Q9ZPI5 (MFP2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	725 AA.
Sequence status	Complete.
Protein existence	Evidence 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

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Glyoxysome Peroxisome
Ligand	NAD
Molecular function	Isomerase Lyase Oxidoreductase
Technical term	3D-structure Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid beta-oxidation Inferred from expression pattern Ref.5. Source: TAIR
Cellular_component	cell wall Inferred from direct assay PubMed 16287169. Source: TAIR glyoxysome Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay PubMed 15496452. Source: TAIR peroxisome Inferred from direct assay PubMed 17951448. Source: TAIR plasmodesma Inferred from direct assay PubMed 21533090. Source: TAIR
Molecular_function	3-hydroxyacyl-CoA dehydrogenase activity Inferred from direct assay Ref.7. Source: UniProtKB 3-hydroxybutyryl-CoA epimerase activity Inferred from electronic annotation. Source: EC coenzyme binding Inferred from electronic annotation. Source: InterPro dodecenoyl-CoA delta-isomerase activity Inferred from electronic annotation. Source: EC enoyl-CoA hydratase activity Inferred from electronic annotation. Source: EC long-chain-enoyl-CoA hydratase activity Inferred from direct assay Ref.7. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 725

725

Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2

PRO_0000401371

Regions

Motif

723 – 725

3

Microbody targeting signal Potential

Sites

Active site

119

1

Nucleophile Potential

Active site

139

1

Proton acceptor Potential

Secondary structure

1

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725

Helix Strand Turn

Details...

Beta strand

8 – 13

6

Beta strand

17 – 24

8

Turn

26 – 29

4

Helix

33 – 46

14

Beta strand

54 – 62

9

Beta strand

85 – 87

3

Helix

88 – 92

5

Helix

93 – 99

7

Beta strand

101 – 103

3

Beta strand

105 – 109

5

Beta strand

111 – 114

4

Helix

116 – 123

8

Beta strand

124 – 129

6

Beta strand

134 – 136

3

Helix

139 – 142

4

Helix

150 – 158

9

Helix

160 – 169

10

Helix

175 – 180

6

Beta strand

185 – 187

3

Turn

190 – 192

3

Helix

193 – 205

13

Helix

214 – 216

3

Helix

224 – 241

18

Helix

247 – 260

14

Helix

263 – 277

15

Helix

281 – 294

14

Helix

295 – 297

3

Turn

300 – 302

3

Beta strand

303 – 305

3

Beta strand

315 – 318

4

Helix

322 – 332

11

Turn

333 – 335

3

Beta strand

338 – 341

4

Helix

345 – 361

17

Helix

372 – 375

4

Turn

376 – 378

3

Beta strand

379 – 386

8

Helix

387 – 389

3

Beta strand

393 – 397

5

Helix

403 – 416

14

Beta strand

422 – 425

4

Beta strand

428 – 430

3

Helix

432 – 435

4

Turn

436 – 438

3

Turn

442 – 444

3

Beta strand

445 – 450

6

Turn

454 – 456

3

Beta strand

459 – 464

6

Helix

470 – 482

13

Beta strand

486 – 493

8

Turn

494 – 497

4

Helix

498 – 514

17

Helix

519 – 529

11

Helix

535 – 542

8

Helix

544 – 557

14

Helix

559 – 561

3

Helix

567 – 572

6

Helix

605 – 610

6

Turn

618 – 621

4

Helix

624 – 644

21

Beta strand

647 – 649

3

Helix

651 – 662

12

Helix

666 – 668

3

Helix

671 – 678

8

Helix

680 – 694

15

Helix

696 – 698

3

Helix

702 – 710

9

Beta strand

714 – 716

3

Sequences

	Sequence		Length	Mass (Da)
	Q9ZPI5 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: AB079FB354CB394C	FASTA	725	78,840
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
+	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.

IPI

IPI00520365.

RefSeq

NP_187342.1. NM_111566.3.

UniGene

At.24386.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2WTB	X-ray	2.50	A	1-725	[»]

ProteinModelPortal

Q9ZPI5.

SMR

Q9ZPI5. Positions 7-719.

ModBase

Search...

Proteomic databases

PaxDb

Q9ZPI5.

PRIDE

Q9ZPI5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT3G06860.1; AT3G06860.1; AT3G06860.

GeneID

819870.

KEGG

ath:AT3G06860.

Organism-specific databases

TAIR

At3g06860.

Phylogenomic databases

eggNOG

COG1250.

HOGENOM

HOG000261347.

InParanoid

Q9ZPI5.

KO

K10527.

OMA

LEWALAC.

PhylomeDB

Q9ZPI5.

ProtClustDB

CLSN2684794.

Enzyme and pathway databases

BioCyc

MetaCyc:AT3G06860-MONOMER.

UniPathway

UPA00659.

Gene expression databases

ArrayExpress

Q9ZPI5.

Genevestigator

Q9ZPI5.

Family and domain databases

Gene3D

1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.

InterPro

IPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Pfam

PF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]

SUPFAM

SSF48179. 6DGDH_C_like. 2 hits.

PROSITE

PS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9ZPI5.

Entry information

Entry name

MFP2_ARATH

Accession

Primary (citable) accession number: Q9ZPI5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 30, 2010
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program