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Protein

Enolase

Gene

eno

Organism
Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Status
Reviewed-Annotation score: Annotation score: 5 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. 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

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

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

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processGlycolysis, Virulence
LigandMagnesium, Metal-binding

Enzyme and pathway databases

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

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication
  • Secreted UniRule annotation1 Publication
  • Cell surface UniRule annotation1 Publication

  • 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.

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

Structurei

Secondary structure

1435
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 13Combined sources11
Beta strandi19 – 27Combined sources9
Beta strandi32 – 36Combined sources5
Beta strandi44 – 47Combined sources4
Helixi59 – 61Combined sources3
Helixi65 – 73Combined sources9
Helixi75 – 79Combined sources5
Helixi87 – 98Combined sources12
Turni104 – 106Combined sources3
Helixi108 – 126Combined sources19
Helixi130 – 135Combined sources6
Beta strandi144 – 151Combined sources8
Helixi153 – 155Combined sources3
Beta strandi157 – 159Combined sources3
Beta strandi163 – 168Combined sources6
Helixi175 – 195Combined sources21
Helixi215 – 228Combined sources14
Beta strandi237 – 243Combined sources7
Helixi246 – 249Combined sources4
Turni252 – 255Combined sources4
Beta strandi256 – 258Combined sources3
Helixi260 – 263Combined sources4
Helixi272 – 285Combined sources14
Beta strandi288 – 293Combined sources6
Helixi300 – 310Combined sources11
Turni311 – 313Combined sources3
Beta strandi314 – 319Combined sources6
Turni320 – 324Combined sources5
Helixi326 – 334Combined sources9
Beta strandi339 – 343Combined sources5
Helixi345 – 348Combined sources4
Helixi351 – 363Combined sources13
Beta strandi367 – 371Combined sources5
Helixi381 – 388Combined sources8
Beta strandi393 – 395Combined sources3
Beta strandi399 – 401Combined sources3
Helixi402 – 418Combined sources17
Helixi419 – 421Combined sources3
Helixi426 – 429Combined sources4
Helixi431 – 433Combined sources3

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...

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.
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.

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.
PATRICi19723304. VBIStrPyo30273_0600.

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...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT86712; AAT86712; M6_Spy0577.
KEGGispa:M6_Spy0577.
PATRICi19723304. VBIStrPyo30273_0600.

Phylogenomic databases

HOGENOMiHOG000072174.
KOiK01689.

Enzyme and pathway databases

UniPathwayiUPA00109; 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.
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_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: April 12, 2017
This is version 103 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. 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

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.