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Protein

Enolase

Gene

eno

Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Status
Reviewed-Annotation score: Annotation score: 4 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.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-independent phosphoglycerate mutase (gpmI)
  4. Enolase (eno)
  5. 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 sitei157SubstrateUniRule annotation1
Binding sitei166SubstrateUniRule annotation1
Active sitei207Proton donorUniRule annotation1
Metal bindingi244MagnesiumUniRule 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

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, 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:CBU_1674
OrganismiCoxiella burnetii (strain RSA 493 / Nine Mile phase I)
Taxonomic identifieri227377 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
Proteomesi
  • UP000002671 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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001338771 – 428EnolaseAdd BLAST428

Proteomic databases

PRIDEiQ83B44.

Interactioni

Subunit structurei

Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation.UniRule annotation

Protein-protein interaction databases

STRINGi227377.CBU_1674.

Structurei

Secondary structure

1428
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 14Combined sources10
Beta strandi20 – 28Combined sources9
Beta strandi33 – 37Combined sources5
Helixi60 – 62Combined sources3
Helixi66 – 73Combined sources8
Helixi75 – 80Combined sources6
Helixi88 – 99Combined sources12
Turni105 – 107Combined sources3
Helixi109 – 126Combined sources18
Helixi131 – 136Combined sources6
Turni137 – 139Combined sources3
Beta strandi146 – 153Combined sources8
Beta strandi163 – 170Combined sources8
Helixi177 – 197Combined sources21
Helixi217 – 230Combined sources14
Turni235 – 237Combined sources3
Beta strandi240 – 244Combined sources5
Helixi247 – 249Combined sources3
Beta strandi250 – 252Combined sources3
Beta strandi259 – 261Combined sources3
Helixi265 – 278Combined sources14
Beta strandi281 – 285Combined sources5
Helixi293 – 303Combined sources11
Turni304 – 306Combined sources3
Beta strandi307 – 312Combined sources6
Turni313 – 317Combined sources5
Helixi319 – 327Combined sources9
Beta strandi332 – 336Combined sources5
Helixi338 – 341Combined sources4
Helixi344 – 356Combined sources13
Beta strandi360 – 364Combined sources5
Helixi374 – 381Combined sources8
Beta strandi385 – 388Combined sources4
Beta strandi392 – 394Combined sources3
Helixi395 – 411Combined sources17
Helixi419 – 422Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TQPX-ray2.20A/B1-428[»]
ProteinModelPortaliQ83B44.
SMRiQ83B44.
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

eggNOGiENOG4105C70. Bacteria.
COG0148. LUCA.
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.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SMARTiSM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q83B44-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTATITDINA HEILDSRANP TLEVRVTLSS QAYGCAAVPS GASTGEREAV
60 70 80 90 100
ELRDNDLERY GGKGVLQAVE NVNGPIRDAL LGQDPRSQEE IDRIMIELDG
110 120 130 140 150
TENKANLGAN AILGVSLAVA YAAANNADLP LYRYLGGDGG PFSMPVPMMN
160 170 180 190 200
IINGGAHATN NLDFQEFMIV PVGAPTFAEA LRYGAEVFHA LKKRLVSRGL
210 220 230 240 250
MSAVGDEGGF APDLPNNEAA FELILEAIED ANYVPGKDIY LALDAASSEL
260 270 280 290 300
YQNGRYDFEN NQLTSEEMID RLTEWTKKYP VISIEDGLSE NDWAGWKLLT
310 320 330 340 350
ERLENKVQLV GDDIFVTNPD ILEKGIKKNI ANAILVKLNQ IGTLTETLAT
360 370 380 390 400
VGLAKSNKYG VIISHRSGET EDTTIADLAV ATDARQIKTG SLCRSDRVAK
410 420
YNRLLQIERE LNDQAPYAGK EAFLFNRK
Length:428
Mass (Da):46,626
Last modified:June 1, 2003 - v1
Checksum:iB58295D02CC2BE61
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016828 Genomic DNA. Translation: AAO91170.1.
RefSeqiNP_820656.1. NC_002971.3.
WP_005770583.1. NZ_CDBG01000001.1.

Genome annotation databases

EnsemblBacteriaiAAO91170; AAO91170; CBU_1674.
GeneIDi1209585.
KEGGicbu:CBU_1674.
PATRICi17932089. VBICoxBur82552_1663.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016828 Genomic DNA. Translation: AAO91170.1.
RefSeqiNP_820656.1. NC_002971.3.
WP_005770583.1. NZ_CDBG01000001.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TQPX-ray2.20A/B1-428[»]
ProteinModelPortaliQ83B44.
SMRiQ83B44.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi227377.CBU_1674.

Proteomic databases

PRIDEiQ83B44.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO91170; AAO91170; CBU_1674.
GeneIDi1209585.
KEGGicbu:CBU_1674.
PATRICi17932089. VBICoxBur82552_1663.

Phylogenomic databases

eggNOGiENOG4105C70. Bacteria.
COG0148. LUCA.
HOGENOMiHOG000072174.
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.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SMARTiSM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiENO_COXBU
AccessioniPrimary (citable) accession number: Q83B44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Coxiella burnetii
    Coxiella burnetii (strain RSA 493): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.