ID   AIM1_ARATH              Reviewed;         721 AA.
AC   Q9ZPI6;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   02-SEP-2026, entry version 178.
DE   RecName: Full=Peroxisomal fatty acid beta-oxidation multifunctional protein AIM1 {ECO:0000305};
DE   AltName: Full=Protein ABNORMAL INFLORESCENCE MERISTEM 1 {ECO:0000303|PubMed:10521521};
DE            Short=AtAIM1 {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:20463021};
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:20463021};
GN   Name=AIM1; OrderedLocusNames=At4g29010; ORFNames=F19B15.40;
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,
RP   BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=10521521; DOI=10.1105/tpc.11.10.1911;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   FUNCTION.
RX   PubMed=17544464; DOI=10.1016/j.phytochem.2007.04.024;
RA   Delker C., Zolman B.K., Miersch O., Wasternack C.;
RT   "Jasmonate biosynthesis in Arabidopsis thaliana requires peroxisomal beta-
RT   oxidation enzymes--additional proof by properties of pex6 and aim1.";
RL   Phytochemistry 68:1642-1650(2007).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
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   [8]
RP   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).
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).
CC   -!- FUNCTION: Involved in peroxisomal fatty acid beta-oxidation. Required
CC       for wound-induced jasmonate biosynthesis. Possesses enoyl-CoA hydratase
CC       activity against short chain substrates (C4-C6) and 3-hydroxyacyl-CoA
CC       dehydrogenase activity against chains of variable sizes (C6-C16)
CC       (PubMed:10521521, PubMed:17544464, PubMed:20463021). Possesses
CC       cinnamoyl-CoA hydratase activity and is involved in the peroxisomal
CC       beta-oxidation pathway for the biosynthesis of benzoic acid (BA).
CC       Required for the accumulation in seeds of benzoylated glucosinolates
CC       (BGs) and substituted hydroxybenzoylated choline esters, which are BA-
CC       containing secondary metabolites. Required for salicylic acid (SA) in
CC       seeds (PubMed:24254312). {ECO:0000269|PubMed:10521521,
CC       ECO:0000269|PubMed:17544464, ECO:0000269|PubMed:20463021,
CC       ECO:0000269|PubMed:24254312}.
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:20463021};
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:20463021};
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 + NADH +
CC         H(+); 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:20463021};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-3-hydroxybutanoyl-CoA + NAD(+) = acetoacetyl-CoA + NADH +
CC         H(+); 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 + NADH +
CC         H(+); 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 + NADH +
CC         H(+); 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         NADH + H(+); 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 + NADH + H(+); 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=115 uM for crotonyl-CoA {ECO:0000269|PubMed:10521521};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10521521}.
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: Reduced rosette size, twisted leaves, and
CC       abnormal and sterile flowers. {ECO:0000269|PubMed:10521521}.
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; AF123253; AAD18041.1; -; Genomic_DNA.
DR   EMBL; AL078470; CAB43915.1; -; Genomic_DNA.
DR   EMBL; AL161574; CAB79659.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85572.1; -; Genomic_DNA.
DR   EMBL; OZ408686; CAO7049146.1; -; Genomic_DNA.
DR   EMBL; AY059815; AAL24297.1; -; mRNA.
DR   EMBL; AY072072; AAL59895.1; -; mRNA.
DR   EMBL; AY096659; AAM20293.1; -; mRNA.
DR   PIR; T08956; T08956.
DR   RefSeq; NP_194630.1; NM_119045.5.
DR   AlphaFoldDB; Q9ZPI6; -.
DR   SMR; Q9ZPI6; -.
DR   BioGRID; 14309; 8.
DR   FunCoup; Q9ZPI6; 2624.
DR   STRING; 3702.Q9ZPI6; -.
DR   SwissLipids; SLP:000000866; -.
DR   iPTMnet; Q9ZPI6; -.
DR   MetOSite; Q9ZPI6; -.
DR   PaxDb; 3702-Q9ZPI6; -.
DR   ProteomicsDB; 244919; -.
DR   GeneID; 829022; -.
DR   KEGG; ath:AT4G29010; -.
DR   Araport; AT4G29010; -.
DR   TAIR; AT4G29010; AIM1.
DR   eggNOG; KOG1683; Eukaryota.
DR   HOGENOM; CLU_009834_16_3_1; -.
DR   InParanoid; Q9ZPI6; -.
DR   OMA; DPLFWKP; -.
DR   PhylomeDB; Q9ZPI6; -.
DR   BioCyc; MetaCyc:AT4G29010-MONOMER; -.
DR   SABIO-RK; Q9ZPI6; -.
DR   UniPathway; UPA00659; -.
DR   CD-CODE; 4299E36E; Nucleolus.
DR   PRO; PR:Q9ZPI6; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9ZPI6; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISM:TAIR.
DR   GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR   GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0120092; F:(2E)-butenoyl-CoA hydratase activity; IEA:RHEA.
DR   GO; GO:0003857; F:(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR   GO; GO:0018812; F:3-hydroxyacyl-CoA dehydratase activity; EXP: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; IDA:UniProtKB.
DR   GO; GO:0016509; F:long-chain (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity; IEA:RHEA.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; ISS:TAIR.
DR   GO; GO:0009908; P:flower development; IMP:TAIR.
DR   GO; GO:0009695; P:jasmonic acid biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0009845; P:seed germination; IMP:TIGR.
DR   CDD; cd06558; crotonase-like; 1.
DR   FunFam; 3.40.50.720:FF:000009; Fatty oxidation complex, alpha subunit; 1.
DR   FunFam; 1.10.1040.50:FF:000004; Peroxisomal fatty acid beta-oxidation multifunctional protein; 1.
DR   FunFam; 3.90.226.10:FF:000025; Peroxisomal fatty acid beta-oxidation multifunctional protein; 1.
DR   Gene3D; 1.10.1040.50; -; 1.
DR   Gene3D; 3.90.226.10; 2-enoyl-CoA Hydratase, Chain A, domain 1; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   PANTHER; PTHR23309; 3-HYDROXYACYL-COA DEHYROGENASE; 1.
DR   PANTHER; PTHR23309:SF53; PEROXISOMAL FATTY ACID BETA-OXIDATION MULTIFUNCTIONAL PROTEIN AIM1; 1.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE   1: Evidence at protein level;
KW   Fatty acid metabolism; Isomerase; Lipid metabolism; Lyase;
KW   Multifunctional enzyme; NAD; Oxidoreductase; Peroxisome;
KW   Reference proteome.
FT   CHAIN           1..721
FT                   /note="Peroxisomal fatty acid beta-oxidation
FT                   multifunctional protein AIM1"
FT                   /id="PRO_0000401372"
FT   MOTIF           719..721
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        116
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        136
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   721 AA;  77858 MW;  F72FB3252B2216CF CRC64;
     MAKKIGVTME VGNDGVAVIT ISNPPVNSLA SPIISGLKEK FRDANQRNDV KAIVLIGNNG
     RFSGGFDINV FQQVHKTGDL SLMPEVSVEL VCNLMEDSRK PVVAAVEGLA LGGGLELAMA
     CHARVAAPKA QLGLPELTLG VIPGFGGTQR LPRLVGLAKA TDMILLSKSI SSEEGHKLGL
     IDALVPPGDV LSTSRKWALD IAEGRKPFLQ SLHRTDKIGS LSEARAILKN SRQLAKKIAP
     NMPQHHACIE VIEEGIIHGG YSGVLKEAEV FKQLVLSDTA KGLVHVFFAQ RATSKVPNVT
     DVGLKPRPIK KVAVIGGGLM GSGIATALLL SNIRVVLKEI NSEFLMKGIK SVEANMKSLV
     SRGKLTQDKA GKALSLFKGV LDYTEFNDVD MVIEAVIENI QLKQNIFKEI EKVCSPHCIL
     ASNTSTIDLD VIGEKTNSKD RIVGAHFFSP AHLMPLLEIV RSKNTSAQVI LDLMAVGKAI
     KKVPVVVGNC IGFAVNRTFF PYSQAAHMLA NLGVDLFRID SVITSFGLPL GPFQLGDLAG
     HGIGLAVGPI YAKVYGDRMF RSPMTELLLK SGRNGKINGR GYYIYEKGSK PKPDPSVLSI
     VEKSRKLTNI MPGGKPISVT DKEIVEMILF PVVNEACRVL DEGVVIRASD LDIASVLGMS
     FPSYRGGIVF WADTVGPKYI YERLKKLSET YGSFFKPSRY LEERAMNGML LSESKSSRSK
     L
//