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Q8WZM4

- ETR2_CANTR

UniProt

Q8WZM4 - ETR2_CANTR

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
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    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    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

    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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MYSVLKQSIR PRLLATHNQF RTMITAQAVL YTQHGEPKDV LFTQSFEIDD    50
    DNLAPNEVIV KTLGSPINPS DINQIQGVYP SKPAKTTGFG TAEPAAPCGN 100
    EGLFEVIKVG SNVSSLEAGD WVIPSHVNFG TWRTHALGND DDFIKLPNPA 150
    QSKANGKPNG LTINQGATIS VNPLTAYLML THYVKLTPGK DWFIQNGGTS 200
    AVGKYASQIG KLLNFNSISV IRDRPNLDEV VASLKELGAT QVITEDQNNS 250
    KEFGPTIKEW IKQSGGEAKL ALNCVGGKSS TGIARKLNNN GLMLTYGGMS 300
    FQPVTIPTSL YIFKNFTSAG FWVTELLKNN KELKTSTLNQ IIAWYEEGKL 350
    TDAKSIETLY DGTKPLHELY QDGVANSKDG KQLITY 386
    Length:386
    Mass (Da):42,117
    Last modified:March 1, 2002 - v1
    Checksum:i91ABE00831F0C2E8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U94996 Genomic DNA. Translation: AAL55471.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U94996 Genomic DNA. Translation: AAL55471.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 64 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