LOCUS       NP_598290                722 aa            linear   ROD 10-APR-2024
DEFINITION  peroxisomal bifunctional enzyme [Rattus norvegicus].
ACCESSION   NP_598290
VERSION     NP_598290.1
DBSOURCE    REFSEQ: accession NM_133606.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Sridhar,S., Kiema,T.R., Schmitz,W., Widersten,M. and Wierenga,R.K.
  TITLE     Structural enzymology studies with the substrate
            3S-hydroxybutanoyl-CoA: bifunctional MFE1 is a less efficient
            dehydrogenase than monofunctional HAD
  JOURNAL   FEBS Open Bio 14 (4), 655-674 (2024)
   PUBMED   38458818
  REMARK    GeneRIF: Structural enzymology studies with the substrate
            3S-hydroxybutanoyl-CoA: bifunctional MFE1 is a less efficient
            dehydrogenase than monofunctional HAD.
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Kasaragod,P., Schmitz,W., Hiltunen,J.K. and Wierenga,R.K.
  TITLE     The isomerase and hydratase reaction mechanism of the crotonase
            active site of the multifunctional enzyme (type-1), as deduced from
            structures of complexes with 3S-hydroxy-acyl-CoA
  JOURNAL   FEBS J 280 (13), 3160-3175 (2013)
   PUBMED   23351063
  REMARK    GeneRIF: Data from crystallographic binding studies suggest that a
            catalytic water molecule, bound between two catalytic glutamates
            (Glu103/Glu123), plays important role in enoyl-CoA isomerase and
            enoyl-CoA hydratase reaction mechanisms of MFE1.
REFERENCE   3  (residues 1 to 722)
  AUTHORS   Kasaragod,P., Venkatesan,R., Kiema,T.R., Hiltunen,J.K. and
            Wierenga,R.K.
  TITLE     Crystal structure of liganded rat peroxisomal multifunctional
            enzyme type 1: a flexible molecule with two interconnected active
            sites
  JOURNAL   J Biol Chem 285 (31), 24089-24098 (2010)
   PUBMED   20463028
  REMARK    GeneRIF: liganded rat peroxisomal multifunctional enzyme type 1 is
            a flexible molecule with two interconnected active sites [rpMFE1]
REFERENCE   4  (residues 1 to 722)
  AUTHORS   Ghosh,D. and Berg,J.M.
  TITLE     A proteome-wide perspective on peroxisome targeting signal
            1(PTS1)-Pex5p affinities
  JOURNAL   J Am Chem Soc 132 (11), 3973-3979 (2010)
   PUBMED   20178365
REFERENCE   5  (residues 1 to 722)
  AUTHORS   Zhao,S., Xu,W., Jiang,W., Yu,W., Lin,Y., Zhang,T., Yao,J., Zhou,L.,
            Zeng,Y., Li,H., Li,Y., Shi,J., An,W., Hancock,S.M., He,F., Qin,L.,
            Chin,J., Yang,P., Chen,X., Lei,Q., Xiong,Y. and Guan,K.L.
  TITLE     Regulation of cellular metabolism by protein lysine acetylation
  JOURNAL   Science 327 (5968), 1000-1004 (2010)
   PUBMED   20167786
REFERENCE   6  (residues 1 to 722)
  AUTHORS   Chen,G.L., Balfe,A., Erwa,W., Hoefler,G., Gaertner,J., Aikawa,J.
            and Chen,W.W.
  TITLE     Import of human bifunctional enzyme into peroxisomes of human
            hepatoma cells in vitro
  JOURNAL   Biochem Biophys Res Commun 178 (3), 1084-1091 (1991)
   PUBMED   1651711
REFERENCE   7  (residues 1 to 722)
  AUTHORS   Palosaari,P.M. and Hiltunen,J.K.
  TITLE     Peroxisomal bifunctional protein from rat liver is a trifunctional
            enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA
            dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities
  JOURNAL   J Biol Chem 265 (5), 2446-2449 (1990)
   PUBMED   2303409
REFERENCE   8  (residues 1 to 722)
  AUTHORS   Litwin,J.A., Volkl,A., Muller-Hocker,J. and Fahimi,H.D.
  TITLE     Immunocytochemical demonstration of peroxisomal enzymes in human
            kidney biopsies
  JOURNAL   Virchows Arch B Cell Pathol Incl Mol Pathol 54 (4), 207-213 (1988)
   PUBMED   2895531
REFERENCE   9  (residues 1 to 722)
  AUTHORS   Ishii,N., Hijikata,M., Osumi,T. and Hashimoto,T.
  TITLE     Structural organization of the gene for rat enoyl-CoA
            hydratase:3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme
  JOURNAL   J Biol Chem 262 (17), 8144-8150 (1987)
   PUBMED   3036802
REFERENCE   10 (residues 1 to 722)
  AUTHORS   Osumi,T., Ishii,N., Hijikata,M., Kamijo,K., Ozasa,H., Furuta,S.,
            Miyazawa,S., Kondo,K., Inoue,K., Kagamiyama,H. et al.
  TITLE     Molecular cloning and nucleotide sequence of the cDNA for rat
            peroxisomal enoyl-CoA: hydratase-3-hydroxyacyl-CoA dehydrogenase
            bifunctional enzyme
  JOURNAL   J Biol Chem 260 (15), 8905-8910 (1985)
   PUBMED   4019459
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: K03249.1, BC089777.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..722
                     /product="peroxisomal bifunctional enzyme"
                     /EC_number="1.1.1.35"
                     /EC_number="5.3.3.8"
                     /EC_number="4.2.1.17"
                     /note="peroxisomal bifunctional enzyme type 1; peroxisomal
                     enoyl-CoA/hydrotase-3-hydroxyacyl-CoA; enoyl-CoA,
                     hydratase/3-hydroxyacyl CoA dehydrogenase; L-specific
                     bifunctional protein; multifunctional enzyme type 1;
                     enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A
                     dehydrogenase; multifunctional enzyme 1; multifunctional
                     protein 1"
                     /calculated_mol_wt=78527
     Region          1..281
                     /region_name="Enoyl-CoA hydratase / isomerase"
                     /note="propagated from UniProtKB/Swiss-Prot (P07896.2)"
     Site            2
                     /site_type="blocked"
                     /note="Blocked amino end (Ala); propagated from
                     UniProtKB/Swiss-Prot (P07896.2)"
     Region          20..706
                     /region_name="fadJ"
                     /note="fatty acid oxidation complex subunit alpha FadJ;
                     PRK11154"
                     /db_xref="CDD:236864"
     Site            103
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P07896.2)"
     Site            123
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P07896.2)"
     Site            173
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9DBM2; propagated from
                     UniProtKB/Swiss-Prot (P07896.2)"
     Site            190
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9DBM2; propagated from
                     UniProtKB/Swiss-Prot (P07896.2)"
     Site            218
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9DBM2; propagated from
                     UniProtKB/Swiss-Prot (P07896.2)"
     Site            249
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBM2; propagated from
                     UniProtKB/Swiss-Prot (P07896.2)"
     Site            275
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9DBM2; propagated from
                     UniProtKB/Swiss-Prot (P07896.2)"
     Region          282..571
                     /region_name="3-hydroxyacyl-CoA dehydrogenase"
                     /note="propagated from UniProtKB/Swiss-Prot (P07896.2)"
     Site            345
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q08426; propagated from
                     UniProtKB/Swiss-Prot (P07896.2)"
     Site            359
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBM2; propagated from
                     UniProtKB/Swiss-Prot (P07896.2)"
     Site            463
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBM2; propagated from
                     UniProtKB/Swiss-Prot (P07896.2)"
     Site            547
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q08426; propagated from
                     UniProtKB/Swiss-Prot (P07896.2)"
     Site            583
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q08426; propagated from
                     UniProtKB/Swiss-Prot (P07896.2)"
     Site            590
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9DBM2; propagated from
                     UniProtKB/Swiss-Prot (P07896.2)"
     Site            709
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9DBM2; propagated from
                     UniProtKB/Swiss-Prot (P07896.2)"
     Region          720..722
                     /region_name="Microbody targeting signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P07896.2)"
     CDS             1..722
                     /gene="Ehhadh"
                     /gene_synonym="Lbp; MEF; Mfe; Mfe1; MFP1; Pbe; Pbfe;
                     pe-CoA; perMFE-1"
                     /coded_by="NM_133606.3:22..2190"
                     /db_xref="GeneID:171142"
                     /db_xref="RGD:621441"
ORIGIN      
        1 maeylrlphs lamirlcnpp vnavsptvir evrnglqkag sdhtvkaivi cgangnfcag
       61 adihgfsaft pglalgslvd eiqryqkpvl aaiqgvalgg glelalgchy rianakarvg
      121 lpevtlgilp gargtqllpr vvgvpvaldl itsgkylsad ealrlgilda vvksdpveea
      181 ikfaqkiidk pieprrifnk pvpslpnmds vfaeaiakvr kqypgvlape tcvrsiqasv
      241 khpyevgike eeklfmylra sgqakalqya ffaeksankw stpsgaswkt asaqpvssvg
      301 vlglgtmgrg iaisfarvgi svvavesdpk qldaakkiit ftlekeasra hqngqasakp
      361 klrfssstke lstvdlvvea vfedmnlkkk vfaelsalck pgaflctnts alnvddiass
      421 tdrpqlvigt hffspahvmr llevipsrys spttiatvms lskkigkigv vvgncygfvg
      481 nrmlapyynq gfflleegsk pedvdgvlee fgfkmgpfrv sdlagldvgw kirkgqgltg
      541 pslppgtpvr krgnsryspl gdmlceagrf gqktgkgwyq ydkplgrihk pdpwlstfls
      601 qyrevhhieq rtiskeeile rclyslinea frileegmaa rpehidviyl hgygwprhkg
      661 gpmfyaasvg lptvleklqk yyrqnpdipq lepsdylrrl vaqgspplke wqslagphgs
      721 kl
//
