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Protein

Enolase

Gene

eno

Organism
Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

2-phospho-D-glycerate = phosphoenolpyruvate + H2O.UniRule annotation

Cofactori

Mg2+UniRule annotation

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.UniRule annotation

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-independent phosphoglycerate mutase (gpmI)
  4. Enolase (eno)
  5. Pyruvate kinase (Caur_3128)
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
Binding sitei156SubstrateUniRule annotation1
Binding sitei165SubstrateUniRule annotation1
Active sitei206Proton donorUniRule annotation1
Metal bindingi243MagnesiumUniRule annotation1
Metal bindingi286MagnesiumUniRule annotation1
Binding sitei286SubstrateUniRule annotation1
Metal bindingi313MagnesiumUniRule annotation1
Binding sitei313SubstrateUniRule annotation1
Active sitei338Proton acceptorUniRule annotation1
Binding sitei338Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei389SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processGlycolysis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00109; 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:Caur_3808
OrganismiChloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
Taxonomic identifieri324602 [NCBI]
Taxonomic lineageiBacteriaChloroflexiChloroflexiaChloroflexalesChloroflexineaeChloroflexaceaeChloroflexus
Proteomesi
  • UP000002008 Componenti: Chromosome

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

Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000791261 – 426EnolaseAdd BLAST426

Proteomic databases

PRIDEiA9WCM4.

Interactioni

Protein-protein interaction databases

STRINGi324602.Caur_3808.

Structurei

Secondary structure

1426
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 14Combined sources11
Beta strandi20 – 28Combined sources9
Beta strandi33 – 37Combined sources5
Beta strandi46 – 48Combined sources3
Turni57 – 59Combined sources3
Helixi60 – 62Combined sources3
Helixi66 – 73Combined sources8
Helixi75 – 80Combined sources6
Helixi88 – 99Combined sources12
Turni105 – 107Combined sources3
Helixi109 – 127Combined sources19
Helixi131 – 136Combined sources6
Helixi137 – 139Combined sources3
Beta strandi145 – 152Combined sources8
Helixi154 – 156Combined sources3
Beta strandi158 – 160Combined sources3
Beta strandi165 – 169Combined sources5
Helixi176 – 195Combined sources20
Turni196 – 198Combined sources3
Beta strandi205 – 207Combined sources3
Beta strandi214 – 217Combined sources4
Helixi218 – 229Combined sources12
Turni235 – 237Combined sources3
Beta strandi238 – 243Combined sources6
Helixi246 – 249Combined sources4
Beta strandi251 – 254Combined sources4
Turni258 – 261Combined sources4
Helixi267 – 279Combined sources13
Beta strandi282 – 289Combined sources8
Helixi294 – 304Combined sources11
Turni305 – 307Combined sources3
Beta strandi308 – 313Combined sources6
Turni314 – 318Combined sources5
Helixi320 – 328Combined sources9
Beta strandi333 – 337Combined sources5
Helixi339 – 342Combined sources4
Helixi345 – 356Combined sources12
Turni357 – 359Combined sources3
Beta strandi361 – 365Combined sources5
Helixi375 – 382Combined sources8
Beta strandi387 – 390Combined sources4
Helixi400 – 412Combined sources13
Helixi413 – 415Combined sources3
Helixi420 – 423Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4YWSX-ray2.45A/B1-426[»]
4Z17X-ray2.65A/B1-426[»]
4Z1YX-ray2.53A/B1-426[»]
ProteinModelPortaliA9WCM4.
SMRiA9WCM4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni365 – 368Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C70. Bacteria.
COG0148. LUCA.
HOGENOMiHOG000072174.
InParanoidiA9WCM4.
KOiK01689.
OMAiEFMIIPV.
OrthoDBiPOG091H02DK.

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.
IPR034390. Enolase-like_superfamily.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiView protein in Pfam
PF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SFLDiSFLDG00178. enolase. 1 hit.
SFLDS00001. Enolase. 1 hit.
SMARTiView protein in SMART
SM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiView protein in PROSITE
PS00164. ENOLASE. 1 hit.

Sequencei

Sequence statusi: Complete.

A9WCM4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTLIEAIVA REVLDSRGNP TIEVDVRLES GDVGRAIVPS GASTGAHEAL
60 70 80 90 100
ELRDGDKSRY NGKGVLKAVQ AVNEDIAEAL IGFDAADQIA LDQELIALDG
110 120 130 140 150
TPNKSKLGAN AILGVSLAAA KAAAAAFGLP LYRYLGGVYA HVLPVPMMNI
160 170 180 190 200
MNGGQHATNS TDFQEFMIMP VGAESFREGL RWGAEIYHML KKVIHDRGFS
210 220 230 240 250
TTVGDEGGFA PSLPTNDAPL QLIMEAIEKA GYRPGEQIVI ALDPATTEIF
260 270 280 290 300
EDGKYHLKRE GRSLSSAEMV DYWVDLVNRY PIISLEDGLA EDDWEGWALL
310 320 330 340 350
RAKLGDRVQL VGDDFLVTNV QRLQRAIEAK AANSILIKLN QIGSLTETLS
360 370 380 390 400
AIQLAQRSGW TAVVSHRSGE SEDVTIADLV VATNAGQIKT GAPARTDRIA
410 420
KYNQLLRIEE ELGSAARYAG RSAFKV
Length:426
Mass (Da):45,897
Last modified:February 5, 2008 - v1
Checksum:i1EAF451AA599E19D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000909 Genomic DNA. Translation: ABY36986.1.
RefSeqiWP_012259639.1. NC_010175.1.
YP_001637375.1. NC_010175.1.

Genome annotation databases

EnsemblBacteriaiABY36986; ABY36986; Caur_3808.
GeneIDi5825617.
KEGGicau:Caur_3808.
PATRICi21419084. VBIChlAur28763_4274.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000909 Genomic DNA. Translation: ABY36986.1.
RefSeqiWP_012259639.1. NC_010175.1.
YP_001637375.1. NC_010175.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4YWSX-ray2.45A/B1-426[»]
4Z17X-ray2.65A/B1-426[»]
4Z1YX-ray2.53A/B1-426[»]
ProteinModelPortaliA9WCM4.
SMRiA9WCM4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi324602.Caur_3808.

Proteomic databases

PRIDEiA9WCM4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABY36986; ABY36986; Caur_3808.
GeneIDi5825617.
KEGGicau:Caur_3808.
PATRICi21419084. VBIChlAur28763_4274.

Phylogenomic databases

eggNOGiENOG4105C70. Bacteria.
COG0148. LUCA.
HOGENOMiHOG000072174.
InParanoidiA9WCM4.
KOiK01689.
OMAiEFMIIPV.
OrthoDBiPOG091H02DK.

Enzyme and pathway databases

UniPathwayiUPA00109; 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.
IPR034390. Enolase-like_superfamily.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiView protein in Pfam
PF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SFLDiSFLDG00178. enolase. 1 hit.
SFLDS00001. Enolase. 1 hit.
SMARTiView protein in SMART
SM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiView protein in PROSITE
PS00164. ENOLASE. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiENO_CHLAA
AccessioniPrimary (citable) accession number: A9WCM4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: April 12, 2017
This is version 64 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.