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Protein

Enolase

Gene

eno

Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
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 sitei159SubstrateUniRule annotation1
Binding sitei168SubstrateUniRule annotation1
Active sitei209Proton donorUniRule annotation1
Metal bindingi246MagnesiumUniRule annotation1
Metal bindingi287MagnesiumUniRule annotation1
Binding sitei287SubstrateUniRule annotation1
Metal bindingi314MagnesiumUniRule annotation1
Binding sitei314SubstrateUniRule annotation1
Active sitei339Proton acceptorUniRule annotation1
Binding sitei339Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei390SubstrateUniRule 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:syc0886_c
OrganismiSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
Taxonomic identifieri269084 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeSynechococcus
Proteomesi
  • UP000001175 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_00001339911 – 430EnolaseAdd BLAST430

Interactioni

Protein-protein interaction databases

STRINGi269084.syc0886_c.

Structurei

Secondary structure

1430
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 18Combined sources11
Beta strandi24 – 32Combined sources9
Beta strandi37 – 41Combined sources5
Helixi64 – 66Combined sources3
Helixi70 – 83Combined sources14
Helixi91 – 102Combined sources12
Turni108 – 110Combined sources3
Helixi112 – 129Combined sources18
Helixi134 – 139Combined sources6
Helixi140 – 142Combined sources3
Beta strandi148 – 155Combined sources8
Helixi157 – 159Combined sources3
Beta strandi160 – 163Combined sources4
Beta strandi166 – 172Combined sources7
Helixi179 – 199Combined sources21
Helixi219 – 232Combined sources14
Turni238 – 240Combined sources3
Beta strandi241 – 246Combined sources6
Helixi249 – 252Combined sources4
Beta strandi257 – 260Combined sources4
Beta strandi263 – 265Combined sources3
Helixi267 – 280Combined sources14
Beta strandi283 – 288Combined sources6
Helixi295 – 305Combined sources11
Turni306 – 308Combined sources3
Beta strandi309 – 314Combined sources6
Turni315 – 319Combined sources5
Helixi321 – 330Combined sources10
Beta strandi334 – 338Combined sources5
Helixi340 – 343Combined sources4
Helixi346 – 358Combined sources13
Beta strandi362 – 366Combined sources5
Helixi376 – 383Combined sources8
Beta strandi387 – 392Combined sources6
Beta strandi394 – 396Combined sources3
Helixi397 – 413Combined sources17
Helixi414 – 416Combined sources3
Helixi420 – 422Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ROPX-ray2.05A1-430[»]
5J04X-ray2.30A/B5-429[»]
ProteinModelPortaliQ5N3P4.
SMRiQ5N3P4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni366 – 369Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0148. 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.
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.

Q5N3P4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPDDYGTQIA EITAREILDS RGRPTVEAEV HLEDGSVGLA QVPSGASTGT
60 70 80 90 100
FEAHELRDDD PSRYGGKGVQ KAVENVSAIE DALIGLSALD QEGLDKAMIA
110 120 130 140 150
LDGTPNKKNL GANAILAVSL ATAHAAATSL NLPLYRYLGG PLANVLPVPM
160 170 180 190 200
MNVINGGAHA DNNVDFQEFM IMPVGAPSFK EALRWGAEVF HALAKVLKDK
210 220 230 240 250
GLATGVGDEG GFAPNLGSNK EALELLLTAI EAAGYKPGEQ VALAMDVASS
260 270 280 290 300
EFYKNGLYTC DGVSHEPAGM IGILADLVSQ YPIVSIEDGL QEDDWSNWKT
310 320 330 340 350
LTQQLGSTVQ LVGDDLFVTN PDRLQSGIEQ GVGNAVLIKL NQIGTLTETL
360 370 380 390 400
RTIDLATRSG YRSVISHRSG ETEDTTIADL AVATRAGQIK TGSLSRSERI
410 420 430
AKYNRLLRIE AALGENALYA GAIGLGPKGR
Length:430
Mass (Da):45,379
Last modified:February 1, 2005 - v1
Checksum:iA21B12D699866725
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008231 Genomic DNA. Translation: BAD79076.1.
RefSeqiWP_011243198.1. NC_006576.1.

Genome annotation databases

EnsemblBacteriaiBAD79076; BAD79076; syc0886_c.
KEGGisyc:syc0886_c.

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.

Entry informationi

Entry nameiENO_SYNP6
AccessioniPrimary (citable) accession number: Q5N3P4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: February 1, 2005
Last modified: June 7, 2017
This is version 92 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

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