biological processi

Enzyme and pathway databases

<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 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

<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 - Cellular componenti

<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

Proteomic databases

<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

Protein-protein interaction databases

<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

<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

<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

Phylogenomic databases

Family and domain databases

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

Sequence databases

Genome annotation databases

<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

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

<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 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

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Functionⁱ

Enzyme regulationⁱ

Kineticsⁱ

pH dependenceⁱ

Pathwayⁱ: glycolysis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ