DHB4_MOUSE
ID DHB4_MOUSE Reviewed; 735 AA.
AC P51660; Q9DBM3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Peroxisomal multifunctional enzyme type 2 {ECO:0000305};
DE Short=MFE-2;
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase 4;
DE Short=17-beta-HSD 4;
DE AltName: Full=D-bifunctional protein;
DE Short=DBP;
DE AltName: Full=Multifunctional protein 2;
DE Short=MFP-2 {ECO:0000303|PubMed:17442273};
DE Contains:
DE RecName: Full=(3R)-hydroxyacyl-CoA dehydrogenase;
DE EC=1.1.1.n12 {ECO:0000250|UniProtKB:P51659};
DE Contains:
DE RecName: Full=Enoyl-CoA hydratase 2;
DE EC=4.2.1.107 {ECO:0000269|PubMed:17442273};
DE EC=4.2.1.119 {ECO:0000250|UniProtKB:P51659};
DE AltName: Full=3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase;
GN Name=Hsd17b4 {ECO:0000312|MGI:MGI:105089}; Synonyms=Edh17b4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8547180; DOI=10.1016/0960-0760(95)00204-9;
RA Normand T., Husen B., Leenders F., Pelczar H., Baert J.-L., Begue A.,
RA Flourens A.C., Adamski J., de Launoit Y.;
RT "Molecular characterization of mouse 17 beta-hydroxysteroid dehydrogenase
RT IV.";
RL J. Steroid Biochem. Mol. Biol. 55:541-548(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Amnion, Liver, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17442273; DOI=10.1016/j.bbrc.2007.03.198;
RA Dirkx R., Meyhi E., Asselberghs S., Reddy J., Baes M., Van Veldhoven P.P.;
RT "Beta-oxidation in hepatocyte cultures from mice with peroxisomal gene
RT knockouts.";
RL Biochem. Biophys. Res. Commun. 357:718-723(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-46; LYS-57; LYS-68; LYS-84;
RP LYS-275; LYS-355; LYS-423; LYS-578; LYS-662 AND LYS-724, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-46; LYS-564 AND LYS-706, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Bifunctional enzyme acting on the peroxisomal beta-oxidation
CC pathway for fatty acids (PubMed:17442273). Catalyzes the formation of
CC 3-ketoacyl-CoA intermediates from straight-chain, 2-methyl-branched-
CC chain fatty acids bile acid intermediates. With EHHADH, catalyzes the
CC hydration of trans-2-enoyl-CoA and the dehydrogenation of 3-
CC hydroxyacyl-CoA, but with opposite chiral specificity (By similarity).
CC {ECO:0000250|UniProtKB:P51659, ECO:0000269|PubMed:17442273}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:32711, ChEBI:CHEBI:15378, ChEBI:CHEBI:57319,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726;
CC EC=1.1.1.n12; Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32712;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-
CC cholestan-26-oyl-CoA = (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-
CC cholest-24-en-26-oyl-CoA + H2O; Xref=Rhea:RHEA:18933,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:59807, ChEBI:CHEBI:59879;
CC EC=4.2.1.107; Evidence={ECO:0000269|PubMed:17442273};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18935;
CC Evidence={ECO:0000269|PubMed:17442273};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:26526, ChEBI:CHEBI:15377, ChEBI:CHEBI:57319,
CC ChEBI:CHEBI:58856; EC=4.2.1.119;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26527;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-octenoyl-CoA + H2O = (3R)-hydroxyoctanoyl-CoA;
CC Xref=Rhea:RHEA:40187, ChEBI:CHEBI:15377, ChEBI:CHEBI:62242,
CC ChEBI:CHEBI:74279; Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40188;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyoctanoyl-CoA + NAD(+) = 3-oxooctanoyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:40191, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:62619, ChEBI:CHEBI:74279;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40192;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyhexadecanoyl-CoA + NAD(+) = 3-oxohexadecanoyl-CoA
CC + H(+) + NADH; Xref=Rhea:RHEA:40243, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57349, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:74278; Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40244;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-hexadecenedioyl-CoA + H2O = (3R)-hydroxyhexadecanedioyl-
CC CoA; Xref=Rhea:RHEA:40255, ChEBI:CHEBI:15377, ChEBI:CHEBI:77075,
CC ChEBI:CHEBI:77079; Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40256;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyhexadecanedioyl-CoA + NAD(+) = 3-
CC oxohexadecanedioyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:40263,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:77079, ChEBI:CHEBI:77081;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40264;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyhexadecanoyl-CoA = (2E)-hexadecenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:39159, ChEBI:CHEBI:15377, ChEBI:CHEBI:61526,
CC ChEBI:CHEBI:74278; Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:39161;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-3-hydroxydecanoyl-CoA = (2E)-decenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:45992, ChEBI:CHEBI:15377, ChEBI:CHEBI:61406,
CC ChEBI:CHEBI:74272; Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45994;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-3-hydroxydecanoyl-CoA + NAD(+) = 3-oxodecanoyl-CoA + H(+)
CC + NADH; Xref=Rhea:RHEA:45832, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:62548, ChEBI:CHEBI:74272;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45833;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-
CC cholestan-26-oyl-CoA + NAD(+) = 3alpha,7alpha,12alpha-trihydroxy-24-
CC oxo-5beta-cholestan-26-oyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:47088,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58507, ChEBI:CHEBI:59807;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47089;
CC Evidence={ECO:0000250|UniProtKB:P51659};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000269|PubMed:17442273}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P51659}.
CC -!- INTERACTION:
CC P51660; P42858: HTT; Xeno; NbExp=15; IntAct=EBI-8328056, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:P97852}.
CC -!- TISSUE SPECIFICITY: Present in many tissues with highest concentrations
CC in liver and kidney.
CC -!- MISCELLANEOUS: The protein is found both as a full-length peptide and
CC in a cleaved version. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; X89998; CAA62015.1; -; mRNA.
DR EMBL; AK004866; BAB23627.1; -; mRNA.
DR EMBL; AK088381; BAC40317.1; -; mRNA.
DR EMBL; AK166801; BAE39029.1; -; mRNA.
DR EMBL; AK167060; BAE39222.1; -; mRNA.
DR EMBL; AK169077; BAE40862.1; -; mRNA.
DR EMBL; BC022175; AAH22175.1; -; mRNA.
DR CCDS; CCDS29242.1; -.
DR RefSeq; NP_032318.2; NM_008292.4.
DR AlphaFoldDB; P51660; -.
DR SMR; P51660; -.
DR BioGRID; 200435; 23.
DR IntAct; P51660; 2.
DR MINT; P51660; -.
DR STRING; 10090.ENSMUSP00000025385; -.
DR ChEMBL; CHEMBL3621031; -.
DR iPTMnet; P51660; -.
DR PhosphoSitePlus; P51660; -.
DR SwissPalm; P51660; -.
DR EPD; P51660; -.
DR jPOST; P51660; -.
DR MaxQB; P51660; -.
DR PaxDb; P51660; -.
DR PeptideAtlas; P51660; -.
DR PRIDE; P51660; -.
DR ProteomicsDB; 279527; -.
DR Antibodypedia; 13742; 422 antibodies from 34 providers.
DR DNASU; 15488; -.
DR Ensembl; ENSMUST00000025385; ENSMUSP00000025385; ENSMUSG00000024507.
DR GeneID; 15488; -.
DR KEGG; mmu:15488; -.
DR UCSC; uc008eww.2; mouse.
DR CTD; 3295; -.
DR MGI; MGI:105089; Hsd17b4.
DR VEuPathDB; HostDB:ENSMUSG00000024507; -.
DR eggNOG; ENOG502QPX4; Eukaryota.
DR GeneTree; ENSGT00940000158343; -.
DR HOGENOM; CLU_010194_18_4_1; -.
DR InParanoid; P51660; -.
DR OMA; LITEMWK; -.
DR OrthoDB; 1120431at2759; -.
DR PhylomeDB; P51660; -.
DR TreeFam; TF105656; -.
DR Reactome; R-MMU-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-MMU-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-MMU-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-MMU-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR UniPathway; UPA00659; -.
DR BioGRID-ORCS; 15488; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Hsd17b4; mouse.
DR PRO; PR:P51660; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P51660; protein.
DR Bgee; ENSMUSG00000024507; Expressed in saccule of membranous labyrinth and 286 other tissues.
DR Genevisible; P51660; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0005777; C:peroxisome; IDA:MGI.
DR GO; GO:0106386; F:(3R)-hydroxyacyl-CoA dehydrogenase (NAD) activity; IEA:RHEA.
DR GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; ISO:MGI.
DR GO; GO:0018812; F:3-hydroxyacyl-CoA dehydratase activity; ISO:MGI.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0033989; F:3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; ISS:UniProtKB.
DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016508; F:long-chain-enoyl-CoA hydratase activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0008209; P:androgen metabolic process; ISO:MGI.
DR GO; GO:0008210; P:estrogen metabolic process; ISO:MGI.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:MGI.
DR GO; GO:0036112; P:medium-chain fatty-acyl-CoA metabolic process; ISO:MGI.
DR GO; GO:0060009; P:Sertoli cell development; IMP:MGI.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IMP:MGI.
DR GO; GO:0036111; P:very long-chain fatty-acyl-CoA metabolic process; ISO:MGI.
DR Gene3D; 3.30.1050.10; -; 1.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR003033; SCP2_sterol-bd_dom.
DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR Pfam; PF02036; SCP2; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF54637; SSF54637; 2.
DR SUPFAM; SSF55718; SSF55718; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Fatty acid metabolism; Isomerase; Lipid metabolism; Lyase;
KW NAD; Oxidoreductase; Peroxisome; Phosphoprotein; Reference proteome.
FT CHAIN 1..735
FT /note="Peroxisomal multifunctional enzyme type 2"
FT /id="PRO_0000054584"
FT CHAIN 1..311
FT /note="(3R)-hydroxyacyl-CoA dehydrogenase"
FT /id="PRO_0000400084"
FT CHAIN 312..735
FT /note="Enoyl-CoA hydratase 2"
FT /id="PRO_0000400085"
FT DOMAIN 483..599
FT /note="MaoC-like"
FT DOMAIN 623..735
FT /note="SCP2"
FT REGION 1..305
FT /note="(3R)-hydroxyacyl-CoA dehydrogenase"
FT REGION 321..621
FT /note="Enoyl-CoA hydratase 2"
FT MOTIF 733..735
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 13..37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 75..76
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 164..168
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 196..199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 405..406
FT /ligand="(3R)-3-hydroxydecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:74272"
FT /evidence="ECO:0000250"
FT BINDING 434
FT /ligand="(3R)-3-hydroxydecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:74272"
FT /evidence="ECO:0000250"
FT BINDING 509..514
FT /ligand="(3R)-3-hydroxydecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:74272"
FT /evidence="ECO:0000250"
FT BINDING 532
FT /ligand="(3R)-3-hydroxydecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:74272"
FT /evidence="ECO:0000250"
FT BINDING 562
FT /ligand="(3R)-3-hydroxydecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:74272"
FT /evidence="ECO:0000250"
FT BINDING 705
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 723
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 46
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 46
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51659"
FT MOD_RES 57
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 68
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 84
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 265
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51659"
FT MOD_RES 275
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51659"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 355
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 423
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 564
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 578
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 662
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 668
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51659"
FT MOD_RES 706
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 724
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 17
FT /note="A -> P (in Ref. 1; CAA62015)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="P -> L (in Ref. 1; CAA62015)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 735 AA; 79482 MW; AD7804FE93EB9BA8 CRC64;
MASPLRFDGR VVLVTGAGGG LGRAYALAFA ERGALVIVND LGGDFKGIGK GSSAADKVVA
EIRRKGGKAV ANYDSVEAGE KLVKTALDTF GRIDVVVNNA GILRDRSFSR ISDEDWDIIH
RVHLRGSFQV TRAAWDHMKK QNYGRILMTS SASGIYGNFG QANYSAAKLG ILGLCNTLAI
EGRKNNIHCN TIAPNAGSRM TETVLPEDLV EALKPEYVAP LVLWLCHESC EENGGLFEVG
AGWIGKLRWE RTLGAIVRKR NQPMTPEAVR DNWEKICDFS NASKPQTIQE STGGIVEVLH
KVDSEGISPN RTSHAAPAAT SGFVGAVGHK LPSFSSSYTE LQSIMYALGV GASVKNPKDL
KFVYEGSADF SCLPTFGVIV AQKSMMNGGL AEVPGLSFNF AKALHGEQYL ELYKPLPRSG
ELKCEAVIAD ILDKGSGVVI VMDVYSYSGK ELICYNQFSV FVVGSGGFGG KRTSEKLKAA
VAVPNRPPDA VLRDATSLNQ AALYRLSGDW NPLHIDPDFA SVAGFEKPIL HGLCTFGFSA
RHVLQQFADN DVSRFKAIKV RFAKPVYPGQ TLQTEMWKEG NRIHFQTKVH ETGDVVISNA
YVDLVPASGV STQTPSEGGE LQSALVFGEI GRRLKSVGRE VVKKANAVFE WHITKGGTVA
AKWTIDLKSG SGEVYQGPAK GSADVTIIIS DEDFMEVVFG KLDPQKAFFS GRLKARGNIM
LSQKLQMILK DYAKL
