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Protein

Enolase

Gene

eno

Organism
Burkholderia mallei (strain NCTC 10247)
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. no protein annotated in this organism
  3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
  4. Enolase (eno)
  5. no protein annotated in this organism
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

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:BMA10247_1466
OrganismiBurkholderia mallei (strain NCTC 10247)
Taxonomic identifieri320389 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

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_10000191911 – 427EnolaseAdd BLAST427

Proteomic databases

PRIDEiA3ML77

Structurei

3D structure databases

ProteinModelPortaliA3ML77
SMRiA3ML77
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

HOGENOMiHOG000072174
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.

A3ML77-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAIVDIIGR EILDSRGNPT VECDVLLESG TMGRAAVPSG ASTGSREAIE
60 70 80 90 100
LRDGEAGRYG GKGVLKAVEH INTEISEAIM GLDASEQAFL DKTLLELDGT
110 120 130 140 150
DNKSRLGANA MLAVSMAVAK AAAEEAGLPL YRYFGGSGAM QLPVPMMNIV
160 170 180 190 200
NGGAHANNSL DIQEFMIVPV SQPTFREALR CGAEVFHALK KILGDRGMST
210 220 230 240 250
AVGDEGGFAP NFGSNDECLS TILQAIEKAG YRAGEDVLLA LDCAASEFYH
260 270 280 290 300
DGKYQLAGEG LQLSSAEFTD YLATLADKFP IVSIEDGMHE GDWDGWKLLT
310 320 330 340 350
ERLGKKVQLV GDDLFVTNTR ILKEGIEKGI ANSILIKINQ IGTLTETFAA
360 370 380 390 400
IEMAKRARYT AVISHRSGET EDSTIADIAV GLNAGQIKTG SLSRSDRISK
410 420
YNQLLRIEED LGDIASYPGK SAFYNLR
Length:427
Mass (Da):45,683
Last modified:April 3, 2007 - v1
Checksum:i37F3B901EEABF5B0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000548 Genomic DNA Translation: ABO06172.1
RefSeqiWP_004192585.1, NZ_CP007802.1

Genome annotation databases

EnsemblBacteriaiABO06172; ABO06172; BMA10247_1466
KEGGibmaz:BM44_1681
bmn:BMA10247_1466
PATRICifig|320389.8.peg.1880

Similar proteinsi

Entry informationi

Entry nameiENO_BURM7
AccessioniPrimary (citable) accession number: A3ML77
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 2007
Last modified: May 23, 2018
This is version 76 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health