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Protein

Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2

Gene

MFP2

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

Functioni

Involved in peroxisomal fatty acid beta-oxidation during seed germination. Possesses enoyl-CoA hydratase activity against long chain substrates (C14-C18) and 3-hydroxyacyl-CoA dehydrogenase activity against chains of variable sizes (C6-C18) (PubMed:10521521, PubMed:16507084, PubMed:20463021). Possesses 3-hydroxy-3-phenylpropionyl-CoA dehydrogenase activity and is involved in the peroxisomal beta-oxidation pathway for the biosynthesis of benzoic acid (BA). Required for the accumulation in seeds of substituted hydroxybenzoylated choline esters, which are BA-containing secondary metabolites (PubMed:24254312).4 Publications

Catalytic activityi

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.
(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.
(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.

Kineticsi

  1. KM=240 µM for crotonyl-CoA1 Publication

    Pathwayi: fatty acid beta-oxidation

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

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei119NucleophileSequence analysis1
    Active sitei139Proton acceptorSequence analysis1

    GO - Molecular functioni

    GO - Biological processi

    • fatty acid beta-oxidation Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase, Lyase, Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciARA:AT3G06860-MONOMER.
    MetaCyc:AT3G06860-MONOMER.
    ReactomeiR-ATH-390918. Peroxisomal lipid metabolism.
    UniPathwayiUPA00659.

    Chemistry databases

    SwissLipidsiSLP:000000867.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2
    Short name:
    AtMPF2
    Including the following 2 domains:
    Enoyl-CoA hydratase/3-2-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC:4.2.1.17, EC:5.1.2.3, EC:5.3.3.8)
    3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.35)
    Gene namesi
    Name:MFP2
    Ordered Locus Names:At3g06860
    ORF Names:F17A9.1
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 3

    Organism-specific databases

    TAIRiAT3G06860.

    Subcellular locationi

    GO - Cellular componenti

    • cell wall Source: TAIR
    • glyoxysome Source: UniProtKB-SubCell
    • nucleolus Source: TAIR
    • peroxisome Source: TAIR
    • plasmodesma Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Glyoxysome, Peroxisome

    Pathology & Biotechi

    Disruption phenotypei

    Accumulation of long-chain acyl-CoA substrates and increased size of peroxisomes.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004013711 – 725Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2Add BLAST725

    Proteomic databases

    PaxDbiQ9ZPI5.
    PRIDEiQ9ZPI5.

    PTM databases

    iPTMnetiQ9ZPI5.

    Expressioni

    Tissue specificityi

    Highly expressed in senescing leaves and at lower levels in flowers and siliques.1 Publication

    Developmental stagei

    Expression increases rapidly during seed germination to reach a peak at 2-3 days after imbibition (DAI) and then declines to basal levels at 5 DAI.1 Publication

    Gene expression databases

    GenevisibleiQ9ZPI5. AT.

    Interactioni

    Protein-protein interaction databases

    BioGridi5205. 1 interactor.
    STRINGi3702.AT3G06860.1.

    Structurei

    Secondary structure

    1725
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi8 – 13Combined sources6
    Beta strandi17 – 24Combined sources8
    Turni26 – 29Combined sources4
    Helixi33 – 46Combined sources14
    Beta strandi54 – 62Combined sources9
    Beta strandi85 – 87Combined sources3
    Helixi88 – 92Combined sources5
    Helixi93 – 99Combined sources7
    Beta strandi101 – 103Combined sources3
    Beta strandi105 – 109Combined sources5
    Beta strandi111 – 114Combined sources4
    Helixi116 – 123Combined sources8
    Beta strandi124 – 129Combined sources6
    Beta strandi134 – 136Combined sources3
    Helixi139 – 142Combined sources4
    Helixi150 – 158Combined sources9
    Helixi160 – 169Combined sources10
    Helixi175 – 180Combined sources6
    Beta strandi185 – 187Combined sources3
    Turni190 – 192Combined sources3
    Helixi193 – 205Combined sources13
    Helixi214 – 216Combined sources3
    Helixi224 – 241Combined sources18
    Helixi247 – 260Combined sources14
    Helixi263 – 277Combined sources15
    Helixi281 – 294Combined sources14
    Helixi295 – 297Combined sources3
    Turni300 – 302Combined sources3
    Beta strandi303 – 305Combined sources3
    Beta strandi315 – 318Combined sources4
    Helixi322 – 332Combined sources11
    Turni333 – 335Combined sources3
    Beta strandi338 – 341Combined sources4
    Helixi345 – 361Combined sources17
    Helixi372 – 375Combined sources4
    Turni376 – 378Combined sources3
    Beta strandi379 – 386Combined sources8
    Helixi387 – 389Combined sources3
    Beta strandi393 – 397Combined sources5
    Helixi403 – 416Combined sources14
    Beta strandi422 – 425Combined sources4
    Beta strandi428 – 430Combined sources3
    Helixi432 – 435Combined sources4
    Turni436 – 438Combined sources3
    Turni442 – 444Combined sources3
    Beta strandi445 – 450Combined sources6
    Turni454 – 456Combined sources3
    Beta strandi459 – 464Combined sources6
    Helixi470 – 482Combined sources13
    Beta strandi486 – 493Combined sources8
    Turni494 – 497Combined sources4
    Helixi498 – 514Combined sources17
    Helixi519 – 529Combined sources11
    Helixi535 – 542Combined sources8
    Helixi544 – 557Combined sources14
    Helixi559 – 561Combined sources3
    Helixi567 – 572Combined sources6
    Helixi605 – 610Combined sources6
    Turni618 – 621Combined sources4
    Helixi624 – 644Combined sources21
    Beta strandi647 – 649Combined sources3
    Helixi651 – 662Combined sources12
    Helixi666 – 668Combined sources3
    Helixi671 – 678Combined sources8
    Helixi680 – 694Combined sources15
    Helixi696 – 698Combined sources3
    Helixi702 – 710Combined sources9
    Beta strandi714 – 716Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2WTBX-ray2.50A1-725[»]
    DisProtiDP00654.
    ProteinModelPortaliQ9ZPI5.
    SMRiQ9ZPI5.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9ZPI5.

    Family & Domainsi

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi723 – 725Microbody targeting signalCurated3

    Domaini

    The epimerase and isomerase activities are contained in the N-terminal region while the dehydrogenase activity is in the C-terminal region.By similarity

    Sequence similaritiesi

    In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.Curated
    In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiKOG1683. Eukaryota.
    COG1024. LUCA.
    COG1250. LUCA.
    HOGENOMiHOG000261347.
    InParanoidiQ9ZPI5.
    KOiK10527.
    OMAiWALACHY.
    OrthoDBiEOG09360359.
    PhylomeDBiQ9ZPI5.

    Family and domain databases

    Gene3Di1.10.1040.10. 2 hits.
    3.40.50.720. 1 hit.
    3.90.226.10. 1 hit.
    InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
    IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
    IPR006108. 3HC_DH_C.
    IPR008927. 6-PGluconate_DH_C-like.
    IPR013328. 6PGD_dom_2.
    IPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00725. 3HCDH. 1 hit.
    PF02737. 3HCDH_N. 1 hit.
    PF00378. ECH_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF48179. SSF48179. 2 hits.
    SSF51735. SSF51735. 1 hit.
    SSF52096. SSF52096. 1 hit.
    PROSITEiPS00067. 3HCDH. 1 hit.
    PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9ZPI5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDSRTKGKTV MEVGGDGVAV ITLINPPVNS LSFDVLYNLK SNYEEALSRN
    60 70 80 90 100
    DVKAIVITGA KGRFSGGFDI SGFGEMQKGN VKEPKAGYIS IDIITDLLEA
    110 120 130 140 150
    ARKPSVAAID GLALGGGLEL AMACHARISA PAAQLGLPEL QLGVIPGFGG
    160 170 180 190 200
    TQRLPRLVGL TKALEMILTS KPVKAEEGHS LGLIDAVVPP AELVTTARRW
    210 220 230 240 250
    ALDIVGRRKP WVSSVSKTDK LPPLGEAREI LTFAKAQTLK RAPNMKHPLM
    260 270 280 290 300
    CLDAIEVGIV SGPRAGLEKE AEVASQVVKL DTTKGLIHVF FSQRGTAKVP
    310 320 330 340 350
    GVTDRGLVPR KIKKVAIIGG GLMGSGIATA LILSNYPVIL KEVNEKFLEA
    360 370 380 390 400
    GIGRVKANLQ SRVRKGSMSQ EKFEKTMSLL KGSLDYESFR DVDMVIEAVI
    410 420 430 440 450
    ENISLKQQIF ADLEKYCPQH CILASNTSTI DLNKIGERTK SQDRIVGAHF
    460 470 480 490 500
    FSPAHIMPLL EIVRTNHTSA QVIVDLLDVG KKIKKTPVVV GNCTGFAVNR
    510 520 530 540 550
    MFFPYTQAAM FLVECGADPY LIDRAISKFG MPMGPFRLCD LVGFGVAIAT
    560 570 580 590 600
    ATQFIENFSE RTYKSMIIPL MQEDKRAGEA TRKGFYLYDD KRKAKPDPEL
    610 620 630 640 650
    KKYIEKARSI SGVKLDPKLA NLSEKDIIEM TFFPVVNEAC RVFAEGIAVK
    660 670 680 690 700
    AADLDIAGIM GMGFPPYRGG IMFWADSIGS KYIYSRLDEW SKAYGEFFKP
    710 720
    CAFLAERGSK GVLLSAPVKQ ASSRL
    Length:725
    Mass (Da):78,840
    Last modified:May 1, 1999 - v1
    Checksum:iAB079FB354CB394C
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF123254 mRNA. Translation: AAD18042.1.
    AC016827 Genomic DNA. Translation: AAF26990.1.
    CP002686 Genomic DNA. Translation: AEE74468.1.
    AY062621 mRNA. Translation: AAL32699.1.
    RefSeqiNP_187342.1. NM_111566.4.
    UniGeneiAt.24386.

    Genome annotation databases

    EnsemblPlantsiAT3G06860.1; AT3G06860.1; AT3G06860.
    GeneIDi819870.
    GrameneiAT3G06860.1; AT3G06860.1; AT3G06860.
    KEGGiath:AT3G06860.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF123254 mRNA. Translation: AAD18042.1.
    AC016827 Genomic DNA. Translation: AAF26990.1.
    CP002686 Genomic DNA. Translation: AEE74468.1.
    AY062621 mRNA. Translation: AAL32699.1.
    RefSeqiNP_187342.1. NM_111566.4.
    UniGeneiAt.24386.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2WTBX-ray2.50A1-725[»]
    DisProtiDP00654.
    ProteinModelPortaliQ9ZPI5.
    SMRiQ9ZPI5.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi5205. 1 interactor.
    STRINGi3702.AT3G06860.1.

    Chemistry databases

    SwissLipidsiSLP:000000867.

    PTM databases

    iPTMnetiQ9ZPI5.

    Proteomic databases

    PaxDbiQ9ZPI5.
    PRIDEiQ9ZPI5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT3G06860.1; AT3G06860.1; AT3G06860.
    GeneIDi819870.
    GrameneiAT3G06860.1; AT3G06860.1; AT3G06860.
    KEGGiath:AT3G06860.

    Organism-specific databases

    TAIRiAT3G06860.

    Phylogenomic databases

    eggNOGiKOG1683. Eukaryota.
    COG1024. LUCA.
    COG1250. LUCA.
    HOGENOMiHOG000261347.
    InParanoidiQ9ZPI5.
    KOiK10527.
    OMAiWALACHY.
    OrthoDBiEOG09360359.
    PhylomeDBiQ9ZPI5.

    Enzyme and pathway databases

    UniPathwayiUPA00659.
    BioCyciARA:AT3G06860-MONOMER.
    MetaCyc:AT3G06860-MONOMER.
    ReactomeiR-ATH-390918. Peroxisomal lipid metabolism.

    Miscellaneous databases

    EvolutionaryTraceiQ9ZPI5.
    PROiQ9ZPI5.

    Gene expression databases

    GenevisibleiQ9ZPI5. AT.

    Family and domain databases

    Gene3Di1.10.1040.10. 2 hits.
    3.40.50.720. 1 hit.
    3.90.226.10. 1 hit.
    InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
    IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
    IPR006108. 3HC_DH_C.
    IPR008927. 6-PGluconate_DH_C-like.
    IPR013328. 6PGD_dom_2.
    IPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00725. 3HCDH. 1 hit.
    PF02737. 3HCDH_N. 1 hit.
    PF00378. ECH_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF48179. SSF48179. 2 hits.
    SSF51735. SSF51735. 1 hit.
    SSF52096. SSF52096. 1 hit.
    PROSITEiPS00067. 3HCDH. 1 hit.
    PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiMFP2_ARATH
    AccessioniPrimary (citable) accession number: Q9ZPI5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 30, 2010
    Last sequence update: May 1, 1999
    Last modified: November 30, 2016
    This is version 125 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

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    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 one 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.