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Q83B44

- ENO_COXBU

UniProt

Q83B44 - ENO_COXBU

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Protein

Enolase

Gene

eno

Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei157 – 1571SubstrateUniRule annotation
Binding sitei166 – 1661SubstrateUniRule annotation
Active sitei207 – 2071Proton donorUniRule annotation
Metal bindingi244 – 2441MagnesiumUniRule annotation
Metal bindingi285 – 2851MagnesiumUniRule annotation
Binding sitei285 – 2851SubstrateUniRule annotation
Metal bindingi312 – 3121MagnesiumUniRule annotation
Binding sitei312 – 3121SubstrateUniRule annotation
Active sitei337 – 3371Proton acceptorUniRule annotation
Binding sitei337 – 3371Substrate (covalent); in inhibited formUniRule annotation
Binding sitei388 – 3881SubstrateUniRule annotation

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. phosphopyruvate hydratase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. glycolytic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciCBUR227377:GJ7S-1645-MONOMER.
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
ProteomesiUP000002671: 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

  1. cell surface Source: UniProtKB-HAMAP
  2. extracellular region Source: UniProtKB-KW
  3. phosphopyruvate hydratase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428EnolasePRO_0000133877Add
BLAST

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

1
428
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 1410Combined sources
Beta strandi20 – 289Combined sources
Beta strandi33 – 375Combined sources
Helixi60 – 623Combined sources
Helixi66 – 738Combined sources
Helixi75 – 806Combined sources
Helixi88 – 9912Combined sources
Turni105 – 1073Combined sources
Helixi109 – 12618Combined sources
Helixi131 – 1366Combined sources
Turni137 – 1393Combined sources
Beta strandi146 – 1538Combined sources
Beta strandi163 – 1708Combined sources
Helixi177 – 19721Combined sources
Helixi217 – 23014Combined sources
Turni235 – 2373Combined sources
Beta strandi240 – 2445Combined sources
Helixi247 – 2493Combined sources
Beta strandi250 – 2523Combined sources
Beta strandi259 – 2613Combined sources
Helixi265 – 27814Combined sources
Beta strandi281 – 2855Combined sources
Helixi293 – 30311Combined sources
Turni304 – 3063Combined sources
Beta strandi307 – 3126Combined sources
Turni313 – 3175Combined sources
Helixi319 – 3279Combined sources
Beta strandi332 – 3365Combined sources
Helixi338 – 3414Combined sources
Helixi344 – 35613Combined sources
Beta strandi360 – 3645Combined sources
Helixi374 – 3818Combined sources
Beta strandi385 – 3884Combined sources
Beta strandi392 – 3943Combined sources
Helixi395 – 41117Combined sources
Helixi419 – 4224Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TQPX-ray2.20A/B1-428[»]
ProteinModelPortaliQ83B44.
SMRiQ83B44. Positions 3-423.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni364 – 3674Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0148.
HOGENOMiHOG000072174.
KOiK01689.
OMAiRSEIKGQ.
OrthoDBiEOG65J589.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
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.
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.

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 .
RefSeqi NP_820656.1. NC_002971.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3TQP X-ray 2.20 A/B 1-428 [» ]
ProteinModelPortali Q83B44.
SMRi Q83B44. Positions 3-423.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 227377.CBU_1674.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO91170 ; AAO91170 ; CBU_1674 .
GeneIDi 1209585.
KEGGi cbu:CBU_1674.
PATRICi 17932089. VBICoxBur82552_1663.

Phylogenomic databases

eggNOGi COG0148.
HOGENOMi HOG000072174.
KOi K01689.
OMAi RSEIKGQ.
OrthoDBi EOG65J589.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00187 .
BioCyci CBUR227377:GJ7S-1645-MONOMER.

Family and domain databases

Gene3Di 3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPi MF_00318. Enolase.
InterProi IPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N_like.
[Graphical view ]
PANTHERi PTHR11902. PTHR11902. 1 hit.
Pfami PF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF001400. Enolase. 1 hit.
PRINTSi PR00148. ENOLASE.
SUPFAMi SSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsi TIGR01060. eno. 1 hit.
PROSITEi PS00164. ENOLASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RSA 493 / Nine Mile phase I.

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 26, 2014
This is version 81 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

External Data

Dasty 3