SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q2YPV0

- ENO_BRUA2

UniProt

Q2YPV0 - ENO_BRUA2

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Enolase
Gene
eno, BAB1_1155
Organism
Brucella abortus (strain 2308)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis By similarity.UniRule annotation

Catalytic activityi

2-phospho-D-glycerate = phosphoenolpyruvate + H2O.UniRule annotation

Cofactori

Magnesium By similarity.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 By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei154 – 1541Substrate By similarity
Binding sitei163 – 1631Substrate By similarity
Active sitei204 – 2041Proton donor By similarity
Metal bindingi241 – 2411Magnesium By similarity
Metal bindingi284 – 2841Magnesium By similarity
Binding sitei284 – 2841Substrate By similarity
Metal bindingi311 – 3111Magnesium By similarity
Binding sitei311 – 3111Substrate By similarity
Active sitei336 – 3361Proton acceptor By similarity
Binding sitei336 – 3361Substrate (covalent); in inhibited form By similarity
Binding sitei387 – 3871Substrate By similarity

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

BioCyciBABO359391:GKDV-1177-MONOMER.
BMEL359391:GJOQ-1177-MONOMER.
UniPathwayiUPA00109; UER00187.

Names & Taxonomyi

Protein namesi
Recommended name:
Enolase (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
2-phosphoglycerate dehydratase
Gene namesi
Name:eno
Ordered Locus Names:BAB1_1155
OrganismiBrucella abortus (strain 2308)
Taxonomic identifieri359391 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000002719: Chromosome I

Subcellular locationi

Cytoplasm By similarity. Secreted By similarity. Cell surface By similarity
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 By similarity.UniRule annotation

GO - Cellular componenti

  1. cell surface Source: UniProtKB-SubCell
  2. extracellular region Source: UniProtKB-SubCell
  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 – 425425EnolaseUniRule annotation
PRO_0000267006Add
BLAST

Proteomic databases

PRIDEiQ2YPV0.

Interactioni

Protein-protein interaction databases

STRINGi359391.BAB1_1155.

Structurei

3D structure databases

ProteinModelPortaliQ2YPV0.
SMRiQ2YPV0. Positions 2-418.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni363 – 3664Substrate binding By similarity

Sequence similaritiesi

Belongs to the enolase family.

Phylogenomic databases

eggNOGiCOG0148.
HOGENOMiHOG000072173.
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.

Q2YPV0-1 [UniParc]FASTAAdd to Basket

« Hide

MTAIIDIVGR EILDSRGNPT VEVDVVLEDG SFGRAAVPSG ASTGAHEAVE    50
LRDGGSRYLG KGVEKAVEVV NGKIFDAIAG MDAESQLLID QTLIDLDGSA 100
NKGNLGANAI LGVSLAVAKA AAQASGLPLY RYVGGTNAHV LPVPMMNIIN 150
GGAHADNPID FQEFMILPVG ATSIREAVRY GSEVFHTLKK RLKDAGHNTN 200
VGDEGGFAPN LKNAQAALDF IMESIEKAGF KPGEDIALGL DCAATEFFKD 250
GNYVYEGERK TRDPKAQAKY LAKLASDYPI VTIEDGMAED DWEGWKYLTD 300
LIGNKCQLVG DDLFVTNSAR LRDGIRLGVA NSILVKVNQI GSLSETLDAV 350
ETAHKAGYTA VMSHRSGETE DSTIADLAVA TNCGQIKTGS LARSDRTAKY 400
NQLIRIEEEL GKQARYAGRS ALKLL 425
Length:425
Mass (Da):45,261
Last modified:February 7, 2006 - v1
Checksum:iA148573BD4696545
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM040264 Genomic DNA. Translation: CAJ11111.1.
RefSeqiYP_414546.1. NC_007618.1.

Genome annotation databases

EnsemblBacteriaiCAJ11111; CAJ11111; BAB1_1155.
GeneIDi3788689.
KEGGibmf:BAB1_1155.
PATRICi17845267. VBIBruMel86222_1203.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM040264 Genomic DNA. Translation: CAJ11111.1 .
RefSeqi YP_414546.1. NC_007618.1.

3D structure databases

ProteinModelPortali Q2YPV0.
SMRi Q2YPV0. Positions 2-418.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 359391.BAB1_1155.

Proteomic databases

PRIDEi Q2YPV0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAJ11111 ; CAJ11111 ; BAB1_1155 .
GeneIDi 3788689.
KEGGi bmf:BAB1_1155.
PATRICi 17845267. VBIBruMel86222_1203.

Phylogenomic databases

eggNOGi COG0148.
HOGENOMi HOG000072173.
KOi K01689.
OMAi RSEIKGQ.
OrthoDBi EOG65J589.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00187 .
BioCyci BABO359391:GKDV-1177-MONOMER.
BMEL359391:GJOQ-1177-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: 2308.

Entry informationi

Entry nameiENO_BRUA2
AccessioniPrimary (citable) accession number: Q2YPV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: February 7, 2006
Last modified: June 11, 2014
This is version 64 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

Complete proteome

Documents

  1. Brucella abortus strain 2308
    Brucella abortus (strain 2308): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi