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Protein

Enolase

Gene

eno

Organism
Staphylococcus carnosus (strain TM300)
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), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
  4. Enolase (eno)
  5. Pyruvate kinase (pykA)
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 sitei157SubstrateUniRule annotation1
Binding sitei166SubstrateUniRule annotation1
Active sitei207Proton donorUniRule annotation1
Metal bindingi244MagnesiumUniRule annotation1
Metal bindingi291MagnesiumUniRule annotation1
Binding sitei291SubstrateUniRule annotation1
Metal bindingi318MagnesiumUniRule annotation1
Binding sitei318SubstrateUniRule annotation1
Active sitei343Proton acceptorUniRule annotation1
Binding sitei343Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei394SubstrateUniRule 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:Sca_0428
OrganismiStaphylococcus carnosus (strain TM300)
Taxonomic identifieri396513 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000444 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_10001330201 – 434EnolaseAdd BLAST434

Proteomic databases

PRIDEiB9DJJ9.

Interactioni

Protein-protein interaction databases

STRINGi396513.Sca_0428.

Structurei

3D structure databases

ProteinModelPortaliB9DJJ9.
SMRiB9DJJ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni370 – 373Substrate 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.
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.

B9DJJ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIITDVYAR EVLDSRGNPT VEVEVLTESG AFGRALVPSG ASTGEYEAVE
60 70 80 90 100
LRDGDKDRYL GKGVTKAVEN VNEKIAPEIV EGEFSVLDQV SIDKMMIQLD
110 120 130 140 150
GTENKGKLGA NAILGVSIAV ARAAADLLGQ PLYKYLGGFN GKQLPVPMMN
160 170 180 190 200
IVNGGSHSDA PIAFQEFMIL PVGADSFKES LRWGAEIFHN LAKILKKRGL
210 220 230 240 250
ETAVGDEGGF APKFHGTEDA VDTILEAIKA VGLEPGKDVY LGFDIASSEF
260 270 280 290 300
YENGVYDYTK FEGPEGAKRT SAEQVDYLEE LVNKYPIITI EDGMDENDWD
310 320 330 340 350
GWKQLTDRLG KKVQLVGDDL FVTNTKKLSE GIEKGIGNSI LIKVNQIGTL
360 370 380 390 400
TETFDAIQMA QKAGYTAVIS HRSGETEDTT IADIAVATNA GQIKTGSLSR
410 420 430
TDRIAKYNQL LRIEDELYET AEFDGIHSFY NLDK
Length:434
Mass (Da):47,269
Last modified:March 24, 2009 - v1
Checksum:i7D2771B5B4243F57
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM295250 Genomic DNA. Translation: CAL27342.1.
RefSeqiWP_015899686.1. NC_012121.1.

Genome annotation databases

KEGGisca:SCA_0428.
PATRICi19601622. VBIStaCar105558_0428.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM295250 Genomic DNA. Translation: CAL27342.1.
RefSeqiWP_015899686.1. NC_012121.1.

3D structure databases

ProteinModelPortaliB9DJJ9.
SMRiB9DJJ9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi396513.Sca_0428.

Proteomic databases

PRIDEiB9DJJ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGisca:SCA_0428.
PATRICi19601622. VBIStaCar105558_0428.

Phylogenomic databases

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

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.
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.
ProtoNetiSearch...

Entry informationi

Entry nameiENO_STACT
AccessioniPrimary (citable) accession number: B9DJJ9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: April 12, 2017
This is version 57 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.