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Reviewed, UniProtKB/Swiss-Prot Q9Y927 (ENO_AERPE)

Last modified November 25, 2008. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Enolase
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase
    2-phospho-D-glycerate hydro-lyase
Gene names
Name: eno
Ordered Locus Names: APE_2458
OrganismAeropyrum pernix [Complete proteome] [HAMAP]
Taxonomic identifier56636 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O.

Cofactor

Magnesium. Required for catalysis and for stabilizing the dimer By similarity.

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.

Pathway

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

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 archaeal cell surface By similarity.

Sequence similarities

Belongs to the enolase family.

Ontologies

Keywords

   Biological processGlycolysis
   Cellular componentCytoplasm
Secreted
   LigandMagnesium
Metal-binding
   Molecular functionLyase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processglycolysis

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcell surface

Inferred from electronic annotation. Source: HAMAP

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

phosphopyruvate hydratase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: HAMAP

phosphopyruvate hydratase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Enolase
PRO_0000134019

Regions

Region367 – 3704Substrate binding By similarity

Sites

Active site2101Proton donor By similarity
Active site3401Proton acceptor By similarity
Metal binding2471Magnesium By similarity
Metal binding2881Magnesium By similarity
Metal binding3151Magnesium By similarity
Binding site1581Substrate By similarity
Binding site1671Substrate By similarity
Binding site2881Substrate By similarity
Binding site3151Substrate By similarity
Binding site3401Substrate (covalent); in inhibited form By similarity
Binding site3911Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Y927-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 924E6362F8BDFDDE

FASTA43246,344
        10         20         30         40         50         60 
MGVNDFAIER VWGLQVLDSR GNPTVKAYVK LAGGSLGWGI APSGASRGER EAVELRDGGG 

        70         80         90        100        110        120 
KWRGKGVSRA VSLLNTVVAP RLEGVDARRQ AQIDRLLIEL DGTPNKSRLG GNTTTALSIA 

       130        140        150        160        170        180 
VSRAAAAQAR LELFQYLGGA GARRLPIPLL NVINGGVHAG NELDFQEFMI IPYGFESFTE 

       190        200        210        220        230        240 
AMRAAVETYG ELKSLLKDRY GASAVNVGDE GGFAPPMRSA EEALKTLVDA VEKAGYQPGS 

       250        260        270        280        290        300 
EIALGIDAAA SQLYSNGRYS VEGKSLSREE LLSLYQRLVE QYPIVYLEDP FSEDDYEGFK 

       310        320        330        340        350        360 
AAVDALSTET IIVGDDLLVT NPQRVKEASA LKAVTGLLVK VNQVGTLTEA LEAIQAARDR 

       370        380        390        400        410        420 
GIVHIVSHRS GDTEDTFIAD LAVATEALMI KTGAPARGER TSKYNRLLEI ENILGYSAEY 

       430 
AGPELRGVMG RR 

« Hide

References

[1]"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1."
Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. expand/collapse author list , Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.
DNA Res. 6:83-101(1999) [PubMed: 10382966] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K1.

Cross-references

Sequence databases

BA000002 Genomic DNA. Translation: BAA81473.1.
PIRA72477.
RefSeqNP_148623.1.

3D structure databases

HSSPHSSP built from PDB template 4ENL based on UniProtKB P00924.
ModBaseSearch...

Genome annotation databases

GeneID1445431.
GenomeReviewsGene locus APE_2458 in contig BA000002_GR.
KEGGape:APE_2458.
NMPDRfig|272557.1.peg.1731.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ9Y927.

Family and domain databases

HAMAPMF_00318.
[Tree]
InterProIPR000941. Enolase.
[Graphical view]
PANTHERPTHR11902. Enolase. 1 hit.
PfamPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF001400. Enolase. 1 hit.
PRINTSPR00148. ENOLASE.
ProDomPD000902. Enolase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01060. eno. 1 hit.
PROSITEPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameENO_AERPE
AccessionPrimary (citable) accession number: Q9Y927
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1999
Last modified: November 25, 2008
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents