MFP2_ARATH
ID MFP2_ARATH Reviewed; 725 AA.
AC Q9ZPI5;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2 {ECO:0000305};
DE Short=AtMPF2 {ECO:0000303|PubMed:10521521};
DE Includes:
DE RecName: Full=Enoyl-CoA hydratase/3-2-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase;
DE EC=4.2.1.17 {ECO:0000269|PubMed:10521521, ECO:0000269|PubMed:16507084};
DE EC=5.1.2.3 {ECO:0000305};
DE EC=5.3.3.8 {ECO:0000305};
DE Includes:
DE RecName: Full=3-hydroxyacyl-CoA dehydrogenase;
DE EC=1.1.1.35 {ECO:0000269|PubMed:16507084, ECO:0000269|PubMed:20463021};
GN Name=MFP2 {ECO:0000303|PubMed:10521521};
GN OrderedLocusNames=At3g06860 {ECO:0000312|Araport:AT3G06860};
GN ORFNames=F17A9.1 {ECO:0000312|EMBL:AAF26990.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10521521; DOI=10.2307/3871086;
RA Richmond T.A., Bleecker A.B.;
RT "A defect in beta-oxidation causes abnormal inflorescence development in
RT Arabidopsis.";
RL Plant Cell 11:1911-1924(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10816107; DOI=10.1042/bst0280095;
RA Eastmond P.J., Graham I.A.;
RT "The multifunctional protein AtMFP2 is co-ordinately expressed with other
RT genes of fatty acid beta-oxidation during seed germination in Arabidopsis
RT thaliana (L.) Heynh.";
RL Biochem. Soc. Trans. 28:95-99(2000).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16507084; DOI=10.1111/j.1365-313x.2005.02650.x;
RA Rylott E.L., Eastmond P.J., Gilday A.D., Slocombe S.P., Larson T.R.,
RA Baker A., Graham I.A.;
RT "The Arabidopsis thaliana multifunctional protein gene (MFP2) of
RT peroxisomal beta-oxidation is essential for seedling establishment.";
RL Plant J. 45:930-941(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [9]
RP FUNCTION.
RX PubMed=24254312; DOI=10.1104/pp.113.229807;
RA Bussell J.D., Reichelt M., Wiszniewski A.A., Gershenzon J., Smith S.M.;
RT "Peroxisomal ATP-binding cassette transporter COMATOSE and the
RT multifunctional protein abnormal INFLORESCENCE MERISTEM are required for
RT the production of benzoylated metabolites in Arabidopsis seeds.";
RL Plant Physiol. 164:48-54(2014).
RN [10]
RP FUNCTION.
RX PubMed=31064880; DOI=10.1073/pnas.1904143116;
RA Wang L., Wang C., Liu X., Cheng J., Li S., Zhu J.K., Gong Z.;
RT "Peroxisomal beta-oxidation regulates histone acetylation and DNA
RT methylation in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:10576-10585(2019).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20463021; DOI=10.1074/jbc.m110.106005;
RA Arent S., Christensen C.E., Pye V.E., Noergaard A., Henriksen A.;
RT "The multifunctional protein in peroxisomal beta-oxidation: structure and
RT substrate specificity of the Arabidopsis thaliana protein MFP2.";
RL J. Biol. Chem. 285:24066-24077(2010).
CC -!- FUNCTION: Involved in peroxisomal fatty acid beta-oxidation during seed
CC germination. Possesses enoyl-CoA hydratase activity against long chain
CC substrates (C14-C18) and 3-hydroxyacyl-CoA dehydrogenase activity
CC against chains of variable sizes (C6-C18) (PubMed:10521521,
CC PubMed:16507084, PubMed:20463021). Possesses 3-hydroxy-3-
CC phenylpropionyl-CoA dehydrogenase activity and is involved in the
CC peroxisomal beta-oxidation pathway for the biosynthesis of benzoic acid
CC (BA). Required for the accumulation in seeds of substituted
CC hydroxybenzoylated choline esters, which are BA-containing secondary
CC metabolites (PubMed:24254312). Fatty acid beta-oxidation pathway in
CC peroxisomes regulates gene silencing, histone acetylation and DNA
CC methylation (PubMed:31064880). {ECO:0000269|PubMed:10521521,
CC ECO:0000269|PubMed:16507084, ECO:0000269|PubMed:20463021,
CC ECO:0000269|PubMed:24254312, ECO:0000269|PubMed:31064880}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:58856; EC=4.2.1.17;
CC Evidence={ECO:0000269|PubMed:10521521, ECO:0000269|PubMed:16507084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC ChEBI:CHEBI:137480; EC=4.2.1.17;
CC Evidence={ECO:0000269|PubMed:10521521, ECO:0000269|PubMed:16507084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-hydroxybutanoyl-CoA = (2E)-butenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:26558, ChEBI:CHEBI:15377, ChEBI:CHEBI:57316,
CC ChEBI:CHEBI:57332; Evidence={ECO:0000269|PubMed:20463021};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:26560;
CC Evidence={ECO:0000269|PubMed:20463021};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxyoctanoyl-CoA = (2E)-octenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:31199, ChEBI:CHEBI:15377, ChEBI:CHEBI:62242,
CC ChEBI:CHEBI:62617; Evidence={ECO:0000269|PubMed:20463021};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31201;
CC Evidence={ECO:0000269|PubMed:20463021};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-hydroxydodecanoyl-CoA = (2E)-dodecenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:31075, ChEBI:CHEBI:15377, ChEBI:CHEBI:57330,
CC ChEBI:CHEBI:62558; Evidence={ECO:0000269|PubMed:20463021};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31077;
CC Evidence={ECO:0000269|PubMed:20463021};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxytetradecanoyl-CoA = (2E)-tetradecenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:31171, ChEBI:CHEBI:15377, ChEBI:CHEBI:61405,
CC ChEBI:CHEBI:62614; Evidence={ECO:0000269|PubMed:20463021};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31173;
CC Evidence={ECO:0000269|PubMed:20463021};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxyhexanoyl-CoA = (2E)-hexenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:30547, ChEBI:CHEBI:15377, ChEBI:CHEBI:62075,
CC ChEBI:CHEBI:62077; Evidence={ECO:0000269|PubMed:20463021};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30549;
CC Evidence={ECO:0000269|PubMed:20463021};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489;
CC EC=5.3.3.8; Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097;
CC EC=5.3.3.8; Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA;
CC Xref=Rhea:RHEA:21760, ChEBI:CHEBI:57315, ChEBI:CHEBI:57316;
CC EC=5.1.2.3; Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC Evidence={ECO:0000269|PubMed:16507084, ECO:0000269|PubMed:20463021};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22433;
CC Evidence={ECO:0000269|PubMed:20463021};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-hydroxybutanoyl-CoA + NAD(+) = acetoacetyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:30799, ChEBI:CHEBI:15378, ChEBI:CHEBI:57286,
CC ChEBI:CHEBI:57316, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:20463021};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30800;
CC Evidence={ECO:0000269|PubMed:20463021};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxyhexanoyl-CoA + NAD(+) = 3-oxohexanoyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:31143, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:62075, ChEBI:CHEBI:62418;
CC Evidence={ECO:0000269|PubMed:20463021};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31144;
CC Evidence={ECO:0000269|PubMed:20463021};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxyoctanoyl-CoA + NAD(+) = 3-oxooctanoyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:31195, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:62617, ChEBI:CHEBI:62619;
CC Evidence={ECO:0000269|PubMed:20463021};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31196;
CC Evidence={ECO:0000269|PubMed:20463021};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-hydroxydodecanoyl-CoA + NAD(+) = 3-oxododecanoyl-CoA +
CC H(+) + NADH; Xref=Rhea:RHEA:31179, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62558,
CC ChEBI:CHEBI:62615; Evidence={ECO:0000269|PubMed:20463021};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31180;
CC Evidence={ECO:0000269|PubMed:20463021};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxytetradecanoyl-CoA + NAD(+) = 3-oxotetradecanoyl-
CC CoA + H(+) + NADH; Xref=Rhea:RHEA:31167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62543,
CC ChEBI:CHEBI:62614; Evidence={ECO:0000269|PubMed:20463021};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31168;
CC Evidence={ECO:0000269|PubMed:20463021};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=240 uM for crotonyl-CoA {ECO:0000269|PubMed:10521521};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Glyoxysome {ECO:0000305}. Peroxisome
CC {ECO:0000269|PubMed:17951448}.
CC -!- TISSUE SPECIFICITY: Highly expressed in senescing leaves and at lower
CC levels in flowers and siliques. {ECO:0000269|PubMed:10816107}.
CC -!- DEVELOPMENTAL STAGE: Expression increases rapidly during seed
CC germination to reach a peak at 2-3 days after imbibition (DAI) and then
CC declines to basal levels at 5 DAI. {ECO:0000269|PubMed:10816107}.
CC -!- DOMAIN: The epimerase and isomerase activities are contained in the N-
CC terminal region while the dehydrogenase activity is in the C-terminal
CC region. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Accumulation of long-chain acyl-CoA substrates
CC and increased size of peroxisomes. {ECO:0000269|PubMed:16507084}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AF123254; AAD18042.1; -; mRNA.
DR EMBL; AC016827; AAF26990.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74468.1; -; Genomic_DNA.
DR EMBL; AY062621; AAL32699.1; -; mRNA.
DR RefSeq; NP_187342.1; NM_111566.4.
DR PDB; 2WTB; X-ray; 2.50 A; A=1-725.
DR PDBsum; 2WTB; -.
DR AlphaFoldDB; Q9ZPI5; -.
DR SMR; Q9ZPI5; -.
DR BioGRID; 5205; 11.
DR STRING; 3702.AT3G06860.1; -.
DR SwissLipids; SLP:000000867; -.
DR iPTMnet; Q9ZPI5; -.
DR PaxDb; Q9ZPI5; -.
DR PRIDE; Q9ZPI5; -.
DR ProteomicsDB; 250622; -.
DR EnsemblPlants; AT3G06860.1; AT3G06860.1; AT3G06860.
DR GeneID; 819870; -.
DR Gramene; AT3G06860.1; AT3G06860.1; AT3G06860.
DR KEGG; ath:AT3G06860; -.
DR Araport; AT3G06860; -.
DR TAIR; locus:2077542; AT3G06860.
DR eggNOG; KOG1683; Eukaryota.
DR HOGENOM; CLU_009834_16_3_1; -.
DR InParanoid; Q9ZPI5; -.
DR OMA; PFRYMDT; -.
DR OrthoDB; 219667at2759; -.
DR PhylomeDB; Q9ZPI5; -.
DR BioCyc; ARA:AT3G06860-MON; -.
DR BioCyc; MetaCyc:AT3G06860-MON; -.
DR BRENDA; 4.2.1.17; 399.
DR SABIO-RK; Q9ZPI5; -.
DR UniPathway; UPA00659; -.
DR EvolutionaryTrace; Q9ZPI5; -.
DR PRO; PR:Q9ZPI5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9ZPI5; baseline and differential.
DR Genevisible; Q9ZPI5; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0016508; F:long-chain-enoyl-CoA hydratase activity; IDA:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEP:TAIR.
DR DisProt; DP00654; -.
DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR InterPro; IPR006108; 3HC_DH_C.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF48179; SSF48179; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00067; 3HCDH; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fatty acid metabolism; Glyoxysome; Isomerase;
KW Lipid metabolism; Lyase; Multifunctional enzyme; NAD; Oxidoreductase;
KW Peroxisome; Reference proteome.
FT CHAIN 1..725
FT /note="Peroxisomal fatty acid beta-oxidation
FT multifunctional protein MFP2"
FT /id="PRO_0000401371"
FT MOTIF 723..725
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000305"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT ACT_SITE 139
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:2WTB"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:2WTB"
FT TURN 26..29
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 33..46
FT /evidence="ECO:0007829|PDB:2WTB"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:2WTB"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 93..99
FT /evidence="ECO:0007829|PDB:2WTB"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2WTB"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:2WTB"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:2WTB"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:2WTB"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 150..158
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 175..180
FT /evidence="ECO:0007829|PDB:2WTB"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:2WTB"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 193..205
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 224..241
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 247..260
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 263..277
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 281..294
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:2WTB"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:2WTB"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:2WTB"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 322..332
FT /evidence="ECO:0007829|PDB:2WTB"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:2WTB"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 345..361
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 372..375
FT /evidence="ECO:0007829|PDB:2WTB"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:2WTB"
FT STRAND 379..386
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:2WTB"
FT STRAND 393..397
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 403..416
FT /evidence="ECO:0007829|PDB:2WTB"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:2WTB"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 432..435
FT /evidence="ECO:0007829|PDB:2WTB"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:2WTB"
FT TURN 442..444
FT /evidence="ECO:0007829|PDB:2WTB"
FT STRAND 445..450
FT /evidence="ECO:0007829|PDB:2WTB"
FT TURN 454..456
FT /evidence="ECO:0007829|PDB:2WTB"
FT STRAND 459..464
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 470..482
FT /evidence="ECO:0007829|PDB:2WTB"
FT STRAND 486..493
FT /evidence="ECO:0007829|PDB:2WTB"
FT TURN 494..497
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 498..514
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 519..529
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 535..542
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 544..557
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 559..561
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 567..572
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 605..610
FT /evidence="ECO:0007829|PDB:2WTB"
FT TURN 618..621
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 624..644
FT /evidence="ECO:0007829|PDB:2WTB"
FT STRAND 647..649
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 651..662
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 666..668
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 671..678
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 680..694
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 696..698
FT /evidence="ECO:0007829|PDB:2WTB"
FT HELIX 702..710
FT /evidence="ECO:0007829|PDB:2WTB"
FT STRAND 714..716
FT /evidence="ECO:0007829|PDB:2WTB"
SQ 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
