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B1YLD8

- ENO_EXIS2

UniProt

B1YLD8 - ENO_EXIS2

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Protein

Enolase

Gene
eno, Exig_2393
Organism
Exiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15)
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 sitei155 – 1551Substrate By similarity
Binding sitei164 – 1641Substrate By similarity
Active sitei205 – 2051Proton donor By similarity
Metal bindingi242 – 2421Magnesium By similarity
Metal bindingi287 – 2871Magnesium By similarity
Binding sitei287 – 2871Substrate By similarity
Metal bindingi314 – 3141Magnesium By similarity
Binding sitei314 – 3141Substrate By similarity
Active sitei339 – 3391Proton acceptor By similarity
Binding sitei339 – 3391Substrate (covalent); in inhibited form By similarity
Binding sitei390 – 3901Substrate 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

BioCyciESIB262543:GHBP-2474-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:Exig_2393
OrganismiExiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15)
Taxonomic identifieri262543 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillales Family XII. Incertae SedisExiguobacterium
ProteomesiUP000001681: Chromosome

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 – 430430EnolaseUniRule annotationPRO_1000115864Add
BLAST

Proteomic databases

PRIDEiB1YLD8.

Interactioni

Protein-protein interaction databases

STRINGi262543.Exig_2393.

Structurei

3D structure databases

ProteinModelPortaliB1YLD8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni366 – 3694Substrate 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.

B1YLD8-1 [UniParc]FASTAAdd to Basket

« Hide

MSMITEIYAR EILDSRGNPT VEVEVYTEDG GFGRALVPSG ASTGEHEAVE    50
LRDGDKSRYL GKGVLKAVDN VNEKLAPEII GYDVFDQAGI DKKMIDLDGT 100
KNKGNFGANA ILGISMAAAR AAADELGLPL YTYLGGFNAK TLPTPMMNII 150
NGGSHADNNV DFQEFMIMPV GAPTFKEALR MGAEIFHALK SVLSGMGLNT 200
AVGDEGGFAP NLKSNEEAIT VILEAIEKAG YKAGEDVYLA MDVASSEFYD 250
KAAGKYNLAG EGKVLSTEEL VEFYAQLVDK YPIISIEDGC DENDWDGHKL 300
LTDRIGHKVQ LVGDDLFVTN TEKLAEGIEK GIANSILIKV NQIGTLTETF 350
DAIEMAKKAG YTAVVSHRSG ETEDSTIADI AVATNAGQIK TGSLSRTDRI 400
AKYNQLLRIE DMLSDVAVYD GIKSFYNLKK 430
Length:430
Mass (Da):46,328
Last modified:May 20, 2008 - v1
Checksum:iD332A59301988103
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001022 Genomic DNA. Translation: ACB61843.1.
RefSeqiYP_001814860.1. NC_010556.1.

Genome annotation databases

EnsemblBacteriaiACB61843; ACB61843; Exig_2393.
GeneIDi6172765.
KEGGiesi:Exig_2393.
PATRICi32138418. VBIExiSib53410_2431.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001022 Genomic DNA. Translation: ACB61843.1 .
RefSeqi YP_001814860.1. NC_010556.1.

3D structure databases

ProteinModelPortali B1YLD8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 262543.Exig_2393.

Proteomic databases

PRIDEi B1YLD8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACB61843 ; ACB61843 ; Exig_2393 .
GeneIDi 6172765.
KEGGi esi:Exig_2393.
PATRICi 32138418. VBIExiSib53410_2431.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00187 .
BioCyci ESIB262543:GHBP-2474-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: DSM 17290 / JCM 13490 / 255-15.

Entry informationi

Entry nameiENO_EXIS2
AccessioniPrimary (citable) accession number: B1YLD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: June 11, 2014
This is version 41 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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