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Q8WZM4

- ETR2_CANTR

UniProt

Q8WZM4 - ETR2_CANTR

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Protein

Enoyl-[acyl-carrier-protein] reductase [NADPH, B-specific] 2, mitochondrial

Gene

ETR2

Organism
Candida tropicalis (Yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

An acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH.1 Publication
Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei172 – 1721NADP1 Publication
Binding sitei381 – 3811NADP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi199 – 2024NADP1 Publication
Nucleotide bindingi222 – 2243NADP1 Publication
Nucleotide bindingi296 – 2994NADP1 Publication
Nucleotide bindingi321 – 3233NADP1 Publication

GO - Molecular functioni

  1. enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity Source: UniProtKB-EC
  2. trans-2-enoyl-CoA reductase (NADPH) activity Source: UniProtKB
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
  2. fatty acid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Enoyl-[acyl-carrier-protein] reductase [NADPH, B-specific] 2, mitochondrial (EC:1.3.1.10)
Alternative name(s):
Trans-2-enoyl-CoA reductase 2 (EC:1.3.1.38)
Gene namesi
Name:ETR2
OrganismiCandida tropicalis (Yeast)
Taxonomic identifieri5482 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2222MitochondrionSequence AnalysisAdd
BLAST
Chaini23 – 386364Enoyl-[acyl-carrier-protein] reductase [NADPH, B-specific] 2, mitochondrialPRO_0000000899Add
BLAST

Expressioni

Inductioni

Up-regulated by growth on oleic acid.1 Publication

Interactioni

Subunit structurei

Homodimer and heterodimer with ETR1.1 Publication

Protein-protein interaction databases

IntActiQ8WZM4. 1 interaction.

Structurei

Secondary structure

1
386
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 3310Combined sources
Helixi37 – 404Combined sources
Beta strandi42 – 487Combined sources
Beta strandi57 – 6711Combined sources
Helixi69 – 768Combined sources
Beta strandi95 – 973Combined sources
Beta strandi103 – 1097Combined sources
Beta strandi121 – 1277Combined sources
Beta strandi132 – 1398Combined sources
Helixi140 – 1423Combined sources
Beta strandi143 – 1464Combined sources
Helixi149 – 1546Combined sources
Helixi163 – 1675Combined sources
Beta strandi169 – 1713Combined sources
Helixi172 – 18110Combined sources
Beta strandi182 – 1843Combined sources
Turni188 – 1903Combined sources
Beta strandi192 – 1965Combined sources
Helixi201 – 21313Combined sources
Beta strandi216 – 2216Combined sources
Helixi227 – 23711Combined sources
Beta strandi240 – 2445Combined sources
Helixi245 – 2495Combined sources
Turni251 – 2533Combined sources
Helixi254 – 26411Combined sources
Beta strandi268 – 2758Combined sources
Helixi277 – 2859Combined sources
Beta strandi292 – 2954Combined sources
Helixi299 – 3013Combined sources
Beta strandi304 – 3063Combined sources
Helixi308 – 3136Combined sources
Beta strandi317 – 3204Combined sources
Helixi323 – 3264Combined sources
Turni327 – 3293Combined sources
Helixi331 – 34616Combined sources
Beta strandi356 – 3594Combined sources
Beta strandi362 – 3643Combined sources
Helixi366 – 37510Combined sources
Helixi377 – 3793Combined sources
Beta strandi382 – 3854Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H0KX-ray2.11A/B23-386[»]
1N9GX-ray1.98A/C/F1-386[»]
ProteinModelPortaliQ8WZM4.
SMRiQ8WZM4. Positions 23-386.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8WZM4.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
SUPFAMiSSF50129. SSF50129. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8WZM4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYSVLKQSIR PRLLATHNQF RTMITAQAVL YTQHGEPKDV LFTQSFEIDD
60 70 80 90 100
DNLAPNEVIV KTLGSPINPS DINQIQGVYP SKPAKTTGFG TAEPAAPCGN
110 120 130 140 150
EGLFEVIKVG SNVSSLEAGD WVIPSHVNFG TWRTHALGND DDFIKLPNPA
160 170 180 190 200
QSKANGKPNG LTINQGATIS VNPLTAYLML THYVKLTPGK DWFIQNGGTS
210 220 230 240 250
AVGKYASQIG KLLNFNSISV IRDRPNLDEV VASLKELGAT QVITEDQNNS
260 270 280 290 300
KEFGPTIKEW IKQSGGEAKL ALNCVGGKSS TGIARKLNNN GLMLTYGGMS
310 320 330 340 350
FQPVTIPTSL YIFKNFTSAG FWVTELLKNN KELKTSTLNQ IIAWYEEGKL
360 370 380
TDAKSIETLY DGTKPLHELY QDGVANSKDG KQLITY
Length:386
Mass (Da):42,117
Last modified:March 1, 2002 - v1
Checksum:i91ABE00831F0C2E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94996 Genomic DNA. Translation: AAL55471.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94996 Genomic DNA. Translation: AAL55471.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1H0K X-ray 2.11 A/B 23-386 [» ]
1N9G X-ray 1.98 A/C/F 1-386 [» ]
ProteinModelPortali Q8WZM4.
SMRi Q8WZM4. Positions 23-386.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8WZM4. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q8WZM4.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProi IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR11695. PTHR11695. 1 hit.
SUPFAMi SSF50129. SSF50129. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH NADP, INDUCTION BY OLEIC ACID, CATALYTIC ACTIVITY.
    Strain: ATCC 20336 / pK233 / NCYC 997.
  2. "Crystal structure of enoyl thioester reductase 2."
    Airenne T.T., Torkko J.M., Hiltunen J.K.
    Submitted (JUN-2002) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS).

Entry informationi

Entry nameiETR2_CANTR
AccessioniPrimary (citable) accession number: Q8WZM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2002
Last modified: November 26, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3