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Q9ZPI5

- MFP2_ARATH

UniProt

Q9ZPI5 - MFP2_ARATH

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Protein
Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2
Gene
MFP2, At3g06860, F17A9.1
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei119 – 1191Nucleophile Reviewed prediction
Active sitei139 – 1391Proton acceptor Reviewed prediction

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
Complete GO annotation...

GO - Biological processi

  1. 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: Chromosome 3

Organism-specific databases

TAIRiAT3G06860.

Subcellular locationi

Glyoxysome Inferred. Peroxisome Inferred

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
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 MFP2
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiQ9ZPI5.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi723 – 7253Microbody targeting signal Reviewed prediction

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.
In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

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...

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

« 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: June 11, 2014
This is version 108 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

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