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Protein

Enolase 2

Gene

eno2

Organism
Lactobacillus gasseri (strain ATCC 33323 / DSM 20243 / JCM 1131 / NCIMB 11718 / AM63)
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. no protein annotated in this organism
  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 sitei155SubstrateUniRule annotation1
Binding sitei164SubstrateUniRule annotation1
Active sitei205Proton donorUniRule annotation1
Metal bindingi242MagnesiumUniRule 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:
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
Ordered Locus Names:LGAS_1305
OrganismiLactobacillus gasseri (strain ATCC 33323 / DSM 20243 / JCM 1131 / NCIMB 11718 / AM63)
Taxonomic identifieri324831 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

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_00002808561 – 432Enolase 2Add BLAST432

Proteomic databases

PRIDEiQ042F4.

Structurei

Secondary structure

1432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 13Combined sources10
Beta strandi19 – 27Combined sources9
Beta strandi32 – 36Combined sources5
Helixi59 – 61Combined sources3
Helixi65 – 72Combined sources8
Helixi74 – 79Combined sources6
Helixi87 – 98Combined sources12
Turni104 – 106Combined sources3
Helixi108 – 126Combined sources19
Helixi130 – 135Combined sources6
Beta strandi147 – 151Combined sources5
Beta strandi164 – 168Combined sources5
Helixi175 – 195Combined sources21
Helixi217 – 228Combined sources12
Turni234 – 236Combined sources3
Beta strandi237 – 242Combined sources6
Helixi245 – 248Combined sources4
Helixi271 – 280Combined sources10
Beta strandi283 – 287Combined sources5
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 strandi388 – 390Combined sources3
Beta strandi394 – 396Combined sources3
Helixi397 – 413Combined sources17
Helixi414 – 416Combined sources3
Helixi421 – 424Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4MKSX-ray2.08A/B1-432[»]
ProteinModelPortaliQ042F4.
SMRiQ042F4.
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

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

Q042F4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVITDIHAR EVLDSRGNPT VEAEVYTELG GFGRAIVPSG ASTGEHEAVE
60 70 80 90 100
LRDGDKSRFG GQGVLTAVEN VNGEIAKAVI GLDVTDQRLI DQTMIDLDGT
110 120 130 140 150
PNKGRLGANA ILSVSLASAR AAADELGLPL YEYLGGPNAH VLPTPMMNVI
160 170 180 190 200
NGGKHADNNV DIQEFMIMPV GAKSLHEAVR MGAETFHTLK GLLQERGEST
210 220 230 240 250
AVGDEGGFAP NLKNNEEPFE ILVEAIQRAG YKPGQDIAIA FDCAASEFYN
260 270 280 290 300
KDTKKYVTVA DGREYTAEEW TSLIEDLVDK YPVISVEDPL DENDWEGWKT
310 320 330 340 350
FTERLGDKVQ IVGDDLFVTN TSYLEKGIKM GVANSILIKL NQIGTLTETF
360 370 380 390 400
EAIEMAKEAG YTAVVSHRSG ETEDTTIADL VVATNAGQIK TGSMSRTDRI
410 420 430
AKYNQLMRIE EALGSTAQYK GIHSFYNLHK QF
Length:432
Mass (Da):46,911
Last modified:November 14, 2006 - v1
Checksum:i8567FD11E2EC934C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000413 Genomic DNA. Translation: ABJ60668.1.
RefSeqiWP_003647015.1. NZ_BALQ01000002.1.

Genome annotation databases

EnsemblBacteriaiABJ60668; ABJ60668; LGAS_1305.
GeneIDi29638960.
KEGGilga:LGAS_1305.

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 nameiENO2_LACGA
AccessioniPrimary (citable) accession number: Q042F4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: November 14, 2006
Last modified: July 5, 2017
This is version 82 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

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