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Q8WZM3 (ETR1_CANTR) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Enoyl-[acyl-carrier-protein] reductase [NADPH, B-specific] 1, mitochondrial

EC=1.3.1.10
Alternative name(s):
Trans-2-enoyl-CoA reductase 1
EC=1.3.1.38
Gene names
Name:ETR1
OrganismCandida tropicalis (Yeast)
Taxonomic identifier5482 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for respiration and the maintenance of the mitochondrial compartment. Oxidoreductase with a preference for short and medium chain substrates, including trans-2-hexenoyl-CoA (C6), trans-2-decenoyl-CoA (C10), and trans-2-hexadecenoyl-CoA (C16). May play a role in mitochondrial fatty acid synthesis. Ref.1 Ref.2 Ref.3

Catalytic activity

An acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH. Ref.2

Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH. Ref.2

Subunit structure

Homodimer and heterodimer with etr2. Ref.1 Ref.2

Subcellular location

Mitochondrion Ref.1.

Induction

Up-regulated by growth on oleic acid. Ref.2

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2222Mitochondrion Ref.1
Chain23 – 386364Enoyl-[acyl-carrier-protein] reductase [NADPH, B-specific] 1, mitochondrial
PRO_0000000898

Regions

Nucleotide binding199 – 2024NADP
Nucleotide binding222 – 2243NADP
Nucleotide binding296 – 2994NADP
Nucleotide binding321 – 3233NADP

Sites

Binding site1721NADP
Binding site3811NADP

Experimental info

Mutagenesis791Y → N: 0.1% of catalytic activity. Ref.3

Secondary structure

......................................................................... 386
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8WZM3 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: FCBC174A240742D8

FASTA38642,161
        10         20         30         40         50         60 
MYSVLKQSIR PRLLATHNQF RTMITAQAVL YTQHGEPKDV LFTQSFEIDD DNLAPNEVIV 

        70         80         90        100        110        120 
KTLGSPVNPS DINQIQGVYP SKPAKTTGFG TTEPAAPCGN EGLFEVIKVG SNVSSLEAGD 

       130        140        150        160        170        180 
WVIPSHVNFG TWRTHALGND DDFIKLPNPA QSKANGKPNG LTINQGATIS VNPLTAYLML 

       190        200        210        220        230        240 
THYVKLTPGK DWFIQNGGTS AVGKYASQIG KLLNFNSISV IRDRPNLDEV VASLKELGAT 

       250        260        270        280        290        300 
QVITEDQNNS REFGPTIKEW IKQSGGEAKL ALNCVGGKSS TGIARKLNNN GLMLTYGGMS 

       310        320        330        340        350        360 
FQPVTIPTSL YIFKNFTSAG FWVTELLKNN KELKTSTLNQ IIAWYEEGKL TDAKSIETLY 

       370        380 
DGTKPLHELY QDGVANSKDG KQLITY 

« Hide

References

[1]"Candida tropicalis Etr1p and Saccharomyces cerevisiae Ybr026p (Mrf1'p), 2-enoyl thioester reductases essential for mitochondrial respiratory competence."
Torkko J.M., Koivuranta K.T., Miinalainen I.J., Yagi A.I., Schmitz W., Kastaniotis A.J., Airenne T.T., Gurvitz A., Hiltunen K.J.
Mol. Cell. Biol. 21:6243-6253(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-29, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
Strain: ATCC 20336 / pK233 / NCYC 997.
[2]"Candida tropicalis expresses two mitochondrial 2-enoyl thioester reductases that are able to form both homodimers and heterodimers."
Torkko J.M., Koivuranta K.T., Kastaniotis A.J., Airenne T.T., Glumoff T., Ilves M., Hartig A., Gurvitz A., Hiltunen J.K.
J. Biol. Chem. 278:41213-41220(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT, INDUCTION BY OLEIC ACID, CATALYTIC ACTIVITY, FUNCTION.
Strain: ATCC 20336 / pK233 / NCYC 997.
[3]"Structure-function analysis of enoyl thioester reductase involved in mitochondrial maintenance."
Airenne T.T., Torkko J.M., Van den plas S., Sormunen R.T., Kastaniotis A.J., Wierenga R.K., Hiltunen J.K.
J. Mol. Biol. 327:47-59(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH NADP, MUTAGENESIS OF TYR-79, FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U94997 Genomic DNA. Translation: AAL55472.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GU7X-ray1.70A/B23-386[»]
1GUFX-ray2.25A/B23-386[»]
1GYRX-ray2.60A/B/C23-386[»]
1N9GX-ray1.98B/D/E1-386[»]
ProteinModelPortalQ8WZM3.
SMRQ8WZM3. Positions 23-386.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8WZM3. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProIPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11695. PTHR11695. 1 hit.
SUPFAMSSF50129. SSF50129. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ8WZM3.

Entry information

Entry nameETR1_CANTR
AccessionPrimary (citable) accession number: Q8WZM3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2002
Last modified: March 19, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references