Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Enolase

Gene

eno

Organism
Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Status
Reviewed-Annotation score: -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. Binds plasminogen when expressed on the bacterial cell surface, potentially allowing the bacterium to acquire surface-associated proteolytic activity, which in turn contributes to tissue invasion and virulence.UniRule annotation1 Publication

Catalytic activityi

2-phospho-D-glycerate = phosphoenolpyruvate + H2O.UniRule annotation

Cofactori

Mg2+UniRule annotation

Activity 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

Kineticsi

Catalytically active also when expressed on the bacterial cell surface.
  1. KM=1.49 mM for 2-phospho-D-glycerate1 Publication
  1. Vmax=31.25 mmol/min/mg enzyme1 Publication

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. Glyceraldehyde-3-phosphate dehydrogenase (gap)
  2. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
  4. Enolase (eno)
  5. Pyruvate kinase (M6_Spy0975)
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 bindingi243MagnesiumUniRule annotation1
Metal bindingi292MagnesiumUniRule annotation1
Binding sitei292SubstrateUniRule annotation1
Metal bindingi319MagnesiumUniRule annotation1
Binding sitei319SubstrateUniRule annotation1
Active sitei344Proton acceptorUniRule annotation1
Binding sitei344Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei395SubstrateUniRule annotation1
Sitei428Important for binding of plasminogen1
Sitei434Important for binding of plasminogen1
Sitei435Important for binding of plasminogen1

GO - Molecular functioni

  • magnesium ion binding Source: UniProtKB-UniRule
  • phosphopyruvate hydratase activity Source: CAFA

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processGlycolysis, Virulence
LigandMagnesium, Metal-binding

Enzyme and pathway databases

SABIO-RKiQ5XD01
UniPathwayi
UPA00109;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:M6_Spy0577
OrganismiStreptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Taxonomic identifieri286636 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000001167 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi428K → L: No effect on catalytic activity; significant decrease in the ability to bind Glu- and Lys-plasminogen. 1 Publication1
Mutagenesisi434K → L: No effect on catalytic activity; significant decrease in the ability to bind Glu- and Lys-plasminogen. 1 Publication1
Mutagenesisi435K → L: No effect on catalytic activity; significant decrease in the ability to bind Glu- and Lys-plasminogen. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001339842 – 435EnolaseAdd BLAST434

Proteomic databases

PRIDEiQ5XD01

Structurei

Secondary structure

1435
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ5XD01
SMRiQ5XD01
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni371 – 374Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000072174
KOiK01689

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
IPR036849 Enolase-like_C_sf
IPR029017 Enolase-like_N
IPR034390 Enolase-like_superfamily
IPR020810 Enolase_C
IPR020809 Enolase_CS
IPR020811 Enolase_N
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
TIGRFAMsiTIGR01060 eno, 1 hit
PROSITEiView protein in PROSITE
PS00164 ENOLASE, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5XD01-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSIITDVYAR EVLDSRGNPT LEVEVYTESG AFGRGMVPSG ASTGEHEAVE
60 70 80 90 100
LRDGDKSRYL GLGTQKAVDN VNNIIAKAII GYDVRDQQAI DRAMIALDGT
110 120 130 140 150
PNKGKLGANA ILGVSIAVAR AAADYLEVPL YTYLGGFNTK VLPTPMMNII
160 170 180 190 200
NGGSHSDAPI AFQEFMIMPV GAPTFKEGLR WGAEVFHALK KILKERGLVT
210 220 230 240 250
AVGDEGGFAP KFEGTEDGVE TILKAIEAAG YEAGENGIMI GFDCASSEFY
260 270 280 290 300
DKERKVYDYT KFEGEGAAVR TSAEQVDYLE ELVNKYPIIT IEDGMDENDW
310 320 330 340 350
DGWKVLTERL GKRVQLVGDD FFVTNTEYLA RGIKENAANS ILIKVNQIGT
360 370 380 390 400
LTETFEAIEM AKEAGYTAVV SHRSGETEDS TIADIAVATN AGQIKTGSLS
410 420 430
RTDRIAKYNQ LLRIEDQLGE VAQYKGIKSF YNLKK
Length:435
Mass (Da):47,355
Last modified:January 23, 2007 - v3
Checksum:i5E285F357966C572
GO

Sequence cautioni

The sequence AAT86712 differs from that shown. Reason: Frameshift at position 40.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti42S → G AA sequence (PubMed:9603964).Curated1
Sequence conflicti44G → T AA sequence (PubMed:9603964).Curated1
Sequence conflicti367T → S AA sequence (PubMed:9603964).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000003 Genomic DNA Translation: AAT86712.1 Frameshift.

Genome annotation databases

EnsemblBacteriaiAAT86712; AAT86712; M6_Spy0577
KEGGispa:M6_Spy0577

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000003 Genomic DNA Translation: AAT86712.1 Frameshift.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZLFX-ray2.15A/B/C/D1-435[»]
3ZLGX-ray2.10A/B/C/D1-435[»]
3ZLHX-ray2.90A/B/C/D1-435[»]
ProteinModelPortaliQ5XD01
SMRiQ5XD01
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ5XD01

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT86712; AAT86712; M6_Spy0577
KEGGispa:M6_Spy0577

Phylogenomic databases

HOGENOMiHOG000072174
KOiK01689

Enzyme and pathway databases

UniPathwayi
UPA00109;UER00187

SABIO-RKiQ5XD01

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
IPR036849 Enolase-like_C_sf
IPR029017 Enolase-like_N
IPR034390 Enolase-like_superfamily
IPR020810 Enolase_C
IPR020809 Enolase_CS
IPR020811 Enolase_N
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
TIGRFAMsiTIGR01060 eno, 1 hit
PROSITEiView protein in PROSITE
PS00164 ENOLASE, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiENO_STRP6
AccessioniPrimary (citable) accession number: Q5XD01
Secondary accession number(s): P82479
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 23, 2007
Last modified: October 10, 2018
This is version 111 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again