Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9ZPI5 (MFP2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2

Short name=AtMPF2

Including the following 2 domains:

  1. 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
  2. 3-hydroxyacyl-CoA dehydrogenase
    EC=1.1.1.35
Gene names
Name:MFP2
Ordered Locus Names:At3g06860
ORF Names:F17A9.1
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length725 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.1 Ref.6 Ref.7

Catalytic activity

(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.

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subcellular location

Glyoxysome Probable. Peroxisome Probable.

Tissue specificity

Highly expressed in senescing leaves and at lower levels in flowers and siliques. Ref.5

Developmental stage

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. Ref.5

Domain

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

Disruption phenotype

Accumulation of long-chain acyl-CoA substrates and increased size of peroxisomes. Ref.6

Sequence similarities

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.

Biophysicochemical properties

Kinetic parameters:

KM=240 µM for crotonyl-CoA Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 725725Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2
PRO_0000401371

Regions

Motif723 – 7253Microbody targeting signal Potential

Sites

Active site1191Nucleophile Potential
Active site1391Proton acceptor Potential

Secondary structure

........................................................................................................................... 725
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9ZPI5 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: AB079FB354CB394C

FASTA72578,840
        10         20         30         40         50         60 
MDSRTKGKTV MEVGGDGVAV ITLINPPVNS LSFDVLYNLK SNYEEALSRN DVKAIVITGA 

        70         80         90        100        110        120 
KGRFSGGFDI SGFGEMQKGN VKEPKAGYIS IDIITDLLEA ARKPSVAAID GLALGGGLEL 

       130        140        150        160        170        180 
AMACHARISA PAAQLGLPEL QLGVIPGFGG TQRLPRLVGL TKALEMILTS KPVKAEEGHS 

       190        200        210        220        230        240 
LGLIDAVVPP AELVTTARRW ALDIVGRRKP WVSSVSKTDK LPPLGEAREI LTFAKAQTLK 

       250        260        270        280        290        300 
RAPNMKHPLM CLDAIEVGIV SGPRAGLEKE AEVASQVVKL DTTKGLIHVF FSQRGTAKVP 

       310        320        330        340        350        360 
GVTDRGLVPR KIKKVAIIGG GLMGSGIATA LILSNYPVIL KEVNEKFLEA GIGRVKANLQ 

       370        380        390        400        410        420 
SRVRKGSMSQ EKFEKTMSLL KGSLDYESFR DVDMVIEAVI ENISLKQQIF ADLEKYCPQH 

       430        440        450        460        470        480 
CILASNTSTI DLNKIGERTK SQDRIVGAHF FSPAHIMPLL EIVRTNHTSA QVIVDLLDVG 

       490        500        510        520        530        540 
KKIKKTPVVV GNCTGFAVNR MFFPYTQAAM FLVECGADPY LIDRAISKFG MPMGPFRLCD 

       550        560        570        580        590        600 
LVGFGVAIAT ATQFIENFSE RTYKSMIIPL MQEDKRAGEA TRKGFYLYDD KRKAKPDPEL 

       610        620        630        640        650        660 
KKYIEKARSI SGVKLDPKLA NLSEKDIIEM TFFPVVNEAC RVFAEGIAVK AADLDIAGIM 

       670        680        690        700        710        720 
GMGFPPYRGG IMFWADSIGS KYIYSRLDEW SKAYGEFFKP CAFLAERGSK GVLLSAPVKQ 


ASSRL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF123254 mRNA. Translation: AAD18042.1.
AC016827 Genomic DNA. Translation: AAF26990.1.
CP002686 Genomic DNA. Translation: AEE74468.1.
AY062621 mRNA. Translation: AAL32699.1.
RefSeqNP_187342.1. NM_111566.3.
UniGeneAt.24386.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WTBX-ray2.50A1-725[»]
DisProtDP00654.
ProteinModelPortalQ9ZPI5.
SMRQ9ZPI5. Positions 7-719.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid5205. 1 interaction.

Proteomic databases

PaxDbQ9ZPI5.
PRIDEQ9ZPI5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G06860.1; AT3G06860.1; AT3G06860.
GeneID819870.
KEGGath:AT3G06860.

Organism-specific databases

TAIRAT3G06860.

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261347.
InParanoidQ9ZPI5.
KOK10527.
OMAFFKPCSY.
PhylomeDBQ9ZPI5.

Enzyme and pathway databases

BioCycARA:AT3G06860-MONOMER.
MetaCyc:AT3G06860-MONOMER.
UniPathwayUPA00659.

Gene expression databases

ArrayExpressQ9ZPI5.
GenevestigatorQ9ZPI5.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
InterProIPR006180. 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]
PfamPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9ZPI5.

Entry information

Entry nameMFP2_ARATH
AccessionPrimary (citable) accession number: Q9ZPI5
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names