AIM1_ARATH
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 03-AUG-2022, entry version 162.
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=10.2307/3871086;
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=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 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 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 [6]
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 [7]
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 [8]
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 + 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: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=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; 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 STRING; 3702.AT4G29010.1; -.
DR SwissLipids; SLP:000000866; -.
DR iPTMnet; Q9ZPI6; -.
DR MetOSite; Q9ZPI6; -.
DR PaxDb; Q9ZPI6; -.
DR PRIDE; Q9ZPI6; -.
DR ProteomicsDB; 244919; -.
DR EnsemblPlants; AT4G29010.1; AT4G29010.1; AT4G29010.
DR GeneID; 829022; -.
DR Gramene; AT4G29010.1; AT4G29010.1; AT4G29010.
DR KEGG; ath:AT4G29010; -.
DR Araport; AT4G29010; -.
DR TAIR; locus:2119891; AT4G29010.
DR eggNOG; KOG1683; Eukaryota.
DR HOGENOM; CLU_009834_16_3_1; -.
DR InParanoid; Q9ZPI6; -.
DR OMA; DPLFWKP; -.
DR OrthoDB; 219667at2759; -.
DR PhylomeDB; Q9ZPI6; -.
DR BioCyc; MetaCyc:AT4G29010-MON; -.
DR SABIO-RK; Q9ZPI6; -.
DR UniPathway; UPA00659; -.
DR PRO; PR:Q9ZPI6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZPI6; baseline and differential.
DR Genevisible; Q9ZPI6; AT.
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: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; IDA:UniProtKB.
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 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 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
