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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

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 – 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
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 Curated. Peroxisome Curated

GO - Cellular componenti

  1. cell wall Source: TAIR
  2. glyoxysome Source: UniProtKB-KW
  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 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

ExpressionAtlasiQ9ZPI5. baseline and differential.
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 – 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.
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

        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 .
RefSeqi NP_187342.1. NM_111566.3.
UniGenei At.24386.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

ExpressionAtlasi Q9ZPI5. baseline and differential.
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: November 26, 2014
This is version 111 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