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Protein

Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplastic

Gene

MOD1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NAD-dependent reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Catalyzes the last reduction step in the de novo synthesis cycle of fatty acids. Involved in the elongation cycle of fatty acids which are used in lipid metabolism. Required for normal plant growth.2 Publications

Catalytic activityi

An acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.

Enzyme regulationi

Inhibited by the phytotoxin cyperin and the synthetic antimicrobial compound triclosan.1 Publication

Kineticsi

  1. KM=288 µM for crotonyl-CoA1 Publication

    Pathway:ifatty acid biosynthesis

    This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
    View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei101 – 1011NAD; via carbonyl oxygenBy similarity
    Binding sitei108 – 1081NADBy similarity
    Binding sitei262 – 2621NAD; via carbonyl oxygenBy similarity
    Active sitei264 – 2641Proton acceptorBy similarity
    Active sitei274 – 2741Proton acceptorBy similarity
    Binding sitei282 – 2821NADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi165 – 1662NADBy similarity
    Nucleotide bindingi212 – 2132NADBy similarity
    Nucleotide bindingi312 – 3165NADBy similarity

    GO - Molecular functioni

    • copper ion binding Source: TAIR
    • enoyl-[acyl-carrier-protein] reductase (NADH) activity Source: UniProtKB-EC
    • enoyl-[acyl-carrier-protein] reductase activity Source: TAIR

    GO - Biological processi

    • fatty acid biosynthetic process Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

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

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciARA:AT2G05990-MONOMER.
    ARA:GQT-2200-MONOMER.
    UniPathwayiUPA00094.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplastic (EC:1.3.1.9)
    Short name:
    ENR
    Alternative name(s):
    NADH-dependent enoyl-ACP reductase 1
    Protein MOSAIC DEATH 1
    Gene namesi
    Name:MOD1
    Synonyms:ENR-A, ENR1
    Ordered Locus Names:At2g05990
    ORF Names:T6P5.19
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548 Componenti: Chromosome 2

    Organism-specific databases

    TAIRiAT2G05990.

    Subcellular locationi

    GO - Cellular componenti

    • chloroplast Source: TAIR
    • chloroplast envelope Source: TAIR
    • chloroplast stroma Source: TAIR
    • fatty acid synthase complex Source: TAIR
    • thylakoid Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Plastid

    Pathology & Biotechi

    Disruption phenotypei

    Premature cell death in several organs, chlorotic and curly leaves, semidwarfism, distorted siliques, premature senescence of primary inflorescences, reduced fertility and decrease in total lipid content.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi226 – 2261T → I: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 7474ChloroplastSequence AnalysisAdd
    BLAST
    Chaini75 – 390316Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplasticPRO_0000420278Add
    BLAST

    Proteomic databases

    PRIDEiQ9SLA8.
    ProMEXiQ9SLA8.

    Expressioni

    Tissue specificityi

    Expressed in flowers and siliques and at lower levels in roots and leaves (at protein level).2 Publications

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    BioGridi551. 1 interaction.
    IntActiQ9SLA8. 1 interaction.
    STRINGi3702.AT2G05990.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SLA8.
    SMRiQ9SLA8. Positions 87-383.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    InParanoidiQ9SLA8.
    KOiK00208.
    OMAiDQSIAWG.
    PhylomeDBiQ9SLA8.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.

    Sequencei

    Sequence statusi: Complete.

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

    Q9SLA8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAATAASSLQ IATRRPSMSS PSKILKAGTY IVGANPGNAS WDKLSCTRQL
    60 70 80 90 100
    SNLGCLRNHS AVPTCKRPFS FSTRAMSESS ENKAPSGLPI DLRGKRAFIA
    110 120 130 140 150
    GIADDNGYGW AIAKSLAAAG AEILVGTWVP ALNIFETSLR RGKFDQSRVL
    160 170 180 190 200
    PDGSLMEIKK VYALDAVFDN PEDVPEDVKT NKRYAGSSNW TVQEAAECVK
    210 220 230 240 250
    KDFGSIDILV HSLANGPEVS KPLLETSRKG YLAAISASSY SFVSLLRHFL
    260 270 280 290 300
    PIMNPGGASI SLTYIASERI IPGYGGGMSS AKAALESDTR VLAYEAGRKS
    310 320 330 340 350
    NIRVNTISAG PLGSRAAKAI GFIDTMIEYS YNNGPIQKTL TADEVGNAAA
    360 370 380 390
    FLASPLASAI TGATIYVDNG LNAMGVALDS PVFKDLNSKN
    Length:390
    Mass (Da):41,214
    Last modified:May 1, 2000 - v1
    Checksum:i95E549A6E64BE5BC
    GO

    Sequence cautioni

    The sequence AAG40070.1 differs from that shown. Reason: Frameshift at position 150. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 241I → V in CAA74175 (PubMed:10380806).Curated
    Sequence conflicti35 – 351N → Y in CAA74175 (PubMed:10380806).Curated
    Sequence conflicti59 – 602HS → NT in CAA74175 (PubMed:10380806).Curated
    Sequence conflicti234 – 2341A → V in CAA74175 (PubMed:10380806).Curated
    Sequence conflicti376 – 3761V → R in AAF37208 (PubMed:10380806).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y13860 Genomic DNA. Translation: CAA74175.1.
    AF207593 mRNA. Translation: AAF37208.1.
    AC005970 Genomic DNA. Translation: AAC95176.1.
    CP002685 Genomic DNA. Translation: AEC05988.1.
    CP002685 Genomic DNA. Translation: AEC05989.1.
    AF324719 mRNA. Translation: AAG40070.1. Frameshift.
    AY056192 mRNA. Translation: AAL07041.1.
    AY113962 mRNA. Translation: AAM45010.1.
    PIRiH84473.
    RefSeqiNP_565331.1. NM_126612.2.
    NP_849940.1. NM_179609.1.
    UniGeneiAt.23842.

    Genome annotation databases

    EnsemblPlantsiAT2G05990.1; AT2G05990.1; AT2G05990.
    AT2G05990.2; AT2G05990.2; AT2G05990.
    GeneIDi815152.
    KEGGiath:AT2G05990.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y13860 Genomic DNA. Translation: CAA74175.1.
    AF207593 mRNA. Translation: AAF37208.1.
    AC005970 Genomic DNA. Translation: AAC95176.1.
    CP002685 Genomic DNA. Translation: AEC05988.1.
    CP002685 Genomic DNA. Translation: AEC05989.1.
    AF324719 mRNA. Translation: AAG40070.1. Frameshift.
    AY056192 mRNA. Translation: AAL07041.1.
    AY113962 mRNA. Translation: AAM45010.1.
    PIRiH84473.
    RefSeqiNP_565331.1. NM_126612.2.
    NP_849940.1. NM_179609.1.
    UniGeneiAt.23842.

    3D structure databases

    ProteinModelPortaliQ9SLA8.
    SMRiQ9SLA8. Positions 87-383.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi551. 1 interaction.
    IntActiQ9SLA8. 1 interaction.
    STRINGi3702.AT2G05990.1.

    Proteomic databases

    PRIDEiQ9SLA8.
    ProMEXiQ9SLA8.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT2G05990.1; AT2G05990.1; AT2G05990.
    AT2G05990.2; AT2G05990.2; AT2G05990.
    GeneIDi815152.
    KEGGiath:AT2G05990.

    Organism-specific databases

    TAIRiAT2G05990.

    Phylogenomic databases

    InParanoidiQ9SLA8.
    KOiK00208.
    OMAiDQSIAWG.
    PhylomeDBiQ9SLA8.

    Enzyme and pathway databases

    UniPathwayiUPA00094.
    BioCyciARA:AT2G05990-MONOMER.
    ARA:GQT-2200-MONOMER.

    Miscellaneous databases

    PROiQ9SLA8.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Sequences surrounding the transcription initiation site of the Arabidopsis enoyl-acyl carrier protein reductase gene control seed expression in transgenic tobacco."
      de Boer G.J., Testerink C., Pielage G., Nijkamp H.J., Stuitje A.R.
      Plant Mol. Biol. 39:1197-1207(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
      Strain: cv. Landsberg erecta.
    2. "Deficiency in fatty acid synthase leads to premature cell death and dramatic alterations in plant morphology."
      Mou Z., He Y., Dai Y., Liu X., Li J.
      Plant Cell 12:405-418(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF THR-226.
      Strain: cv. Columbia.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    6. "A pathogenic fungi diphenyl ether phytotoxin targets plant enoyl (acyl carrier protein) reductase."
      Dayan F.E., Ferreira D., Wang Y.H., Khan I.A., McInroy J.A., Pan Z.
      Plant Physiol. 147:1062-1071(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiFABI_ARATH
    AccessioniPrimary (citable) accession number: Q9SLA8
    Secondary accession number(s): O04942, Q9FEF2, Q9M672
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2012
    Last sequence update: May 1, 2000
    Last modified: June 24, 2015
    This is version 106 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.