ID ECHP_RAT Reviewed; 722 AA.
AC P07896; Q5EBD2;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 192.
DE RecName: Full=Peroxisomal bifunctional enzyme {ECO:0000305};
DE Short=PBE;
DE Short=PBFE;
DE AltName: Full=Multifunctional enzyme 1 {ECO:0000303|PubMed:11781327};
DE Short=MFE1;
DE AltName: Full=Multifunctional protein 1;
DE Short=MFP1;
DE Includes:
DE RecName: Full=Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase;
DE EC=4.2.1.17 {ECO:0000269|PubMed:12106015, ECO:0000269|PubMed:2303409};
DE EC=5.3.3.8 {ECO:0000269|PubMed:11781327, ECO:0000269|PubMed:12106015, ECO:0000269|PubMed:2303409};
DE Includes:
DE RecName: Full=3-hydroxyacyl-CoA dehydrogenase;
DE EC=1.1.1.35 {ECO:0000269|PubMed:2303409};
GN Name=Ehhadh {ECO:0000312|RGD:621441};
GN Synonyms=Mfe1 {ECO:0000303|PubMed:11781327};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=4019459; DOI=10.1016/s0021-9258(17)39435-8;
RA Osumi T., Ishii N., Hijikata M., Kamijo K., Ozasa H., Furuta S.,
RA Miyazawa S., Kondo K., Inoue K., Kagamiyama H., Hashimoto T.;
RT "Molecular cloning and nucleotide sequence of the cDNA for rat peroxisomal
RT enoyl-CoA: hydratase-3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme.";
RL J. Biol. Chem. 260:8905-8910(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
RX PubMed=3036802; DOI=10.1016/s0021-9258(18)47541-2;
RA Ishii N., Hijikata M., Osumi T., Hashimoto T.;
RT "Structural organization of the gene for rat enoyl-CoA hydratase:3-
RT hydroxyacyl-CoA dehydrogenase bifunctional enzyme.";
RL J. Biol. Chem. 262:8144-8150(1987).
RN [4]
RP PROTEIN SEQUENCE OF 260-265; 294-302; 520-531 AND 710-719.
RX PubMed=8856068; DOI=10.1111/j.1432-1033.1996.0660h.x;
RA Dieuaide-Noubhani M., Novikov D., Baumgart E., Vanhooren J.C.T.,
RA Fransen M., Goethals M., Vandekerckhove J., Van Veldhoven P.P.,
RA Mannaerts G.P.;
RT "Further characterization of the peroxisomal 3-hydroxyacyl-CoA
RT dehydrogenases from rat liver. Relationship between the different
RT dehydrogenases and evidence that fatty acids and the C27 bile acids di- and
RT tri-hydroxycoprostanic acids are metabolized by separate multifunctional
RT proteins.";
RL Eur. J. Biochem. 240:660-666(1996).
RN [5]
RP FUNCTION AS AN ISOMERASE, AND CATALYTIC ACTIVITY.
RX PubMed=2303409; DOI=10.1016/s0021-9258(19)39819-9;
RA Palosaari P.M., Hiltunen J.K.;
RT "Peroxisomal bifunctional protein from rat liver is a trifunctional enzyme
RT possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and
RT delta 3, delta 2-enoyl-CoA isomerase activities.";
RL J. Biol. Chem. 265:2446-2449(1990).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12106015; DOI=10.1042/bj20020292;
RA Kiema T.R., Taskinen J.P., Pirilae P.L., Koivuranta K.T., Wierenga R.K.,
RA Hiltunen J.K.;
RT "Organization of the multifunctional enzyme type 1: interaction between
RT N- and C-terminal domains is required for the hydratase-1/isomerase
RT activity.";
RL Biochem. J. 367:433-441(2002).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND CATALYTIC ACTIVITY.
RX PubMed=11781327; DOI=10.1074/jbc.m112228200;
RA Zhang D., Yu W., Geisbrecht B.V., Gould S.J., Sprecher H., Schulz H.;
RT "Functional characterization of delta3,delta2-enoyl-CoA isomerases from rat
RT liver.";
RL J. Biol. Chem. 277:9127-9132(2002).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23351063; DOI=10.1111/febs.12150;
RA Kasaragod P., Schmitz W., Hiltunen J.K., Wierenga R.K.;
RT "The isomerase and hydratase reaction mechanism of the crotonase active
RT site of the multifunctional enzyme (type-1), as deduced from structures of
RT complexes with 3S-hydroxy-acyl-CoA.";
RL FEBS J. 280:3160-3175(2013).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 260-722, AND SUBUNIT.
RX PubMed=16330050; DOI=10.1016/j.jmb.2005.10.085;
RA Taskinen J.P., Kiema T.R., Hiltunen J.K., Wierenga R.K.;
RT "Structural studies of MFE-1: the 1.9 A crystal structure of the
RT dehydrogenase part of rat peroxisomal MFE-1.";
RL J. Mol. Biol. 355:734-746(2006).
CC -!- FUNCTION: Peroxisomal trifunctional enzyme possessing 2-enoyl-CoA
CC hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-
CC CoA isomerase activities (PubMed:2303409, PubMed:12106015,
CC PubMed:23351063). Catalyzes two of the four reactions of the long chain
CC fatty acids peroxisomal beta-oxidation pathway (PubMed:2303409,
CC PubMed:12106015). Can also use branched-chain fatty acids such as 2-
CC methyl-2E-butenoyl-CoA as a substrate, which is hydrated into (2S,3S)-
CC 3-hydroxy-2-methylbutanoyl-CoA (Probable). Optimal isomerase for 2,5
CC double bonds into 3,5 form isomerization in a range of enoyl-CoA
CC species. Also able to isomerize both 3-cis and 3-trans double bonds
CC into the 2-trans form in a range of enoyl-CoA species
CC (PubMed:11781327). Regulates the amount of medium-chain dicarboxylic
CC fatty acids which are essential regulators of all fatty acid oxidation
CC pathways (By similarity). Also involved in the degradation of long-
CC chain dicarboxylic acids through peroxisomal beta-oxidation (By
CC similarity). {ECO:0000250|UniProtKB:Q08426,
CC ECO:0000250|UniProtKB:Q9DBM2, ECO:0000269|PubMed:11781327,
CC ECO:0000269|PubMed:12106015, ECO:0000269|PubMed:2303409,
CC ECO:0000305|PubMed:23351063}.
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:0000305|PubMed:2303409};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16106;
CC Evidence={ECO:0000305|PubMed:2303409};
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:0000305|PubMed:2303409};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20725;
CC Evidence={ECO:0000305|PubMed:2303409};
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|PubMed:11781327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45901;
CC Evidence={ECO:0000305|PubMed:11781327};
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|PubMed:11781327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45229;
CC Evidence={ECO:0000305|PubMed:11781327};
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:0000250|UniProtKB:Q08426};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22433;
CC Evidence={ECO:0000250|UniProtKB:Q08426};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3S)-3-hydroxy-2-methylbutanoyl-CoA = (2E)-2-methylbut-2-
CC enoyl-CoA + H2O; Xref=Rhea:RHEA:31119, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57312, ChEBI:CHEBI:57337;
CC Evidence={ECO:0000305|PubMed:23351063};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31121;
CC Evidence={ECO:0000305|PubMed:23351063};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3E,5Z)-tetradecadienoyl-CoA = (2E,5Z)-tetradecadienoyl-CoA;
CC Xref=Rhea:RHEA:47464, ChEBI:CHEBI:71586, ChEBI:CHEBI:87701;
CC Evidence={ECO:0000269|PubMed:11781327};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:47466;
CC Evidence={ECO:0000269|PubMed:11781327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3E,5Z)-octadienoyl-CoA = (2E,5Z)-octadienoyl-CoA;
CC Xref=Rhea:RHEA:49932, ChEBI:CHEBI:85108, ChEBI:CHEBI:131990;
CC Evidence={ECO:0000269|PubMed:11781327};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:49934;
CC Evidence={ECO:0000269|PubMed:11781327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxydecanoyl-CoA + NAD(+) = 3-oxodecanoyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:31187, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:62548, ChEBI:CHEBI:62616;
CC Evidence={ECO:0000269|PubMed:2303409};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31188;
CC Evidence={ECO:0000305|PubMed:2303409};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3E)-decenoyl-CoA = (2E)-decenoyl-CoA; Xref=Rhea:RHEA:45752,
CC ChEBI:CHEBI:61406, ChEBI:CHEBI:84793;
CC Evidence={ECO:0000269|PubMed:2303409};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45753;
CC Evidence={ECO:0000305|PubMed:2303409};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3Z)-hexenoyl-CoA = (2E)-hexenoyl-CoA; Xref=Rhea:RHEA:45748,
CC ChEBI:CHEBI:62077, ChEBI:CHEBI:85415;
CC Evidence={ECO:0000269|PubMed:2303409};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45749;
CC Evidence={ECO:0000305|PubMed:2303409};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3E)-hexenoyl-CoA = (2E)-hexenoyl-CoA; Xref=Rhea:RHEA:45736,
CC ChEBI:CHEBI:62077, ChEBI:CHEBI:84790;
CC Evidence={ECO:0000269|PubMed:12106015, ECO:0000269|PubMed:2303409};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45737;
CC Evidence={ECO:0000305|PubMed:12106015, ECO:0000305|PubMed:2303409};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxydecanoyl-CoA = (2E)-decenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:31191, ChEBI:CHEBI:15377, ChEBI:CHEBI:61406,
CC ChEBI:CHEBI:62616; Evidence={ECO:0000269|PubMed:12106015,
CC ECO:0000269|PubMed:2303409};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31193;
CC Evidence={ECO:0000305|PubMed:12106015, ECO:0000305|PubMed:2303409};
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:12106015};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30549;
CC Evidence={ECO:0000305|PubMed:12106015};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxyhexadecanoyl-CoA + NAD(+) = 3-oxohexadecanoyl-CoA
CC + H(+) + NADH; Xref=Rhea:RHEA:31159, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57349, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:62613; Evidence={ECO:0000250|UniProtKB:Q08426};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31160;
CC Evidence={ECO:0000250|UniProtKB:Q08426};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxyhexadecanoyl-CoA = (2E)-hexadecenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:31163, ChEBI:CHEBI:15377, ChEBI:CHEBI:61526,
CC ChEBI:CHEBI:62613; Evidence={ECO:0000250|UniProtKB:Q08426};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31165;
CC Evidence={ECO:0000250|UniProtKB:Q08426};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-hexadecenedioyl-CoA + H2O = (3S)-hydroxyhexadecanedioyl-
CC CoA; Xref=Rhea:RHEA:40259, ChEBI:CHEBI:15377, ChEBI:CHEBI:77075,
CC ChEBI:CHEBI:77080; Evidence={ECO:0000250|UniProtKB:Q08426};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40260;
CC Evidence={ECO:0000250|UniProtKB:Q08426};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxyhexadecanedioyl-CoA + NAD(+) = 3-
CC oxohexadecanedioyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:40267,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:77080, ChEBI:CHEBI:77081;
CC Evidence={ECO:0000250|UniProtKB:Q08426};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40268;
CC Evidence={ECO:0000250|UniProtKB:Q08426};
CC -!- ACTIVITY REGULATION: Enzyme activity enhanced by acetylation.
CC {ECO:0000250}.
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000269|PubMed:11781327, ECO:0000269|PubMed:12106015,
CC ECO:0000269|PubMed:2303409}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16330050}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:11781327}.
CC -!- PTM: Acetylated, leading to enhanced enzyme activity. Acetylation is
CC enhanced by up to 80% after treatment either with trichostin A (TCA) or
CC with nicotinamide (NAM) with highest increase on Lys-345. Acetylation
CC and enzyme activity increased by about 1.5% on addition of fatty acids
CC (By similarity). {ECO:0000250|UniProtKB:Q08426}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000305|PubMed:12106015}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. {ECO:0000305|PubMed:12106015}.
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DR EMBL; K03249; AAA41825.1; -; mRNA.
DR EMBL; BC089777; AAH89777.1; -; mRNA.
DR EMBL; J02748; AAA41826.1; -; Genomic_DNA.
DR PIR; A23575; DWRTEP.
DR RefSeq; NP_598290.1; NM_133606.1.
DR PDB; 1ZCJ; X-ray; 1.90 A; A=260-722.
DR PDB; 2X58; X-ray; 2.80 A; A/B=1-722.
DR PDB; 3ZW8; X-ray; 2.50 A; A/B=1-722.
DR PDB; 3ZW9; X-ray; 2.90 A; A/B=1-722.
DR PDB; 3ZWA; X-ray; 2.47 A; A/B=1-722.
DR PDB; 3ZWB; X-ray; 3.10 A; A/B=1-722.
DR PDB; 3ZWC; X-ray; 2.30 A; A/B=1-722.
DR PDB; 5MGB; X-ray; 2.80 A; A/B=1-722.
DR PDB; 5OMO; X-ray; 2.49 A; A/B=1-722.
DR PDB; 6Z5F; X-ray; 2.25 A; AAA/BBB=1-722.
DR PDB; 6Z5O; X-ray; 1.70 A; AAA=1-722.
DR PDB; 6Z5V; X-ray; 2.33 A; AAA/BBB=1-722.
DR PDB; 6ZIB; X-ray; 2.70 A; AAA/BBB=1-722.
DR PDB; 6ZIC; X-ray; 2.20 A; AAA/BBB=1-722.
DR PDBsum; 1ZCJ; -.
DR PDBsum; 2X58; -.
DR PDBsum; 3ZW8; -.
DR PDBsum; 3ZW9; -.
DR PDBsum; 3ZWA; -.
DR PDBsum; 3ZWB; -.
DR PDBsum; 3ZWC; -.
DR PDBsum; 5MGB; -.
DR PDBsum; 5OMO; -.
DR PDBsum; 6Z5F; -.
DR PDBsum; 6Z5O; -.
DR PDBsum; 6Z5V; -.
DR PDBsum; 6ZIB; -.
DR PDBsum; 6ZIC; -.
DR AlphaFoldDB; P07896; -.
DR SMR; P07896; -.
DR IntAct; P07896; 7.
DR MINT; P07896; -.
DR STRING; 10116.ENSRNOP00000002410; -.
DR ChEMBL; CHEMBL3232; -.
DR SwissLipids; SLP:000001144; -.
DR iPTMnet; P07896; -.
DR PhosphoSitePlus; P07896; -.
DR PaxDb; 10116-ENSRNOP00000002410; -.
DR Ensembl; ENSRNOT00000002410.5; ENSRNOP00000002410.2; ENSRNOG00000001770.5.
DR GeneID; 171142; -.
DR KEGG; rno:171142; -.
DR UCSC; RGD:621441; rat.
DR AGR; RGD:621441; -.
DR CTD; 1962; -.
DR RGD; 621441; Ehhadh.
DR eggNOG; KOG1683; Eukaryota.
DR GeneTree; ENSGT00940000157516; -.
DR HOGENOM; CLU_009834_16_3_1; -.
DR InParanoid; P07896; -.
DR OMA; YNGAAMG; -.
DR OrthoDB; 622692at2759; -.
DR PhylomeDB; P07896; -.
DR TreeFam; TF316708; -.
DR BRENDA; 4.2.1.17; 5301.
DR Reactome; R-RNO-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR SABIO-RK; P07896; -.
DR UniPathway; UPA00659; -.
DR EvolutionaryTrace; P07896; -.
DR PRO; PR:P07896; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001770; Expressed in liver and 17 other cell types or tissues.
DR Genevisible; P07896; RN.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IDA:UniProtKB.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0016863; F:intramolecular oxidoreductase activity, transposing C=C bonds; IDA:UniProtKB.
DR GO; GO:0016509; F:long-chain-3-hydroxyacyl-CoA dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IDA:UniProtKB.
DR CDD; cd06558; crotonase-like; 1.
DR Gene3D; 1.10.1040.50; -; 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:SF9; PEROXISOMAL BIFUNCTIONAL ENZYME; 1.
DR Pfam; PF00725; 3HCDH; 2.
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 3D-structure; Acetylation; Direct protein sequencing;
KW Fatty acid metabolism; Isomerase; Lipid metabolism; Lyase;
KW Multifunctional enzyme; NAD; Oxidoreductase; Peroxisome; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..722
FT /note="Peroxisomal bifunctional enzyme"
FT /id="PRO_0000109249"
FT REGION 1..281
FT /note="Enoyl-CoA hydratase / isomerase"
FT REGION 282..571
FT /note="3-hydroxyacyl-CoA dehydrogenase"
FT MOTIF 720..722
FT /note="Microbody targeting signal"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 103
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 123
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="Blocked amino end (Ala)"
FT MOD_RES 38
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 173
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 173
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 182
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 190
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 190
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 218
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 218
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 241
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 249
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 253
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 275
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 275
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 279
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 289
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 330
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 345
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q08426"
FT MOD_RES 359
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 463
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 531
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 547
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08426"
FT MOD_RES 576
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 583
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q08426"
FT MOD_RES 583
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 590
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 590
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 709
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 709
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT MOD_RES 721
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBM2"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3ZWC"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:3ZWA"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:3ZWC"
FT TURN 19..22
FT /evidence="ECO:0007829|PDB:3ZWC"
FT HELIX 26..40
FT /evidence="ECO:0007829|PDB:3ZWC"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:3ZWC"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3ZWC"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:5OMO"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:3ZWC"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:3ZWC"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:3ZWC"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:3ZWC"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:3ZWC"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:3ZWC"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:3ZWC"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:3ZWC"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:3ZWC"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:3ZWC"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:3ZWA"
FT HELIX 159..164
FT /evidence="ECO:0007829|PDB:3ZWC"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:3ZWC"
FT HELIX 176..187
FT /evidence="ECO:0007829|PDB:3ZWC"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:5MGB"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:3ZWC"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:3ZWC"
FT HELIX 208..222
FT /evidence="ECO:0007829|PDB:3ZWC"
FT HELIX 227..241
FT /evidence="ECO:0007829|PDB:3ZWC"
FT HELIX 244..259
FT /evidence="ECO:0007829|PDB:3ZWC"
FT HELIX 262..272
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 273..278
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:3ZW9"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 306..316
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 329..352
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:3ZW9"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 385..398
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 414..418
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT STRAND 427..432
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 452..464
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT STRAND 468..472
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT TURN 476..479
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 480..496
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 501..511
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 517..524
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 526..535
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT STRAND 538..541
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 560..566
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT TURN 572..575
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT STRAND 576..583
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT STRAND 589..591
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 593..605
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 615..635
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT STRAND 638..640
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 642..652
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 657..659
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 662..669
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 671..684
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 689..691
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 695..702
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 708..710
FT /evidence="ECO:0007829|PDB:1ZCJ"
FT HELIX 711..715
FT /evidence="ECO:0007829|PDB:1ZCJ"
SQ SEQUENCE 722 AA; 78658 MW; 76ACC709C5F23E86 CRC64;
MAEYLRLPHS LAMIRLCNPP VNAVSPTVIR EVRNGLQKAG SDHTVKAIVI CGANGNFCAG
ADIHGFSAFT PGLALGSLVD EIQRYQKPVL AAIQGVALGG GLELALGCHY RIANAKARVG
LPEVTLGILP GARGTQLLPR VVGVPVALDL ITSGKYLSAD EALRLGILDA VVKSDPVEEA
IKFAQKIIDK PIEPRRIFNK PVPSLPNMDS VFAEAIAKVR KQYPGVLAPE TCVRSIQASV
KHPYEVGIKE EEKLFMYLRA SGQAKALQYA FFAEKSANKW STPSGASWKT ASAQPVSSVG
VLGLGTMGRG IAISFARVGI SVVAVESDPK QLDAAKKIIT FTLEKEASRA HQNGQASAKP
KLRFSSSTKE LSTVDLVVEA VFEDMNLKKK VFAELSALCK PGAFLCTNTS ALNVDDIASS
TDRPQLVIGT HFFSPAHVMR LLEVIPSRYS SPTTIATVMS LSKKIGKIGV VVGNCYGFVG
NRMLAPYYNQ GFFLLEEGSK PEDVDGVLEE FGFKMGPFRV SDLAGLDVGW KIRKGQGLTG
PSLPPGTPVR KRGNSRYSPL GDMLCEAGRF GQKTGKGWYQ YDKPLGRIHK PDPWLSTFLS
QYREVHHIEQ RTISKEEILE RCLYSLINEA FRILEEGMAA RPEHIDVIYL HGYGWPRHKG
GPMFYAASVG LPTVLEKLQK YYRQNPDIPQ LEPSDYLRRL VAQGSPPLKE WQSLAGPHGS
KL
//
