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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).3 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

    Pathway:ifatty 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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei119 – 1191NucleophileSequence Analysis
    Active sitei139 – 1391Proton acceptorSequence Analysis

    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.
    UniPathwayiUPA00659.

    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
    ProteomesiUP000006548 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)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 725725Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2PRO_0000401371Add
    BLAST

    Proteomic databases

    PaxDbiQ9ZPI5.
    PRIDEiQ9ZPI5.

    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

    Interactioni

    Protein-protein interaction databases

    BioGridi5205. 1 interaction.
    STRINGi3702.AT3G06860.1.

    Structurei

    Secondary structure

    1
    725
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 136Combined sources
    Beta strandi17 – 248Combined sources
    Turni26 – 294Combined sources
    Helixi33 – 4614Combined sources
    Beta strandi54 – 629Combined sources
    Beta strandi85 – 873Combined sources
    Helixi88 – 925Combined sources
    Helixi93 – 997Combined sources
    Beta strandi101 – 1033Combined sources
    Beta strandi105 – 1095Combined sources
    Beta strandi111 – 1144Combined sources
    Helixi116 – 1238Combined sources
    Beta strandi124 – 1296Combined sources
    Beta strandi134 – 1363Combined sources
    Helixi139 – 1424Combined sources
    Helixi150 – 1589Combined sources
    Helixi160 – 16910Combined sources
    Helixi175 – 1806Combined sources
    Beta strandi185 – 1873Combined sources
    Turni190 – 1923Combined sources
    Helixi193 – 20513Combined sources
    Helixi214 – 2163Combined sources
    Helixi224 – 24118Combined sources
    Helixi247 – 26014Combined sources
    Helixi263 – 27715Combined sources
    Helixi281 – 29414Combined sources
    Helixi295 – 2973Combined sources
    Turni300 – 3023Combined sources
    Beta strandi303 – 3053Combined sources
    Beta strandi315 – 3184Combined sources
    Helixi322 – 33211Combined sources
    Turni333 – 3353Combined sources
    Beta strandi338 – 3414Combined sources
    Helixi345 – 36117Combined sources
    Helixi372 – 3754Combined sources
    Turni376 – 3783Combined sources
    Beta strandi379 – 3868Combined sources
    Helixi387 – 3893Combined sources
    Beta strandi393 – 3975Combined sources
    Helixi403 – 41614Combined sources
    Beta strandi422 – 4254Combined sources
    Beta strandi428 – 4303Combined sources
    Helixi432 – 4354Combined sources
    Turni436 – 4383Combined sources
    Turni442 – 4443Combined sources
    Beta strandi445 – 4506Combined sources
    Turni454 – 4563Combined sources
    Beta strandi459 – 4646Combined sources
    Helixi470 – 48213Combined sources
    Beta strandi486 – 4938Combined sources
    Turni494 – 4974Combined sources
    Helixi498 – 51417Combined sources
    Helixi519 – 52911Combined sources
    Helixi535 – 5428Combined sources
    Helixi544 – 55714Combined sources
    Helixi559 – 5613Combined sources
    Helixi567 – 5726Combined sources
    Helixi605 – 6106Combined sources
    Turni618 – 6214Combined sources
    Helixi624 – 64421Combined sources
    Beta strandi647 – 6493Combined sources
    Helixi651 – 66212Combined sources
    Helixi666 – 6683Combined sources
    Helixi671 – 6788Combined sources
    Helixi680 – 69415Combined sources
    Helixi696 – 6983Combined sources
    Helixi702 – 7109Combined sources
    Beta strandi714 – 7163Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WTBX-ray2.50A1-725[»]
    DisProtiDP00654.
    ProteinModelPortaliQ9ZPI5.
    SMRiQ9ZPI5. Positions 7-719.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9ZPI5.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi723 – 7253Microbody targeting signalSequence Analysis

    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

    eggNOGiCOG1250.
    HOGENOMiHOG000261347.
    InParanoidiQ9ZPI5.
    KOiK10527.
    OMAiLEWALAC.
    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 hit.
    [Graphical view]
    SUPFAMiSSF48179. SSF48179. 2 hits.
    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_111566.3.
    UniGeneiAt.24386.

    Genome annotation databases

    EnsemblPlantsiAT3G06860.1; AT3G06860.1; AT3G06860.
    GeneIDi819870.
    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_111566.3.
    UniGeneiAt.24386.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WTBX-ray2.50A1-725[»]
    DisProtiDP00654.
    ProteinModelPortaliQ9ZPI5.
    SMRiQ9ZPI5. Positions 7-719.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi5205. 1 interaction.
    STRINGi3702.AT3G06860.1.

    Proteomic databases

    PaxDbiQ9ZPI5.
    PRIDEiQ9ZPI5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    TAIRiAT3G06860.

    Phylogenomic databases

    eggNOGiCOG1250.
    HOGENOMiHOG000261347.
    InParanoidiQ9ZPI5.
    KOiK10527.
    OMAiLEWALAC.
    PhylomeDBiQ9ZPI5.

    Enzyme and pathway databases

    UniPathwayiUPA00659.
    BioCyciARA:AT3G06860-MONOMER.
    MetaCyc:AT3G06860-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiQ9ZPI5.
    PROiQ9ZPI5.

    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 hit.
    [Graphical view]
    SUPFAMiSSF48179. SSF48179. 2 hits.
    SSF52096. SSF52096. 1 hit.
    PROSITEiPS00067. 3HCDH. 1 hit.
    PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "A defect in beta-oxidation causes abnormal inflorescence development in Arabidopsis."
      Richmond T.A., Bleecker A.B.
      Plant Cell 11:1911-1924(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
      Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
      , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "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.
    5. "The multifunctional protein AtMFP2 is co-ordinately expressed with other genes of fatty acid beta-oxidation during seed germination in Arabidopsis thaliana (L.) Heynh."
      Eastmond P.J., Graham I.A.
      Biochem. Soc. Trans. 28:95-99(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    6. "The Arabidopsis thaliana multifunctional protein gene (MFP2) of peroxisomal beta-oxidation is essential for seedling establishment."
      Rylott E.L., Eastmond P.J., Gilday A.D., Slocombe S.P., Larson T.R., Baker A., Graham I.A.
      Plant J. 45:930-941(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    7. "The multifunctional protein in peroxisomal beta-oxidation: structure and substrate specificity of the Arabidopsis thaliana protein MFP2."
      Arent S., Christensen C.E., Pye V.E., Noergaard A., Henriksen A.
      J. Biol. Chem. 285:24066-24077(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION.

    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: July 22, 2015
    This is version 116 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

    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.