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Q9ZPI5

- MFP2_ARATH

UniProt

Q9ZPI5 - MFP2_ARATH

Protein

Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2

Gene

MFP2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei119 – 1191NucleophileSequence Analysis
    Active sitei139 – 1391Proton acceptorSequence Analysis

    GO - Molecular functioni

    1. 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB
    2. 3-hydroxybutyryl-CoA epimerase activity Source: UniProtKB-EC
    3. coenzyme binding Source: InterPro
    4. dodecenoyl-CoA delta-isomerase activity Source: UniProtKB-EC
    5. enoyl-CoA hydratase activity Source: UniProtKB-EC
    6. long-chain-enoyl-CoA hydratase activity Source: UniProtKB

    GO - Biological processi

    1. fatty acid beta-oxidation Source: TAIR

    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: Chromosome 3

    Organism-specific databases

    TAIRiAT3G06860.

    Subcellular locationi

    Glyoxysome Curated. Peroxisome Curated

    GO - Cellular componenti

    1. cell wall Source: TAIR
    2. glyoxysome Source: UniProtKB-SubCell
    3. nucleolus Source: TAIR
    4. peroxisome Source: TAIR
    5. plasmodesma Source: TAIR

    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

    Gene expression databases

    ArrayExpressiQ9ZPI5.
    GenevestigatoriQ9ZPI5.

    Interactioni

    Protein-protein interaction databases

    BioGridi5205. 1 interaction.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiFFKPCSY.
    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.
    IPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    IPR013328. DH_multihelical.
    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

    MDSRTKGKTV MEVGGDGVAV ITLINPPVNS LSFDVLYNLK SNYEEALSRN    50
    DVKAIVITGA KGRFSGGFDI SGFGEMQKGN VKEPKAGYIS IDIITDLLEA 100
    ARKPSVAAID GLALGGGLEL AMACHARISA PAAQLGLPEL QLGVIPGFGG 150
    TQRLPRLVGL TKALEMILTS KPVKAEEGHS LGLIDAVVPP AELVTTARRW 200
    ALDIVGRRKP WVSSVSKTDK LPPLGEAREI LTFAKAQTLK RAPNMKHPLM 250
    CLDAIEVGIV SGPRAGLEKE AEVASQVVKL DTTKGLIHVF FSQRGTAKVP 300
    GVTDRGLVPR KIKKVAIIGG GLMGSGIATA LILSNYPVIL KEVNEKFLEA 350
    GIGRVKANLQ SRVRKGSMSQ EKFEKTMSLL KGSLDYESFR DVDMVIEAVI 400
    ENISLKQQIF ADLEKYCPQH CILASNTSTI DLNKIGERTK SQDRIVGAHF 450
    FSPAHIMPLL EIVRTNHTSA QVIVDLLDVG KKIKKTPVVV GNCTGFAVNR 500
    MFFPYTQAAM FLVECGADPY LIDRAISKFG MPMGPFRLCD LVGFGVAIAT 550
    ATQFIENFSE RTYKSMIIPL MQEDKRAGEA TRKGFYLYDD KRKAKPDPEL 600
    KKYIEKARSI SGVKLDPKLA NLSEKDIIEM TFFPVVNEAC RVFAEGIAVK 650
    AADLDIAGIM GMGFPPYRGG IMFWADSIGS KYIYSRLDEW SKAYGEFFKP 700
    CAFLAERGSK GVLLSAPVKQ ASSRL 725
    Length:725
    Mass (Da):78,840
    Last modified:May 1, 1999 - v1
    Checksum:iAB079FB354CB394C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF123254 mRNA. Translation: AAD18042.1 .
    AC016827 Genomic DNA. Translation: AAF26990.1 .
    CP002686 Genomic DNA. Translation: AEE74468.1 .
    AY062621 mRNA. Translation: AAL32699.1 .
    RefSeqi NP_187342.1. NM_111566.3.
    UniGenei At.24386.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WTB X-ray 2.50 A 1-725 [» ]
    DisProti DP00654.
    ProteinModelPortali Q9ZPI5.
    SMRi Q9ZPI5. Positions 7-719.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 5205. 1 interaction.

    Proteomic databases

    PaxDbi Q9ZPI5.
    PRIDEi Q9ZPI5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G06860.1 ; AT3G06860.1 ; AT3G06860 .
    GeneIDi 819870.
    KEGGi ath:AT3G06860.

    Organism-specific databases

    TAIRi AT3G06860.

    Phylogenomic databases

    eggNOGi COG1250.
    HOGENOMi HOG000261347.
    InParanoidi Q9ZPI5.
    KOi K10527.
    OMAi FFKPCSY.
    PhylomeDBi Q9ZPI5.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci ARA:AT3G06860-MONOMER.
    MetaCyc:AT3G06860-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q9ZPI5.

    Gene expression databases

    ArrayExpressi Q9ZPI5.
    Genevestigatori Q9ZPI5.

    Family and domain databases

    Gene3Di 1.10.1040.10. 2 hits.
    3.40.50.720. 1 hit.
    3.90.226.10. 1 hit.
    InterProi IPR006180. 3-OHacyl-CoA_DH_CS.
    IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
    IPR006108. 3HC_DH_C.
    IPR008927. 6-PGluconate_DH_C-like.
    IPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    IPR013328. DH_multihelical.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00725. 3HCDH. 1 hit.
    PF02737. 3HCDH_N. 1 hit.
    PF00378. ECH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48179. SSF48179. 2 hits.
    SSF52096. SSF52096. 1 hit.
    PROSITEi PS00067. 3HCDH. 1 hit.
    PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 109 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