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D0J9G5 (D0J9G5_BLASP) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis By similarity. HAMAP-Rule MF_00318

Catalytic activity

2-phospho-D-glycerate = phosphoenolpyruvate + H2O. HAMAP-Rule MF_00318

Cofactor

Magnesium. Required for catalysis and for stabilizing the dimer By similarity. HAMAP-Rule MF_00318

Enzyme regulation

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. HAMAP-Rule MF_00318

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. HAMAP-Rule MF_00318

Subcellular location

Cytoplasm. Secreted. Cell surface. 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. HAMAP-Rule MF_00318

Sequence similarities

Belongs to the enolase family. HAMAP-Rule MF_00318

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region369 – 3724Substrate binding By similarity HAMAP-Rule MF_00318 PIRSR PIRSR001400-2

Sites

Active site2041Proton donor By similarity HAMAP-Rule MF_00318 PIRSR PIRSR001400-1
Active site3421Proton acceptor By similarity HAMAP-Rule MF_00318 PIRSR PIRSR001400-1
Metal binding2411Magnesium By similarity HAMAP-Rule MF_00318
Metal binding2901Magnesium By similarity HAMAP-Rule MF_00318
Metal binding3171Magnesium By similarity HAMAP-Rule MF_00318
Binding site1541Substrate By similarity HAMAP-Rule MF_00318 PIRSR PIRSR001400-2
Binding site1631Substrate By similarity HAMAP-Rule MF_00318 PIRSR PIRSR001400-2
Binding site2901Substrate By similarity HAMAP-Rule MF_00318 PIRSR PIRSR001400-2
Binding site3171Substrate By similarity HAMAP-Rule MF_00318 PIRSR PIRSR001400-2
Binding site3421Substrate (covalent); in inhibited form By similarity HAMAP-Rule MF_00318
Binding site3931Substrate By similarity HAMAP-Rule MF_00318 PIRSR PIRSR001400-2

Amino acid modifications

Modified residue2841Phosphotyrosine By similarity HAMAP-Rule MF_00318

Sequences

Sequence LengthMass (Da)Tools
D0J9G5 [UniParc].

Last modified December 15, 2009. Version 1.
Checksum: 18E2F2EED017663E

FASTA42747,443
        10         20         30         40         50         60 
MSKIKTIKAR QILDSRGNPT VEVDVVTEKN VLGRASVPSG ASKGENEAFE LRDGGEKFLG 

        70         80         90        100        110        120 
NGVMKAVHNV NNIIAPELIG FSVMDQISID KLILDLDGTK NKKRLGANAI LGVSLAVVKA 

       130        140        150        160        170        180 
ASKELNLPLY KYIGGVHAHI LPIPLMNIVN GGRHSDAPIA FQEFMIVPMR ANTFLDAIQM 

       190        200        210        220        230        240 
GYKVFYKLKN ILSKKGLSTN VGDEGGFSSN FNGIEDVLDN ILEAIHQANY EPYEQIGLAL 

       250        260        270        280        290        300 
DCAASEFYQD EKYNYSKFEK ENKEKVERSK EEHVNYLSYL TRRYPIISIE DGMDQNDWEG 

       310        320        330        340        350        360 
WKMLTRELGK EVLLVGDDLF VTKVEKLNEG IKEGIANSIL IKVNQVGTLT ETIATINTGK 

       370        380        390        400        410        420 
ENGYCNIISH RSGDTEDSFI ADLSVALNIG RIKTGSICRS ERTSKYNQLL RIEDMLGKNS 


HYPEWTG

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References

[1]"Nitrogen recycling and nutritional provisioning by Blattabacterium, the cockroach endosymbiont."
Sabree Z.L., Kambhampati S., Moran N.A.
Proc. Natl. Acad. Sci. U.S.A. 106:19521-19526(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BPLAN EMBL ACX83986.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001429 Genomic DNA. Translation: ACX83986.1.
RefSeqYP_003257129.1. NC_013418.2.

3D structure databases

ProteinModelPortalD0J9G5.
ModBaseSearch...

Protein-protein interaction databases

STRING600809.BPLAN_372.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACX83986; ACX83986; BPLAN_372.
GeneID8528103.
KEGGbpi:BPLAN_372.
PATRIC31960689. VBIBlaSp127104_0376.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0148.
HOGENOMHOG000072174.
KOK01689.
OMAEYMIMPL.

Enzyme and pathway databases

BioCycBSP600809:GHSF-375-MONOMER.
UniPathwayUPA00109; UER00187.

Family and domain databases

HAMAPMF_00318. Enolase.
InterProIPR000941. Enolase.
IPR020810. Enolase_C.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
[Graphical view]
PANTHERPTHR11902. PTHR11902. 1 hit.
PfamPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF001400. Enolase. 1 hit.
PRINTSPR00148. ENOLASE.
TIGRFAMsTIGR01060. eno. 1 hit.
PROSITEPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD0J9G5_BLASP
AccessionPrimary (citable) accession number: D0J9G5
Entry history
Integrated into UniProtKB/TrEMBL: December 15, 2009
Last sequence update: December 15, 2009
Last modified: May 1, 2013
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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