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Protein

Enolase 2

Gene

eno2

Organism
Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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-dependent phosphoglycerate mutase (gpmA)
  4. Enolase 1 (eno1), Enolase 2 (eno2)
  5. no protein annotated in this organism
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 sitei154SubstrateUniRule annotation1
Binding sitei163SubstrateUniRule annotation1
Active sitei204Proton donorUniRule annotation1
Metal bindingi251MagnesiumUniRule annotation1
Metal bindingi297MagnesiumUniRule annotation1
Binding sitei297SubstrateUniRule annotation1
Metal bindingi324MagnesiumUniRule annotation1
Binding sitei324SubstrateUniRule annotation1
Active sitei349Proton acceptorUniRule annotation1
Binding sitei349Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei400SubstrateUniRule 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:
Enolase 2UniRule annotation (EC:4.2.1.11UniRule annotation)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase 2UniRule annotation
2-phosphoglycerate dehydratase 2UniRule annotation
Gene namesi
Name:eno2UniRule annotation
Synonyms:eno-2
Ordered Locus Names:CT0145
OrganismiChlorobium tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
Taxonomic identifieri194439 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum
Proteomesi
  • UP000001007 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_00001338691 – 437Enolase 2Add BLAST437

Proteomic databases

PRIDEiQ8KG25.

Interactioni

Protein-protein interaction databases

STRINGi194439.CT0145.

Structurei

3D structure databases

ProteinModelPortaliQ8KG25.
SMRiQ8KG25.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni376 – 379Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C70. Bacteria.
COG0148. LUCA.
HOGENOMiHOG000072173.
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.
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.
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.

Q8KG25-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVITRIHAR QIMDSRGNPT VEVDVHTESS FGRAAVPSGA STGVHEAVEL
60 70 80 90 100
RDKDKSVFLG KGVLKAVENV NTLINDALLG MDVTEQEAID AKLIELDGTP
110 120 130 140 150
NKSKLGANAI LGVSLACAKA GAEYSALPLY RYIGGTTAKT LPVPMMNVLN
160 170 180 190 200
GGAHADNTVD FQEFMIMPIG FERYSDALRC GAEVFHSLKS LLHDRGLSTA
210 220 230 240 250
VGDEGGFAPN VESNEQAIEL VIEAIGMAGY KAGAPTDRGG LGDGHVMIAL
260 270 280 290 300
DPASSEFYDA EKKKYVFKKS SGRELSSEEM ASYWADWASR YPIISIEDGM
310 320 330 340 350
AEDDWEGWKM LTDKIGGRVQ LVGDDLFVTN SKRLAEGIEK GVGNSILIKV
360 370 380 390 400
NQIGTLTETL QAIELAKRNG YTSVISHRSG ETEDTTIAQI AVATNAGQIK
410 420 430
TGSMSRSDRM AKYNELLRIE EELGSTALYP GIGAFRV
Length:437
Mass (Da):46,946
Last modified:October 1, 2002 - v1
Checksum:i7D9969C282B1CD8E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006470 Genomic DNA. Translation: AAM71393.1.
RefSeqiNP_661051.1. NC_002932.3.
WP_010931839.1. NC_002932.3.

Genome annotation databases

EnsemblBacteriaiAAM71393; AAM71393; CT0145.
GeneIDi1007040.
KEGGicte:CT0145.
PATRICi21398399. VBIChlTep116050_0142.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006470 Genomic DNA. Translation: AAM71393.1.
RefSeqiNP_661051.1. NC_002932.3.
WP_010931839.1. NC_002932.3.

3D structure databases

ProteinModelPortaliQ8KG25.
SMRiQ8KG25.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi194439.CT0145.

Proteomic databases

PRIDEiQ8KG25.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM71393; AAM71393; CT0145.
GeneIDi1007040.
KEGGicte:CT0145.
PATRICi21398399. VBIChlTep116050_0142.

Phylogenomic databases

eggNOGiENOG4105C70. Bacteria.
COG0148. LUCA.
HOGENOMiHOG000072173.
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.
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.
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 nameiENO2_CHLTE
AccessioniPrimary (citable) accession number: Q8KG25
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: October 1, 2002
Last modified: March 15, 2017
This is version 98 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.