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Protein

Enolase

Gene

eno

Organism
Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12)
Status
Reviewed-Annotation score: Annotation score: 4 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-dependent phosphoglycerate mutase (gpmA)
  4. Enolase (eno)
  5. Pyruvate kinase, Pyruvate kinase (Blon_1745)
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 bindingi285MagnesiumUniRule annotation1
Binding sitei285SubstrateUniRule annotation1
Metal bindingi312MagnesiumUniRule annotation1
Binding sitei312SubstrateUniRule annotation1
Active sitei337Proton acceptorUniRule annotation1
Binding sitei337Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei388SubstrateUniRule annotation1

GO - Molecular functioni

  • magnesium ion binding Source: InterPro
  • phosphopyruvate hydratase activity Source: UniProtKB-EC
  • protease binding Source: CAFA

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:Blon_1836, BLIJ_1901
OrganismiBifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12)
Taxonomic identifieri391904 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaBifidobacterialesBifidobacteriaceaeBifidobacterium
Proteomesi
  • UP000001360 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

  • cell surface Source: UniProtKB-SubCell
  • cell wall Source: CAFA
  • extracellular region Source: UniProtKB-SubCell
  • phosphopyruvate hydratase complex Source: InterPro

Keywords - Cellular componenti

Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001329861 – 432EnolaseAdd BLAST432

Interactioni

GO - Molecular functioni

  • protease binding Source: CAFA

Structurei

3D structure databases

ProteinModelPortaliB7GTK2.
SMRiB7GTK2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni364 – 367Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

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.

B7GTK2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVIESVYAR QILDSRGNPT VEVYLETEDG AQGKGLVPSG ASTGEAEAWE
60 70 80 90 100
RRDGDKSVYG GKGVLNAVKA VNEVIAPKVI GMDAADQRAL DDLMIELDGT
110 120 130 140 150
PNKGKLGANA ILGVSLAALY ASAESAGLPL YRYIGGTNGH ILPVPNMNIM
160 170 180 190 200
NGGAHADFAT DIQEYMISPY GFDTYSEALR AGVEVYHTLK NVLKKEGLNT
210 220 230 240 250
GLGDEGGFAP KMKSNEDSLK YIMDAISAAG YEPGKQIGIC LDVASSEFYN
260 270 280 290 300
KETGKYRFDG EERDSAYMLD YYENLINEYP IVSIEDPFNE EGWEDWAAIT
310 320 330 340 350
ARLGDRLQFV GDDLLVTNPA RLQKAIDLGA ANSLLVKLNQ IGSVTETLDA
360 370 380 390 400
IELATANGYT SMVSHRSGET PDTTISDLAV AKNTRQIKTG APARGERVAK
410 420 430
YNRLLEIEEE LGSTAQYAGY TAFKACKKYL AK
Length:432
Mass (Da):46,623
Last modified:February 10, 2009 - v1
Checksum:i8417C956554A19BC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001095 Genomic DNA. Translation: ACJ52911.1.
AP010889 Genomic DNA. Translation: BAJ69480.1.
RefSeqiWP_012578127.1. NZ_JDTT01000009.1.

Genome annotation databases

EnsemblBacteriaiACJ52911; ACJ52911; Blon_1836.
BAJ69480; BAJ69480; BLIJ_1901.
KEGGibln:Blon_1836.
blon:BLIJ_1901.
PATRICi21124724. VBIBifLon71229_1842.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001095 Genomic DNA. Translation: ACJ52911.1.
AP010889 Genomic DNA. Translation: BAJ69480.1.
RefSeqiWP_012578127.1. NZ_JDTT01000009.1.

3D structure databases

ProteinModelPortaliB7GTK2.
SMRiB7GTK2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACJ52911; ACJ52911; Blon_1836.
BAJ69480; BAJ69480; BLIJ_1901.
KEGGibln:Blon_1836.
blon:BLIJ_1901.
PATRICi21124724. VBIBifLon71229_1842.

Phylogenomic databases

HOGENOMiHOG000072173.
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_BIFLS
AccessioniPrimary (citable) accession number: B7GTK2
Secondary accession number(s): E8MLQ3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: May 10, 2017
This is version 59 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

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.