Skip Header

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

Enolase

Gene

ENO

Organism
Rhodotorula mucilaginosa (Yeast) (Rhodotorula rubra)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Mg2+ is required for catalysis and for stabilizing the dimer.By similarity

Pathwayi: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. Enolase (ENO)
  5. no protein annotated in this organism
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei160 – 1601SubstrateBy similarity
Binding sitei169 – 1691SubstrateBy similarity
Active sitei212 – 2121Proton donorBy similarity
Metal bindingi247 – 2471MagnesiumBy similarity
Metal bindingi296 – 2961MagnesiumBy similarity
Binding sitei296 – 2961SubstrateBy similarity
Metal bindingi323 – 3231MagnesiumBy similarity
Binding sitei323 – 3231SubstrateBy similarity
Active sitei348 – 3481Proton acceptorBy similarity
Binding sitei399 – 3991SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

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
Allergen: Rho m 1
Gene namesi
Name:ENO
OrganismiRhodotorula mucilaginosa (Yeast) (Rhodotorula rubra)
Taxonomic identifieri5537 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaPucciniomycotinaMicrobotryomycetesSporidiobolalesSporidiobolaceaeRhodotorula

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human. Binds to IgE.1 Publication

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei3465. Rho m 1.0101.
613. Rho m 1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 439439EnolasePRO_0000134057Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ870B9.
SMRiQ870B9. Positions 2-439.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni375 – 3784Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the enolase family.Curated

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.
SMARTiSM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q870B9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAISKIHSRY VYDSRGNPTV EVELTTEKGT FRSIVPSGAS TGVHEALELR
60 70 80 90 100
DGDKSKWLGK GVLKAVANVN DTIAPALIEA NIDVADQAKI DEFLLKLDGT
110 120 130 140 150
PNKAKLGANA ILGVSLAAAK AGAAQKDVPL YKHIADISKA KEGKFVLPVP
160 170 180 190 200
FQNVLNGGSH AGGDLAFQEF MIVPSGAPSF SEGLRIGSEV YHHLKSLTKK
210 220 230 240 250
KYGQSAGNVG DEGGVAPDIK TAKEALDLIV SAIEAAGYTG QVDIAMDVAS
260 270 280 290 300
SEFYKDGLYD LDFKNPNSDK SKWITGPQLA ELYEQLLNEY PIVSIEDPFA
310 320 330 340 350
EDDWEAWSHF FSKVEGKTQI VGDDLTVTNP IRIKKAIETK AADALLLKVN
360 370 380 390 400
QIGTLTESIQ AANDSYAAGW GVMVSHRSGE TEDTFIADLS VGIRSGQTKT
410 420 430
GAPARSERLA KLNQILRIEE ELGDKAIYAG KDFHKAHSL
Length:439
Mass (Da):47,140
Last modified:June 1, 2003 - v1
Checksum:i2C3DD18F63D33F34
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF382946 mRNA. Translation: AAP30720.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF382946 mRNA. Translation: AAP30720.1.

3D structure databases

ProteinModelPortaliQ870B9.
SMRiQ870B9. Positions 2-439.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei3465. Rho m 1.0101.
613. Rho m 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.

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.
SMARTiSM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of enolase allergen from Rhodotorula mucilaginosa."
    Chang C.-Y., Chou H., Tam M.F., Tang R.B., Lai H.-Y., Shen H.-D.
    J. Biomed. Sci. 9:645-655(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALLERGEN.

Entry informationi

Entry nameiENO_RHOMI
AccessioniPrimary (citable) accession number: Q870B9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: June 1, 2003
Last modified: May 11, 2016
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.