Skip Header

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

Q0BSX3

- ENO_GRABC

UniProt

Q0BSX3 - ENO_GRABC

(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

Organism
Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1)
Status
Reviewed - Annotation score: 3 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.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 sitei155 – 1551SubstrateUniRule annotation
Binding sitei164 – 1641SubstrateUniRule annotation
Active sitei205 – 2051Proton donorUniRule annotation
Metal bindingi242 – 2421MagnesiumUniRule 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

BioCyciGBET391165:GHON-1215-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:GbCGDNIH1_1181
OrganismiGranulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1)
Taxonomic identifieri391165 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGranulibacter
ProteomesiUP000001963: 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 – 425425EnolasePRO_0000267040Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi391165.GbCGDNIH1_1181.

Structurei

3D structure databases

ProteinModelPortaliQ0BSX3.
SMRiQ0BSX3. Positions 4-419.
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.

Q0BSX3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAIADIIAR EILDSRGNPT VEVDVTLESG AQGRAAVPSG ASTGAHEAVE
60 70 80 90 100
LRDGDKSRYG GKGVLHAVSF VEGEIFEAIG GMDASEQLRI DETLIAVDGT
110 120 130 140 150
PNKSRLGANA MLAVSLATAK AAANHQGVPL YRYLGGVYAR TLPVPMMNIV
160 170 180 190 200
NGGKHADNPI DIQEFMIQPV AAPTIADAVR VGAEIFAALK KELSAAGHNT
210 220 230 240 250
NVGDEGGFAP GLKSAEEALS FITKACEKAG YRPGEDVTFA LDCAATEFFK
260 270 280 290 300
DGVYDLEGEG KKFDAAGMVR YLEDLAAKFP IVSIEDGLAE DDWEGWKLLT
310 320 330 340 350
DTLGRKVQLV GDDLFVTNPD RLRHGIALGT ANAILVKVNQ IGTLSETLEA
360 370 380 390 400
VETAHRAGYA AVMSHRSGET EDSTIADLAV ATNCGQIKTG SLSRSDRTAK
410 420
YNQLIRIEQD LDTSGRYAGR TILRG
Length:425
Mass (Da):44,964
Last modified:October 17, 2006 - v1
Checksum:i61ADDFF558F007E7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000394 Genomic DNA. Translation: ABI62079.1.
RefSeqiYP_745002.1. NC_008343.1.

Genome annotation databases

EnsemblBacteriaiABI62079; ABI62079; GbCGDNIH1_1181.
GeneIDi4274672.
KEGGigbe:GbCGDNIH1_1181.
PATRICi22078521. VBIGraBet83793_1230.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000394 Genomic DNA. Translation: ABI62079.1 .
RefSeqi YP_745002.1. NC_008343.1.

3D structure databases

ProteinModelPortali Q0BSX3.
SMRi Q0BSX3. Positions 4-419.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 391165.GbCGDNIH1_1181.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABI62079 ; ABI62079 ; GbCGDNIH1_1181 .
GeneIDi 4274672.
KEGGi gbe:GbCGDNIH1_1181.
PATRICi 22078521. VBIGraBet83793_1230.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00187 .
BioCyci GBET391165:GHON-1215-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. "Genome sequence analysis of the emerging human pathogenic acetic acid bacterium Granulibacter bethesdensis."
    Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E., Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.
    J. Bacteriol. 189:8727-8736(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-1260 / CGDNIH1.

Entry informationi

Entry nameiENO_GRABC
AccessioniPrimary (citable) accession number: Q0BSX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: October 17, 2006
Last modified: November 26, 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3