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Q757U3

- ETR1_ASHGO

UniProt

Q757U3 - ETR1_ASHGO

Protein

Probable trans-2-enoyl-CoA reductase, mitochondrial

Gene

ETR1

Organism
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 2 (09 Jan 2013)
      Previous versions | rss
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    Functioni

    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 By similarity.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei154 – 1541NADPBy similarity
    Binding sitei369 – 3691NADPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi182 – 1854NADPBy similarity
    Nucleotide bindingi205 – 2073NADPBy similarity
    Nucleotide bindingi280 – 2834NADPBy similarity
    Nucleotide bindingi305 – 3073NADPBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. aerobic respiration Source: EnsemblFungi
    2. fatty acid biosynthetic process Source: UniProtKB-KW

    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:
    Probable trans-2-enoyl-CoA reductase, mitochondrial (EC:1.3.1.38)
    Gene namesi
    Name:ETR1
    Ordered Locus Names:AEL081W
    OrganismiAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
    Taxonomic identifieri284811 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium
    ProteomesiUP000000591: Chromosome V

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 376Probable trans-2-enoyl-CoA reductase, mitochondrialPRO_0000000896
    Transit peptidei1 – ?MitochondrionSequence Analysis

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi33169.AGOS_AEL081W.

    Structurei

    3D structure databases

    ProteinModelPortaliQ757U3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0604.
    HOGENOMiHOG000294683.
    KOiK07512.
    OrthoDBiEOG7PS1RH.

    Family and domain databases

    Gene3Di3.40.50.720. 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.

    Q757U3-1 [UniParc]FASTAAdd to Basket

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    MQALNTTKRL MSTKQFPLFK SLLYSSHDPA DCTQVLKVHS YTPKVGADES    50
    ILLRTLAFPI NPSDINQLQG VYPSVPEKTL DYSTEKPAAI AGNEGVFEVM 100
    SVPQGERRLA VGDWVIPLYS NTGTWTNYQT CRDAGTLVKV NGLDLYTAAT 150
    IAVNGCTAYQ LVNDYVQWDP SGNEWIVQNA GTSAVSKIVT QVAQARGVKT 200
    LSVIRDRENF AEVAKELEER YGATKVISET QNNDKDFSKD ELPVILGPNA 250
    RVRLALNSVG GKSSGAIARK LERDGTMLTY GGMSRQPVTV PTTLLIFNGL 300
    KSLGYWITEN TKRNPQSKID TISALMRMYG DGQLQPPEAD IKKIEWDVQK 350
    MNDEQLLEAV KNGIQSNGKS VVVLKW 376
    Length:376
    Mass (Da):41,439
    Last modified:January 9, 2013 - v2
    Checksum:iA8F107B8CF1CEC7C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016818 Genomic DNA. Translation: AAS52604.2.
    RefSeqiNP_984780.2. NM_210134.2.

    Genome annotation databases

    GeneIDi4620970.
    KEGGiago:AGOS_AEL081W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016818 Genomic DNA. Translation: AAS52604.2 .
    RefSeqi NP_984780.2. NM_210134.2.

    3D structure databases

    ProteinModelPortali Q757U3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 33169.AGOS_AEL081W.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 4620970.
    KEGGi ago:AGOS_AEL081W.

    Phylogenomic databases

    eggNOGi COG0604.
    HOGENOMi HOG000294683.
    KOi K07512.
    OrthoDBi EOG7PS1RH.

    Family and domain databases

    Gene3Di 3.40.50.720. 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. "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
      Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
      Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
    2. "Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
      Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
      G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 324.
      Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

    Entry informationi

    Entry nameiETR1_ASHGO
    AccessioniPrimary (citable) accession number: Q757U3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: January 9, 2013
    Last modified: October 1, 2014
    This is version 74 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3