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Protein

Enolase

Gene

eno

Organism
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
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 (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
Binding sitei154SubstrateUniRule annotation1
Binding sitei163SubstrateUniRule annotation1
Active sitei204Proton donorUniRule annotation1
Metal bindingi239MagnesiumUniRule annotation1
Metal bindingi280MagnesiumUniRule annotation1
Binding sitei280SubstrateUniRule annotation1
Metal bindingi307MagnesiumUniRule annotation1
Binding sitei307SubstrateUniRule annotation1
Active sitei332Proton acceptorUniRule annotation1
Binding sitei332Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei383SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processGlycolysis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyciCJEJ192222:GJTS-1580-MONOMER.
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:Cj1672c
OrganismiCampylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Taxonomic identifieri192222 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
Proteomesi
  • UP000000799 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_00001338611 – 414EnolaseAdd BLAST414

Proteomic databases

PaxDbiP42448.

Interactioni

Protein-protein interaction databases

IntActiP42448. 31 interactors.
STRINGi192222.Cj1672c.

Structurei

Secondary structure

1414
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 13Combined sources12
Beta strandi19 – 27Combined sources9
Beta strandi32 – 36Combined sources5
Beta strandi41 – 43Combined sources3
Beta strandi45 – 47Combined sources3
Helixi57 – 60Combined sources4
Helixi64 – 71Combined sources8
Helixi73 – 78Combined sources6
Helixi86 – 97Combined sources12
Beta strandi99 – 101Combined sources3
Turni103 – 105Combined sources3
Helixi107 – 124Combined sources18
Helixi129 – 134Combined sources6
Helixi135 – 137Combined sources3
Beta strandi146 – 150Combined sources5
Helixi152 – 154Combined sources3
Beta strandi155 – 158Combined sources4
Beta strandi162 – 168Combined sources7
Helixi174 – 194Combined sources21
Beta strandi212 – 215Combined sources4
Helixi216 – 227Combined sources12
Turni231 – 233Combined sources3
Beta strandi234 – 239Combined sources6
Helixi242 – 245Combined sources4
Beta strandi250 – 253Combined sources4
Beta strandi256 – 258Combined sources3
Helixi260 – 273Combined sources14
Beta strandi276 – 283Combined sources8
Helixi288 – 298Combined sources11
Turni299 – 301Combined sources3
Beta strandi302 – 307Combined sources6
Turni308 – 312Combined sources5
Helixi314 – 323Combined sources10
Beta strandi327 – 331Combined sources5
Helixi333 – 336Combined sources4
Helixi339 – 351Combined sources13
Beta strandi355 – 359Combined sources5
Helixi369 – 376Combined sources8
Beta strandi380 – 383Combined sources4
Helixi390 – 402Combined sources13
Turni403 – 405Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QN3X-ray2.13A/B/C/D1-414[»]
ProteinModelPortaliP42448.
SMRiP42448.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni359 – 362Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

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

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.

P42448-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLVIEDVRAY EVLDSRGNPT VKAEVTLSDG SVGAAIVPSG ASTGSKEALE
60 70 80 90 100
LRDNDERFGG KGVLKAVANV NETIADEILG LDAFNQTQLD DTLRELDGTN
110 120 130 140 150
NYSNLGANAT LGVSMATARA AAAALGMPLY RYLGGANASI LPVPMCNIIN
160 170 180 190 200
GGAHANNNVD FQEFMIMPFG FTSFKEALRS VCEIYAILKK ELANSGHSTA
210 220 230 240 250
LGDEGGFAPN LANNTEPIDL LMTCIKKAGY ENRVKIALDV ASTEFFKDGK
260 270 280 290 300
YHMEGKAFSS EALIERYVEL CAKYPICSIE DGLAENDFEG WIKLTEKLGN
310 320 330 340 350
KIQLVGDDLF VTNEDILREG IIKKMANAVL IKPNQIGTIT QTMRTVRLAQ
360 370 380 390 400
RNNYKCVMSH RSGESEDAFI ADFAVALNTG QIKTGALARG ERTAKYNRLL
410
EIEFESDEYL GEKL
Length:414
Mass (Da):44,939
Last modified:December 1, 2000 - v2
Checksum:i25C132C6B631FF3D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL111168 Genomic DNA. Translation: CAL35768.1.
PIRiE81264.
RefSeqiWP_002851519.1. NC_002163.1.
YP_002345040.1. NC_002163.1.

Genome annotation databases

EnsemblBacteriaiCAL35768; CAL35768; Cj1672c.
GeneIDi905947.
KEGGicje:Cj1672c.
PATRICi20060320. VBICamJej33762_1647.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL111168 Genomic DNA. Translation: CAL35768.1.
PIRiE81264.
RefSeqiWP_002851519.1. NC_002163.1.
YP_002345040.1. NC_002163.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QN3X-ray2.13A/B/C/D1-414[»]
ProteinModelPortaliP42448.
SMRiP42448.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP42448. 31 interactors.
STRINGi192222.Cj1672c.

Proteomic databases

PaxDbiP42448.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAL35768; CAL35768; Cj1672c.
GeneIDi905947.
KEGGicje:Cj1672c.
PATRICi20060320. VBICamJej33762_1647.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
BioCyciCJEJ192222:GJTS-1580-MONOMER.

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 nameiENO_CAMJE
AccessioniPrimary (citable) accession number: P42448
Secondary accession number(s): Q0P7V7, Q9PM05
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: December 1, 2000
Last modified: March 15, 2017
This is version 128 of the entry and version 2 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.