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P07896

- ECHP_RAT

UniProt

P07896 - ECHP_RAT

Protein

Peroxisomal bifunctional enzyme

Gene

Ehhadh

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.
    (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.
    (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.

    Enzyme regulationi

    Enzyme activity enhanced by acetylation.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei100 – 1001Substrate; via amide nitrogenBy similarity
    Sitei103 – 1031Important for catalytic activityBy similarity
    Sitei123 – 1231Important for catalytic activityBy similarity

    GO - Molecular functioni

    1. 3-hydroxyacyl-CoA dehydrogenase activity Source: RGD
    2. coenzyme binding Source: InterPro
    3. dodecenoyl-CoA delta-isomerase activity Source: UniProtKB-EC
    4. enoyl-CoA hydratase activity Source: UniProtKB-EC
    5. enzyme binding Source: UniProtKB

    GO - Biological processi

    1. fatty acid beta-oxidation Source: UniProtKB-UniPathway
    2. internal protein amino acid acetylation Source: UniProtKB

    Keywords - Molecular functioni

    Isomerase, Lyase, Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    SABIO-RKP07896.
    UniPathwayiUPA00659.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisomal bifunctional enzyme
    Short name:
    PBE
    Short name:
    PBFE
    Including the following 2 domains:
    Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase (EC:4.2.1.17, EC:5.3.3.8)
    3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.35)
    Gene namesi
    Name:Ehhadh
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 11

    Organism-specific databases

    RGDi621441. Ehhadh.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. mitochondrion Source: Ensembl
    3. nucleus Source: Ensembl
    4. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 722722Peroxisomal bifunctional enzymePRO_0000109249Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21Blocked amino end (Ala)
    Modified residuei38 – 381N6-succinyllysineBy similarity
    Modified residuei173 – 1731N6-acetyllysine; alternateBy similarity
    Modified residuei173 – 1731N6-succinyllysine; alternateBy similarity
    Modified residuei182 – 1821N6-succinyllysineBy similarity
    Modified residuei190 – 1901N6-acetyllysine; alternateBy similarity
    Modified residuei190 – 1901N6-succinyllysine; alternateBy similarity
    Modified residuei218 – 2181N6-acetyllysine; alternateBy similarity
    Modified residuei218 – 2181N6-succinyllysine; alternateBy similarity
    Modified residuei241 – 2411N6-succinyllysineBy similarity
    Modified residuei249 – 2491N6-acetyllysineBy similarity
    Modified residuei253 – 2531N6-succinyllysineBy similarity
    Modified residuei275 – 2751N6-acetyllysine; alternateBy similarity
    Modified residuei275 – 2751N6-succinyllysine; alternateBy similarity
    Modified residuei279 – 2791N6-succinyllysineBy similarity
    Modified residuei289 – 2891N6-succinyllysineBy similarity
    Modified residuei330 – 3301N6-succinyllysineBy similarity
    Modified residuei345 – 3451N6-acetyllysineBy similarity
    Modified residuei359 – 3591N6-acetyllysineBy similarity
    Modified residuei463 – 4631N6-acetyllysineBy similarity
    Modified residuei531 – 5311N6-succinyllysineBy similarity
    Modified residuei576 – 5761N6-succinyllysineBy similarity
    Modified residuei583 – 5831N6-acetyllysine; alternateBy similarity
    Modified residuei583 – 5831N6-succinyllysine; alternateBy similarity
    Modified residuei590 – 5901N6-acetyllysine; alternateBy similarity
    Modified residuei590 – 5901N6-succinyllysine; alternateBy similarity
    Modified residuei709 – 7091N6-acetyllysine; alternateBy similarity
    Modified residuei709 – 7091N6-succinyllysine; alternateBy similarity
    Modified residuei721 – 7211N6-succinyllysineBy similarity

    Post-translational modificationi

    Acetylated, leading to enhanced enzyme activity. Acetylation is enhanced by up to 80% after treatment either with trichostin A (TCA) or with nicotinamide (NAM) with highest increase on Lys-345. Acetylation and enzyme activity increased by about 1.5% on addition of fatty acids By similarity.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP07896.
    PRIDEiP07896.

    PTM databases

    PhosphoSiteiP07896.

    Expressioni

    Gene expression databases

    GenevestigatoriP07896.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    IntActiP07896. 6 interactions.
    STRINGi10116.ENSRNOP00000002410.

    Structurei

    Secondary structure

    1
    722
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65
    Turni8 – 103
    Beta strandi11 – 166
    Turni19 – 224
    Helixi26 – 4015
    Beta strandi47 – 537
    Beta strandi63 – 653
    Beta strandi67 – 693
    Helixi74 – 8411
    Beta strandi89 – 935
    Beta strandi95 – 984
    Helixi100 – 1067
    Beta strandi108 – 1147
    Beta strandi118 – 1203
    Helixi122 – 1265
    Turni131 – 1333
    Helixi134 – 1429
    Helixi144 – 15310
    Beta strandi156 – 1583
    Helixi159 – 1646
    Beta strandi169 – 1746
    Helixi176 – 18712
    Beta strandi188 – 1903
    Helixi193 – 1953
    Helixi197 – 1993
    Helixi208 – 22215
    Helixi227 – 24115
    Helixi244 – 25916
    Helixi262 – 27211
    Helixi273 – 2786
    Turni283 – 2853
    Turni288 – 2903
    Beta strandi298 – 3025
    Helixi306 – 31611
    Turni317 – 3193
    Beta strandi321 – 3255
    Helixi329 – 35224
    Beta strandi353 – 3553
    Beta strandi362 – 3665
    Helixi368 – 3714
    Beta strandi375 – 3795
    Helixi385 – 39814
    Beta strandi404 – 4074
    Beta strandi410 – 4123
    Helixi414 – 4185
    Helixi424 – 4263
    Beta strandi427 – 4326
    Turni436 – 4383
    Beta strandi441 – 4466
    Helixi452 – 46413
    Beta strandi468 – 4725
    Turni476 – 4794
    Helixi480 – 49617
    Helixi501 – 51111
    Helixi517 – 5248
    Helixi526 – 53510
    Beta strandi538 – 5414
    Helixi560 – 5667
    Turni572 – 5754
    Beta strandi576 – 5838
    Beta strandi589 – 5913
    Helixi593 – 60513
    Helixi615 – 63521
    Beta strandi638 – 6403
    Helixi642 – 65211
    Helixi657 – 6593
    Helixi662 – 6698
    Helixi671 – 68414
    Helixi689 – 6913
    Helixi695 – 7028
    Helixi708 – 7103
    Helixi711 – 7155

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZCJX-ray1.90A260-722[»]
    2X58X-ray2.80A/B1-722[»]
    3ZW8X-ray2.50A/B1-722[»]
    3ZW9X-ray2.90A/B1-722[»]
    3ZWAX-ray2.47A/B1-722[»]
    3ZWBX-ray3.10A/B1-722[»]
    3ZWCX-ray2.30A/B1-722[»]
    ProteinModelPortaliP07896.
    SMRiP07896. Positions 261-719.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07896.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 281281Enoyl-CoA hydratase / isomeraseAdd
    BLAST
    Regioni282 – 5712903-hydroxyacyl-CoA dehydrogenaseAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi720 – 7223Microbody targeting signal

    Sequence similaritiesi

    In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.Curated
    In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiCOG1250.
    GeneTreeiENSGT00720000108673.
    HOGENOMiHOG000261347.
    HOVERGENiHBG104990.
    InParanoidiP07896.
    KOiK07514.
    OMAiLKMRKQH.
    OrthoDBiEOG725DH0.
    PhylomeDBiP07896.
    TreeFamiTF316708.

    Family and domain databases

    Gene3Di1.10.1040.10. 2 hits.
    3.40.50.720. 1 hit.
    3.90.226.10. 1 hit.
    InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
    IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
    IPR006108. 3HC_DH_C.
    IPR008927. 6-PGluconate_DH_C-like.
    IPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    IPR013328. DH_multihelical.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00725. 3HCDH. 2 hits.
    PF02737. 3HCDH_N. 1 hit.
    PF00378. ECH. 1 hit.
    [Graphical view]
    SUPFAMiSSF48179. SSF48179. 2 hits.
    SSF52096. SSF52096. 1 hit.
    PROSITEiPS00067. 3HCDH. 1 hit.
    PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P07896-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEYLRLPHS LAMIRLCNPP VNAVSPTVIR EVRNGLQKAG SDHTVKAIVI    50
    CGANGNFCAG ADIHGFSAFT PGLALGSLVD EIQRYQKPVL AAIQGVALGG 100
    GLELALGCHY RIANAKARVG LPEVTLGILP GARGTQLLPR VVGVPVALDL 150
    ITSGKYLSAD EALRLGILDA VVKSDPVEEA IKFAQKIIDK PIEPRRIFNK 200
    PVPSLPNMDS VFAEAIAKVR KQYPGVLAPE TCVRSIQASV KHPYEVGIKE 250
    EEKLFMYLRA SGQAKALQYA FFAEKSANKW STPSGASWKT ASAQPVSSVG 300
    VLGLGTMGRG IAISFARVGI SVVAVESDPK QLDAAKKIIT FTLEKEASRA 350
    HQNGQASAKP KLRFSSSTKE LSTVDLVVEA VFEDMNLKKK VFAELSALCK 400
    PGAFLCTNTS ALNVDDIASS TDRPQLVIGT HFFSPAHVMR LLEVIPSRYS 450
    SPTTIATVMS LSKKIGKIGV VVGNCYGFVG NRMLAPYYNQ GFFLLEEGSK 500
    PEDVDGVLEE FGFKMGPFRV SDLAGLDVGW KIRKGQGLTG PSLPPGTPVR 550
    KRGNSRYSPL GDMLCEAGRF GQKTGKGWYQ YDKPLGRIHK PDPWLSTFLS 600
    QYREVHHIEQ RTISKEEILE RCLYSLINEA FRILEEGMAA RPEHIDVIYL 650
    HGYGWPRHKG GPMFYAASVG LPTVLEKLQK YYRQNPDIPQ LEPSDYLRRL 700
    VAQGSPPLKE WQSLAGPHGS KL 722
    Length:722
    Mass (Da):78,658
    Last modified:January 23, 2007 - v2
    Checksum:i76ACC709C5F23E86
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K03249 mRNA. Translation: AAA41825.1.
    BC089777 mRNA. Translation: AAH89777.1.
    J02748 Genomic DNA. Translation: AAA41826.1.
    PIRiA23575. DWRTEP.
    RefSeqiNP_598290.1. NM_133606.1.
    UniGeneiRn.3671.

    Genome annotation databases

    EnsembliENSRNOT00000002410; ENSRNOP00000002410; ENSRNOG00000001770.
    GeneIDi171142.
    KEGGirno:171142.
    UCSCiRGD:621441. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K03249 mRNA. Translation: AAA41825.1 .
    BC089777 mRNA. Translation: AAH89777.1 .
    J02748 Genomic DNA. Translation: AAA41826.1 .
    PIRi A23575. DWRTEP.
    RefSeqi NP_598290.1. NM_133606.1.
    UniGenei Rn.3671.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZCJ X-ray 1.90 A 260-722 [» ]
    2X58 X-ray 2.80 A/B 1-722 [» ]
    3ZW8 X-ray 2.50 A/B 1-722 [» ]
    3ZW9 X-ray 2.90 A/B 1-722 [» ]
    3ZWA X-ray 2.47 A/B 1-722 [» ]
    3ZWB X-ray 3.10 A/B 1-722 [» ]
    3ZWC X-ray 2.30 A/B 1-722 [» ]
    ProteinModelPortali P07896.
    SMRi P07896. Positions 261-719.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P07896. 6 interactions.
    STRINGi 10116.ENSRNOP00000002410.

    Chemistry

    ChEMBLi CHEMBL3232.

    PTM databases

    PhosphoSitei P07896.

    Proteomic databases

    PaxDbi P07896.
    PRIDEi P07896.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000002410 ; ENSRNOP00000002410 ; ENSRNOG00000001770 .
    GeneIDi 171142.
    KEGGi rno:171142.
    UCSCi RGD:621441. rat.

    Organism-specific databases

    CTDi 1962.
    RGDi 621441. Ehhadh.

    Phylogenomic databases

    eggNOGi COG1250.
    GeneTreei ENSGT00720000108673.
    HOGENOMi HOG000261347.
    HOVERGENi HBG104990.
    InParanoidi P07896.
    KOi K07514.
    OMAi LKMRKQH.
    OrthoDBi EOG725DH0.
    PhylomeDBi P07896.
    TreeFami TF316708.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    SABIO-RK P07896.

    Miscellaneous databases

    EvolutionaryTracei P07896.
    NextBioi 621936.
    PROi P07896.

    Gene expression databases

    Genevestigatori P07896.

    Family and domain databases

    Gene3Di 1.10.1040.10. 2 hits.
    3.40.50.720. 1 hit.
    3.90.226.10. 1 hit.
    InterProi IPR006180. 3-OHacyl-CoA_DH_CS.
    IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
    IPR006108. 3HC_DH_C.
    IPR008927. 6-PGluconate_DH_C-like.
    IPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    IPR013328. DH_multihelical.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00725. 3HCDH. 2 hits.
    PF02737. 3HCDH_N. 1 hit.
    PF00378. ECH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48179. SSF48179. 2 hits.
    SSF52096. SSF52096. 1 hit.
    PROSITEi PS00067. 3HCDH. 1 hit.
    PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and nucleotide sequence of the cDNA for rat peroxisomal enoyl-CoA: hydratase-3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme."
      Osumi T., Ishii N., Hijikata M., Kamijo K., Ozasa H., Furuta S., Miyazawa S., Kondo K., Inoue K., Kagamiyama H., Hashimoto T.
      J. Biol. Chem. 260:8905-8910(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Liver.
    3. "Structural organization of the gene for rat enoyl-CoA hydratase:3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme."
      Ishii N., Hijikata M., Osumi T., Hashimoto T.
      J. Biol. Chem. 262:8144-8150(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
    4. "Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri-hydroxycoprostanic acids are metabolized by separate multifunctional proteins."
      Dieuaide-Noubhani M., Novikov D., Baumgart E., Vanhooren J.C.T., Fransen M., Goethals M., Vandekerckhove J., Van Veldhoven P.P., Mannaerts G.P.
      Eur. J. Biochem. 240:660-666(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 260-265; 294-302; 520-531 AND 710-719.
    5. "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."
      Palosaari P.M., Hiltunen J.K.
      J. Biol. Chem. 265:2446-2449(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN ISOMERASE.
    6. "Structural studies of MFE-1: the 1.9 A crystal structure of the dehydrogenase part of rat peroxisomal MFE-1."
      Taskinen J.P., Kiema T.R., Hiltunen J.K., Wierenga R.K.
      J. Mol. Biol. 355:734-746(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 260-722, SUBUNIT.

    Entry informationi

    Entry nameiECHP_RAT
    AccessioniPrimary (citable) accession number: P07896
    Secondary accession number(s): Q5EBD2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 138 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3