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Database: UniProt
Entry: A0A2R9C5M2_PANPA
LinkDB: A0A2R9C5M2_PANPA
Original site: A0A2R9C5M2_PANPA 
ID   A0A2R9C5M2_PANPA        Unreviewed;       723 AA.
AC   A0A2R9C5M2;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Peroxisomal bifunctional enzyme {ECO:0000256|ARBA:ARBA00039632};
DE            EC=1.1.1.35 {ECO:0000256|ARBA:ARBA00013000};
DE            EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
DE            EC=5.3.3.8 {ECO:0000256|ARBA:ARBA00012064};
DE   AltName: Full=Multifunctional enzyme 1 {ECO:0000256|ARBA:ARBA00042031};
GN   Name=EHHADH {ECO:0000313|Ensembl:ENSPPAP00000037205.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000037205.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000037205.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000037205.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00036989};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40260;
CC         Evidence={ECO:0000256|ARBA:ARBA00036989};
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:0000256|ARBA:ARBA00036472};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31121;
CC         Evidence={ECO:0000256|ARBA:ARBA00036472};
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:0000256|ARBA:ARBA00036656};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45753;
CC         Evidence={ECO:0000256|ARBA:ARBA00036656};
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:0000256|ARBA:ARBA00036353};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45737;
CC         Evidence={ECO:0000256|ARBA:ARBA00036353};
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:0000256|ARBA:ARBA00035863};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:49934;
CC         Evidence={ECO:0000256|ARBA:ARBA00035863};
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:0000256|ARBA:ARBA00036570};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:47466;
CC         Evidence={ECO:0000256|ARBA:ARBA00036570};
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:0000256|ARBA:ARBA00001391};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31188;
CC         Evidence={ECO:0000256|ARBA:ARBA00001391};
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:0000256|ARBA:ARBA00035760};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31193;
CC         Evidence={ECO:0000256|ARBA:ARBA00035760};
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:0000256|ARBA:ARBA00036386};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40268;
CC         Evidence={ECO:0000256|ARBA:ARBA00036386};
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:0000256|ARBA:ARBA00000193};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31160;
CC         Evidence={ECO:0000256|ARBA:ARBA00000193};
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:0000256|ARBA:ARBA00000469};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31165;
CC         Evidence={ECO:0000256|ARBA:ARBA00000469};
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:0000256|ARBA:ARBA00036370};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30549;
CC         Evidence={ECO:0000256|ARBA:ARBA00036370};
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:0000256|ARBA:ARBA00036336};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45749;
CC         Evidence={ECO:0000256|ARBA:ARBA00036336};
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:0000256|ARBA:ARBA00035949};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45229;
CC         Evidence={ECO:0000256|ARBA:ARBA00035949};
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:0000256|ARBA:ARBA00036547};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22433;
CC         Evidence={ECO:0000256|ARBA:ARBA00036547};
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:0000256|ARBA:ARBA00035959};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45901;
CC         Evidence={ECO:0000256|ARBA:ARBA00035959};
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:0000256|ARBA:ARBA00035909};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20725;
CC         Evidence={ECO:0000256|ARBA:ARBA00035909};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000256|RuleBase:RU003707}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the 3-hydroxyacyl-CoA
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00038365}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family. {ECO:0000256|ARBA:ARBA00008750}.
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DR   EMBL; AJFE02018420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02018421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02018422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02018423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003806653.1; XM_003806605.1.
DR   AlphaFoldDB; A0A2R9C5M2; -.
DR   STRING; 9597.ENSPPAP00000037205; -.
DR   Ensembl; ENSPPAT00000060104.1; ENSPPAP00000037205.1; ENSPPAG00000041357.1.
DR   GeneID; 100985141; -.
DR   KEGG; pps:100985141; -.
DR   CTD; 1962; -.
DR   GeneTree; ENSGT00940000157516; -.
DR   OrthoDB; 622692at2759; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000240080; Chromosome 3.
DR   Bgee; ENSPPAG00000041357; Expressed in liver and 6 other cell types or tissues.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR   GO; GO:0016509; F:long-chain-3-hydroxyacyl-CoA dehydrogenase activity; IEA:Ensembl.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240080}.
FT   DOMAIN          300..475
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          478..582
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   DOMAIN          619..710
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   723 AA;  79466 MW;  1D089B2F2A09E82B CRC64;
     MAEYTRLHNA LALIRLRNPP VNAISTTLLR DIKEGLQKAV IDHTIKAIVI CGAEGKFSAG
     ADIRGFSAPR TFGLTLGHVV DEIQRNEKPV VAAIQGMAFG GGLELALGCH YRIAHAEAQV
     GLPEVTLGLL PGARGTQLLP RLTGVPAALD LITSGRRILA DEALKLGILD KVVNSDPVEE
     AIRFAQRVSD QPLESRRLCN KPIQSLPYMD SIFSEALLKM RRQHPGCLAQ EACVRAVQAA
     VQYPYEVGIK KEEELFLYLL QSGQARALQH AFFAERKANK WSTPSGASWK TASARPVSSV
     GVVGLGTMGR GIVISFARAR IPVIAVDSDK NQLAIANKMI TSVLEKEASK MQQSGHPWSG
     PKPRLTSSMK ELGGVDLVIE AVFEEMSLKK QVFAELSAVC KPEAFLCTNT SALDVDEIAS
     STDRPHLVIG THFFSPAHVM KLLEVIPSQY SSPTTIATVM NLSKKIKKIG VVVGNCFGFV
     GNRMLNPYYN QAYFLLEEGS KPEEVDQVLE EFGFKMGPFR VSDLAGLDVG WKSRKGQGLT
     GPTLPPGTPA RKRGNRRYCP IPDVLCELGR FGQKTGKGWY QYDKPLGRIH KPDPWLSKFL
     SQYRETHHIE PRTISQDEIL ERCLYSLINE AFCILGEGIA ASPEHIDVVY LHGYGWPRHK
     GGPMFYASTV GLPTVLEKLQ KYYRQNPDIP QLEPSDYLKK LASQGNPPLK EWQSLAGSPS
     SKL
//
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