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Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2 (AtMPF2) [Includes: 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)]

 MFP2_ARATH              Reviewed;         725 AA.
Q9ZPI5;
30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
28-MAR-2018, entry version 135.
RecName: Full=Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2;
Short=AtMPF2;
Includes:
RecName: Full=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;
Includes:
RecName: Full=3-hydroxyacyl-CoA dehydrogenase;
EC=1.1.1.35;
Name=MFP2; OrderedLocusNames=At3g06860; ORFNames=F17A9.1;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=10521521; DOI=10.1105/tpc.11.10.1911;
Richmond T.A., Bleecker A.B.;
"A defect in beta-oxidation causes abnormal inflorescence development
in Arabidopsis.";
Plant Cell 11:1911-1924(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
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.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=10816107; DOI=10.1042/bst0280095;
Eastmond P.J., Graham I.A.;
"The multifunctional protein AtMFP2 is co-ordinately expressed with
other genes of fatty acid beta-oxidation during seed germination in
Arabidopsis thaliana (L.) Heynh.";
Biochem. Soc. Trans. 28:95-99(2000).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16507084; DOI=10.1111/j.1365-313X.2005.02650.x;
Rylott E.L., Eastmond P.J., Gilday A.D., Slocombe S.P., Larson T.R.,
Baker A., Graham I.A.;
"The Arabidopsis thaliana multifunctional protein gene (MFP2) of
peroxisomal beta-oxidation is essential for seedling establishment.";
Plant J. 45:930-941(2006).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis
of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
[8]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17951448; DOI=10.1105/tpc.107.050989;
Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T.,
Antonicelli G.E., Rasche N., Lueder F., Weckwerth W., Jahn O.;
"Proteome analysis of Arabidopsis leaf peroxisomes reveals novel
targeting peptides, metabolic pathways, and defense mechanisms.";
Plant Cell 19:3170-3193(2007).
[9]
FUNCTION.
PubMed=24254312; DOI=10.1104/pp.113.229807;
Bussell J.D., Reichelt M., Wiszniewski A.A., Gershenzon J.,
Smith S.M.;
"Peroxisomal ATP-binding cassette transporter COMATOSE and the
multifunctional protein abnormal INFLORESCENCE MERISTEM are required
for the production of benzoylated metabolites in Arabidopsis seeds.";
Plant Physiol. 164:48-54(2014).
[10]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND FUNCTION.
PubMed=20463021; DOI=10.1074/jbc.M110.106005;
Arent S., Christensen C.E., Pye V.E., Noergaard A., Henriksen A.;
"The multifunctional protein in peroxisomal beta-oxidation: structure
and substrate specificity of the Arabidopsis thaliana protein MFP2.";
J. Biol. Chem. 285:24066-24077(2010).
-!- 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)
(PubMed:10521521, PubMed:16507084, PubMed:20463021). Possesses 3-
hydroxy-3-phenylpropionyl-CoA dehydrogenase activity and is
involved in the peroxisomal beta-oxidation pathway for the
biosynthesis of benzoic acid (BA). Required for the accumulation
in seeds of substituted hydroxybenzoylated choline esters, which
are BA-containing secondary metabolites (PubMed:24254312).
{ECO:0000269|PubMed:10521521, ECO:0000269|PubMed:16507084,
ECO:0000269|PubMed:20463021, ECO:0000269|PubMed:24254312}.
-!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-
CoA + H(2)O.
-!- CATALYTIC ACTIVITY: (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-
CoA.
-!- CATALYTIC ACTIVITY: (S)-3-hydroxybutanoyl-CoA = (R)-3-
hydroxybutanoyl-CoA.
-!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
+ NADH.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=240 uM for crotonyl-CoA {ECO:0000269|PubMed:10521521};
-!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
-!- SUBCELLULAR LOCATION: Glyoxysome {ECO:0000305}. Peroxisome
{ECO:0000305}.
-!- TISSUE SPECIFICITY: Highly expressed in senescing leaves and at
lower levels in flowers and siliques.
{ECO:0000269|PubMed:10816107}.
-!- 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.
{ECO:0000269|PubMed:10816107}.
-!- DOMAIN: The epimerase and isomerase activities are contained in
the N-terminal region while the dehydrogenase activity is in the
C-terminal region. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Accumulation of long-chain acyl-CoA
substrates and increased size of peroxisomes.
{ECO:0000269|PubMed:16507084}.
-!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
hydratase/isomerase family. {ECO:0000305}.
-!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-
CoA dehydrogenase family. {ECO:0000305}.
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EMBL; AF123254; AAD18042.1; -; mRNA.
EMBL; AC016827; AAF26990.1; -; Genomic_DNA.
EMBL; CP002686; AEE74468.1; -; Genomic_DNA.
EMBL; AY062621; AAL32699.1; -; mRNA.
RefSeq; NP_187342.1; NM_111566.4.
UniGene; At.24386; -.
PDB; 2WTB; X-ray; 2.50 A; A=1-725.
PDBsum; 2WTB; -.
DisProt; DP00654; -.
ProteinModelPortal; Q9ZPI5; -.
SMR; Q9ZPI5; -.
BioGrid; 5205; 1.
STRING; 3702.AT3G06860.1; -.
SwissLipids; SLP:000000867; -.
iPTMnet; Q9ZPI5; -.
PaxDb; Q9ZPI5; -.
PRIDE; Q9ZPI5; -.
EnsemblPlants; AT3G06860.1; AT3G06860.1; AT3G06860.
GeneID; 819870; -.
Gramene; AT3G06860.1; AT3G06860.1; AT3G06860.
KEGG; ath:AT3G06860; -.
Araport; AT3G06860; -.
TAIR; locus:2077542; AT3G06860.
eggNOG; KOG1683; Eukaryota.
eggNOG; COG1024; LUCA.
eggNOG; COG1250; LUCA.
HOGENOM; HOG000261347; -.
InParanoid; Q9ZPI5; -.
KO; K10527; -.
OMA; PFRYMDT; -.
OrthoDB; EOG09360359; -.
PhylomeDB; Q9ZPI5; -.
BioCyc; ARA:AT3G06860-MONOMER; -.
BioCyc; MetaCyc:AT3G06860-MONOMER; -.
Reactome; R-ATH-390247; Beta-oxidation of very long chain fatty acids.
SABIO-RK; Q9ZPI5; -.
UniPathway; UPA00659; -.
EvolutionaryTrace; Q9ZPI5; -.
PRO; PR:Q9ZPI5; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9ZPI5; baseline and differential.
Genevisible; Q9ZPI5; AT.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IDA:TAIR.
GO; GO:0005777; C:peroxisome; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IDA:UniProtKB.
GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-EC.
GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:UniProtKB-EC.
GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
GO; GO:0016508; F:long-chain-enoyl-CoA hydratase activity; IDA:UniProtKB.
GO; GO:0006635; P:fatty acid beta-oxidation; IEP:TAIR.
InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
InterPro; IPR006108; 3HC_DH_C.
InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
InterPro; IPR001753; Enoyl-CoA_hydra/iso.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF00725; 3HCDH; 1.
Pfam; PF02737; 3HCDH_N; 1.
Pfam; PF00378; ECH_1; 1.
SUPFAM; SSF48179; SSF48179; 2.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF52096; SSF52096; 1.
PROSITE; PS00067; 3HCDH; 1.
PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Fatty acid metabolism; Glyoxysome;
Isomerase; Lipid metabolism; Lyase; Multifunctional enzyme; NAD;
Oxidoreductase; Peroxisome; Reference proteome.
CHAIN 1 725 Peroxisomal fatty acid beta-oxidation
multifunctional protein MFP2.
/FTId=PRO_0000401371.
MOTIF 723 725 Microbody targeting signal.
{ECO:0000305}.
ACT_SITE 119 119 Nucleophile. {ECO:0000255}.
ACT_SITE 139 139 Proton acceptor. {ECO:0000255}.
STRAND 8 13 {ECO:0000244|PDB:2WTB}.
STRAND 17 24 {ECO:0000244|PDB:2WTB}.
TURN 26 29 {ECO:0000244|PDB:2WTB}.
HELIX 33 46 {ECO:0000244|PDB:2WTB}.
STRAND 54 62 {ECO:0000244|PDB:2WTB}.
STRAND 85 87 {ECO:0000244|PDB:2WTB}.
HELIX 88 92 {ECO:0000244|PDB:2WTB}.
HELIX 93 99 {ECO:0000244|PDB:2WTB}.
STRAND 101 103 {ECO:0000244|PDB:2WTB}.
STRAND 105 109 {ECO:0000244|PDB:2WTB}.
STRAND 111 114 {ECO:0000244|PDB:2WTB}.
HELIX 116 123 {ECO:0000244|PDB:2WTB}.
STRAND 124 129 {ECO:0000244|PDB:2WTB}.
STRAND 134 136 {ECO:0000244|PDB:2WTB}.
HELIX 139 142 {ECO:0000244|PDB:2WTB}.
HELIX 150 158 {ECO:0000244|PDB:2WTB}.
HELIX 160 169 {ECO:0000244|PDB:2WTB}.
HELIX 175 180 {ECO:0000244|PDB:2WTB}.
STRAND 185 187 {ECO:0000244|PDB:2WTB}.
TURN 190 192 {ECO:0000244|PDB:2WTB}.
HELIX 193 205 {ECO:0000244|PDB:2WTB}.
HELIX 214 216 {ECO:0000244|PDB:2WTB}.
HELIX 224 241 {ECO:0000244|PDB:2WTB}.
HELIX 247 260 {ECO:0000244|PDB:2WTB}.
HELIX 263 277 {ECO:0000244|PDB:2WTB}.
HELIX 281 294 {ECO:0000244|PDB:2WTB}.
HELIX 295 297 {ECO:0000244|PDB:2WTB}.
TURN 300 302 {ECO:0000244|PDB:2WTB}.
STRAND 303 305 {ECO:0000244|PDB:2WTB}.
STRAND 315 318 {ECO:0000244|PDB:2WTB}.
HELIX 322 332 {ECO:0000244|PDB:2WTB}.
TURN 333 335 {ECO:0000244|PDB:2WTB}.
STRAND 338 341 {ECO:0000244|PDB:2WTB}.
HELIX 345 361 {ECO:0000244|PDB:2WTB}.
HELIX 372 375 {ECO:0000244|PDB:2WTB}.
TURN 376 378 {ECO:0000244|PDB:2WTB}.
STRAND 379 386 {ECO:0000244|PDB:2WTB}.
HELIX 387 389 {ECO:0000244|PDB:2WTB}.
STRAND 393 397 {ECO:0000244|PDB:2WTB}.
HELIX 403 416 {ECO:0000244|PDB:2WTB}.
STRAND 422 425 {ECO:0000244|PDB:2WTB}.
STRAND 428 430 {ECO:0000244|PDB:2WTB}.
HELIX 432 435 {ECO:0000244|PDB:2WTB}.
TURN 436 438 {ECO:0000244|PDB:2WTB}.
TURN 442 444 {ECO:0000244|PDB:2WTB}.
STRAND 445 450 {ECO:0000244|PDB:2WTB}.
TURN 454 456 {ECO:0000244|PDB:2WTB}.
STRAND 459 464 {ECO:0000244|PDB:2WTB}.
HELIX 470 482 {ECO:0000244|PDB:2WTB}.
STRAND 486 493 {ECO:0000244|PDB:2WTB}.
TURN 494 497 {ECO:0000244|PDB:2WTB}.
HELIX 498 514 {ECO:0000244|PDB:2WTB}.
HELIX 519 529 {ECO:0000244|PDB:2WTB}.
HELIX 535 542 {ECO:0000244|PDB:2WTB}.
HELIX 544 557 {ECO:0000244|PDB:2WTB}.
HELIX 559 561 {ECO:0000244|PDB:2WTB}.
HELIX 567 572 {ECO:0000244|PDB:2WTB}.
HELIX 605 610 {ECO:0000244|PDB:2WTB}.
TURN 618 621 {ECO:0000244|PDB:2WTB}.
HELIX 624 644 {ECO:0000244|PDB:2WTB}.
STRAND 647 649 {ECO:0000244|PDB:2WTB}.
HELIX 651 662 {ECO:0000244|PDB:2WTB}.
HELIX 666 668 {ECO:0000244|PDB:2WTB}.
HELIX 671 678 {ECO:0000244|PDB:2WTB}.
HELIX 680 694 {ECO:0000244|PDB:2WTB}.
HELIX 696 698 {ECO:0000244|PDB:2WTB}.
HELIX 702 710 {ECO:0000244|PDB:2WTB}.
STRAND 714 716 {ECO:0000244|PDB:2WTB}.
SEQUENCE 725 AA; 78840 MW; AB079FB354CB394C CRC64;
MDSRTKGKTV MEVGGDGVAV ITLINPPVNS LSFDVLYNLK SNYEEALSRN DVKAIVITGA
KGRFSGGFDI SGFGEMQKGN VKEPKAGYIS IDIITDLLEA ARKPSVAAID GLALGGGLEL
AMACHARISA PAAQLGLPEL QLGVIPGFGG TQRLPRLVGL TKALEMILTS KPVKAEEGHS
LGLIDAVVPP AELVTTARRW ALDIVGRRKP WVSSVSKTDK LPPLGEAREI LTFAKAQTLK
RAPNMKHPLM CLDAIEVGIV SGPRAGLEKE AEVASQVVKL DTTKGLIHVF FSQRGTAKVP
GVTDRGLVPR KIKKVAIIGG GLMGSGIATA LILSNYPVIL KEVNEKFLEA GIGRVKANLQ
SRVRKGSMSQ EKFEKTMSLL KGSLDYESFR DVDMVIEAVI ENISLKQQIF ADLEKYCPQH
CILASNTSTI DLNKIGERTK SQDRIVGAHF FSPAHIMPLL EIVRTNHTSA QVIVDLLDVG
KKIKKTPVVV GNCTGFAVNR MFFPYTQAAM FLVECGADPY LIDRAISKFG MPMGPFRLCD
LVGFGVAIAT ATQFIENFSE RTYKSMIIPL MQEDKRAGEA TRKGFYLYDD KRKAKPDPEL
KKYIEKARSI SGVKLDPKLA NLSEKDIIEM TFFPVVNEAC RVFAEGIAVK AADLDIAGIM
GMGFPPYRGG IMFWADSIGS KYIYSRLDEW SKAYGEFFKP CAFLAERGSK GVLLSAPVKQ
ASSRL


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