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Protein

Enolase

Gene

eno

Organism
Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1)
Status
Reviewed-Annotation score: Annotation score: 3 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-independent phosphoglycerate mutase (gpmI)
  4. Enolase (eno)
  5. Pyruvate kinase (Mmc1_0728), Pyruvate kinase (Mmc1_1432)
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:
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:Mmc1_1562
OrganismiMagnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1)
Taxonomic identifieri156889 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaMagnetococcalesMagnetococcaceaeMagnetococcus
Proteomesi
  • UP000002586 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_00002808621 – 429EnolaseAdd BLAST429

Interactioni

Protein-protein interaction databases

STRINGi156889.Mmc1_1562.

Structurei

3D structure databases

ProteinModelPortaliA0L7X8.
SMRiA0L7X8.
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.
HOGENOMiHOG000072174.
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.

A0L7X8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSIVEIHGR EVIDSRGNPT VEVDVYTEDG GFGRAAVPSG ASTGSREAVE
60 70 80 90 100
LRDGDKSRFL GKGVRKAVDA VNTVLAEVVL GMEVADQKGI DAAMIALDGT
110 120 130 140 150
HNKSRLGANA ILGISMAVAK AAADECDLPL YRYLGGTNTS LLPVPMMNII
160 170 180 190 200
NGGAHADNNV DIQEFMIMPV AATSCTEAIR MGAEVFHSLK KVLKSKGLNT
210 220 230 240 250
AVGDEGGFAP NLGSNEEALK VIVEAIEAAG YKPGEDIKLA LDCASSEFYN
260 270 280 290 300
KETGNYDLTG EGRVLTKQEL VAFYEDLVAK YPIISIEDGF DESDWDGWKL
310 320 330 340 350
MTEALGNKIQ LVGDDLFVTN SKILAEGISK GIANSILVKV NQIGTLTETF
360 370 380 390 400
EAVEMAQRAG YTAVISHRSG ETEDATIADI AVALNAGQIK TGSMSRSDRI
410 420
AKYNQLIRIE EELGGMARFE GMKVFYNLR
Length:429
Mass (Da):45,858
Last modified:December 12, 2006 - v1
Checksum:i32B77C905743931C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000471 Genomic DNA. Translation: ABK44071.1.
RefSeqiWP_011713221.1. NC_008576.1.

Genome annotation databases

EnsemblBacteriaiABK44071; ABK44071; Mmc1_1562.
KEGGimgm:Mmc1_1562.
PATRICi22429693. VBIMagSp23654_1602.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000471 Genomic DNA. Translation: ABK44071.1.
RefSeqiWP_011713221.1. NC_008576.1.

3D structure databases

ProteinModelPortaliA0L7X8.
SMRiA0L7X8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi156889.Mmc1_1562.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK44071; ABK44071; Mmc1_1562.
KEGGimgm:Mmc1_1562.
PATRICi22429693. VBIMagSp23654_1602.

Phylogenomic databases

eggNOGiENOG4105C70. Bacteria.
COG0148. LUCA.
HOGENOMiHOG000072174.
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 nameiENO_MAGMM
AccessioniPrimary (citable) accession number: A0L7X8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: December 12, 2006
Last modified: March 15, 2017
This is version 71 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.