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Protein

Enolase

Gene

eno

Organism
Bacillus anthracis
Status
Reviewed-Annotation score: -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), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA1), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
  4. Enolase (eno), Enolase (eno), Enolase (eno), Enolase (eno), Enolase (eno), Enolase (eno), Enolase (eno), Enolase (eno), Enolase (eno)
  5. Pyruvate kinase (MCCC1A01412_07425), Pyruvate kinase (pykA1), Pyruvate kinase (pyk), Pyruvate kinase (COJ30_11890), Pyruvate kinase (pyk2), Pyruvate kinase (COE56_07990), Pyruvate kinase (BVG01_09765), Pyruvate kinase (pyk), Pyruvate kinase (pyk), Pyruvate kinase (CN488_18960), Pyruvate kinase (CON16_24335), Pyruvate kinase (CN272_12880), Pyruvate kinase (pyk), Pyruvate kinase (pyk), Pyruvate kinase (pykA1), Pyruvate kinase (A9486_00415), Pyruvate kinase (CN907_26205), Pyruvate kinase (COK92_16395), Pyruvate kinase (pyk), Pyruvate kinase (CN286_13255), Pyruvate kinase (A9486_15570), Pyruvate kinase (CN504_15055), Pyruvate kinase (ABW01_15615), Pyruvate kinase (pyk), Pyruvate kinase (pyk)
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 bindingi288MagnesiumUniRule annotation1
Binding sitei288SubstrateUniRule annotation1
Metal bindingi315MagnesiumUniRule annotation1
Binding sitei315SubstrateUniRule annotation1
Active sitei340Proton acceptorUniRule annotation1
Binding sitei340Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei391SubstrateUniRule annotation1

GO - Molecular functioni

  • magnesium ion binding Source: InterPro
  • phosphopyruvate hydratase activity Source: TIGR

GO - Biological processi

  • glycolytic process Source: TIGR

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:BA_5364, GBAA_5364, BAS4985
OrganismiBacillus anthracis
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000594 Componenti: Chromosome
  • UP000000427 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_00001338331 – 431EnolaseAdd BLAST431

Interactioni

Protein-protein interaction databases

IntActiQ81X78, 6 interactors
STRINGi260799.BAS4985

Structurei

3D structure databases

ProteinModelPortaliQ81X78
SMRiQ81X78
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni367 – 370Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C70 Bacteria
COG0148 LUCA
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
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.

Q81X78-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTIIDVYAR EVLDSRGNPT VEVEVYTESG AFGRAIVPSG ASTGEHEAVE
60 70 80 90 100
LRDGDKSRYL GKGVMNAVNN VNEAIAPEIV GFDVTDQAGI DRAMIELDGT
110 120 130 140 150
PNKGKLGANA ILGVSMAVAH AAADFVGLPL YRYLGGFNAK QLPTPMMNII
160 170 180 190 200
NGGSHADNNV DFQEFMILPV GAPTFKESIR MGAEVFHALK AVLHDKGLNT
210 220 230 240 250
AVGDEGGFAP NLGSNREALE VIIEAIEKAG YKAGENVFLG MDVASSEFYN
260 270 280 290 300
KETGKYDLAG EGRTGLTSAE MVDFYEELCK DFPIISIEDG LDENDWDGHK
310 320 330 340 350
LLTERIGDKV QLVGDDLFVT NTQKLAEGIE KGISNSILIK VNQIGTLTET
360 370 380 390 400
FEAIEMAKRA GYTAVVSHRS GETEDATIAD IAVATNAGQI KTGSMSRTDR
410 420 430
IAKYNQLLRI EDELGEIAVY DGIKSFYNIK R
Length:431
Mass (Da):46,418
Last modified:June 1, 2003 - v1
Checksum:i1581E012933C100C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA Translation: AAP29024.1
AE017334 Genomic DNA Translation: AAT34498.1
AE017225 Genomic DNA Translation: AAT57274.1
RefSeqiNP_847538.1, NC_003997.3
WP_000103949.1, NZ_PPES01000025.1
YP_031224.1, NC_005945.1

Genome annotation databases

EnsemblBacteriaiAAP29024; AAP29024; BA_5364
AAT34498; AAT34498; GBAA_5364
AAT57274; AAT57274; BAS4985
GeneIDi1084902
2852252
KEGGiban:BA_5364
bar:GBAA_5364
bat:BAS4985
PATRICifig|198094.11.peg.5323

Similar proteinsi

Entry informationi

Entry nameiENO_BACAN
AccessioniPrimary (citable) accession number: Q81X78
Secondary accession number(s): Q6HR14, Q6KKD3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: June 1, 2003
Last modified: May 23, 2018
This is version 120 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

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