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Protein

Enolase

Gene

eno

Organism
Bacillus anthracis
Status
Unreviewed-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

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

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 (pykA1), Pyruvate kinase (MCCC1A01412_07425), 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

GO - Biological processi

Keywordsi

Molecular functionLyaseUniRule annotation
Biological processGlycolysisUniRule annotation
LigandMagnesiumUniRule annotation, Metal-bindingUniRule annotation

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
ORF Names:COK92_23670Imported
OrganismiBacillus anthracisImported
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000222996 Componenti: Unassembled WGS sequence

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

CytoplasmUniRule annotation, SecretedUniRule annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 134Enolase_NInterPro annotationAdd BLAST131
Domaini139 – 428Enolase_CInterPro annotationAdd BLAST290

Region

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

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

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.

A0A2B3XVD4-1 [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 DGVKSFYNIK R
Length:431
Mass (Da):46,404
Last modified:January 31, 2018 - v1
Checksum:i0D22E012933C100C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
NVDP01000024 Genomic DNA Translation: PFU89681.1
RefSeqiWP_001975088.1, NZ_NVMW01000005.1

Similar proteinsi

Entry informationi

Entry nameiA0A2B3XVD4_BACAN
AccessioniPrimary (citable) accession number: A0A2B3XVD4
Entry historyiIntegrated into UniProtKB/TrEMBL: January 31, 2018
Last sequence update: January 31, 2018
Last modified: April 25, 2018
This is version 4 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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