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P55100

- ECHP_CAVPO

UniProt

P55100 - ECHP_CAVPO

Protein

Peroxisomal bifunctional enzyme

Gene

EHHADH

Organism
Cavia porcellus (Guinea pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 106 (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 sitei103 – 1031Substrate; via amide nitrogenBy similarity
    Sitei106 – 1061Important for catalytic activityBy similarity
    Sitei126 – 1261Important for catalytic activityBy similarity

    GO - Molecular functioni

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

    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

    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
    OrganismiCavia porcellus (Guinea pig)
    Taxonomic identifieri10141 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
    ProteomesiUP000005447: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. peroxisome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 726726Peroxisomal bifunctional enzymePRO_0000109246Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei38 – 381N6-succinyllysineBy similarity
    Modified residuei167 – 1671N6-acetyllysine; alternateBy similarity
    Modified residuei167 – 1671N6-succinyllysine; alternateBy similarity
    Modified residuei173 – 1731N6-acetyllysineBy similarity
    Modified residuei185 – 1851N6-succinyllysineBy similarity
    Modified residuei221 – 2211N6-acetyllysine; alternateBy similarity
    Modified residuei221 – 2211N6-succinyllysine; alternateBy similarity
    Modified residuei282 – 2821N6-succinyllysineBy similarity
    Modified residuei292 – 2921N6-succinyllysineBy similarity
    Modified residuei333 – 3331N6-succinyllysineBy similarity
    Modified residuei348 – 3481N6-acetyllysineBy similarity
    Modified residuei352 – 3521N6-acetyllysineBy similarity
    Modified residuei467 – 4671N6-acetyllysineBy similarity
    Modified residuei535 – 5351N6-succinyllysineBy similarity
    Modified residuei587 – 5871N6-acetyllysine; alternateBy similarity
    Modified residuei587 – 5871N6-succinyllysine; alternateBy similarity
    Modified residuei594 – 5941N6-acetyllysine; alternateBy similarity
    Modified residuei594 – 5941N6-succinyllysine; alternateBy similarity
    Modified residuei713 – 7131N6-acetyllysine; alternateBy similarity
    Modified residuei713 – 7131N6-succinyllysine; alternateBy similarity
    Modified residuei725 – 7251N6-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-348. Acetylation and enzyme activity increased by about 1.5% on addition of fatty acids By similarity.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiP55100.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi10141.ENSCPOP00000019312.

    Structurei

    3D structure databases

    ProteinModelPortaliP55100.
    SMRiP55100. Positions 264-720.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 284284Enoyl-CoA hydratase / isomeraseAdd
    BLAST
    Regioni285 – 5752913-hydroxyacyl-CoA dehydrogenaseAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi724 – 7263Microbody targeting signalBy similarity

    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.
    HOGENOMiHOG000261347.
    HOVERGENiHBG104990.
    InParanoidiP55100.

    Family and domain databases

    Gene3Di1.10.1040.10. 2 hits.
    3.40.50.720. 1 hit.
    3.90.226.10. 1 hit.
    InterProiIPR006176. 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.
    PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P55100-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEYLRLPHS LALIRLRNPP VNAISPAVIH GIKEGLQKAM SDYTIKGIVI    50
    SGANNIFCAG ADIHGFSAPL SFGTGSGLGP IVDEMQRYEK PVVAAIQGMA 100
    LGGGLELSLG CHYRIAHAEA RIGFPEVTLG ILPGARGTQL LPRLIGVPAA 150
    LDLITSGRHI TAGEALKLGI LDKVVNSAPV EEAIKFAQKI LNQPLEPRRI 200
    LNRPVSSLPN MDAIFGEAVE KMRRQHPGQL APETCVRSVQ ASVQYPYEGG 250
    IMKERELFLN LQHSGQAKAL QYAFFAERSA PKWSTPSGAS WKTAAARPVS 300
    SVGVLGLGTM GRGIAISFAR VGIPVIAVES DPKQLETAQK LITSILEKEA 350
    SKSRQQCGQQ RSGPKPRFSS SMKDLASVDL VVEAVFEDMN LKKRVFAELS 400
    AVCKPEAFLC TNTSALDVDE IATSTNRPQQ VIGTHFFSPA HVMKLLEVIP 450
    SRHSSPTTIA TVMDLAKKIK KVAVVVGNCY GFVGNRMLRS YYEQTNFLLE 500
    DGSKPEDIDQ ALEEFGFRMG PFRVSDLAGL DVGWKIRKGQ GLTGPSLQGT 550
    APARKRGNAR YSPIADMLCE LGRFGQKTGQ GWYKYDKPLG RIHKPDPWLS 600
    KFLSEYRETH HIKPRVIGRD EILERCLYAL INEAFRILGE GIAASPEHID 650
    VIYLHGYGWP RHKGGPMFYA ASVGLPTVLE KLQKYYQQNP DIPHLEPCNY 700
    LKKLASQGNP PLKEWQSLAG LPSSKL 726
    Length:726
    Mass (Da):79,375
    Last modified:January 23, 2007 - v2
    Checksum:iF1702122D62C5FF3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X92742 mRNA. Translation: CAA63403.1.
    X85112 mRNA. Translation: CAA59431.1.
    PIRiS68697. S57651.
    RefSeqiNP_001166417.1. NM_001172946.1.

    Genome annotation databases

    GeneIDi100135519.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X92742 mRNA. Translation: CAA63403.1 .
    X85112 mRNA. Translation: CAA59431.1 .
    PIRi S68697. S57651.
    RefSeqi NP_001166417.1. NM_001172946.1.

    3D structure databases

    ProteinModelPortali P55100.
    SMRi P55100. Positions 264-720.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10141.ENSCPOP00000019312.

    Proteomic databases

    PRIDEi P55100.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100135519.

    Phylogenomic databases

    eggNOGi COG1250.
    HOGENOMi HOG000261347.
    HOVERGENi HBG104990.
    InParanoidi P55100.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .

    Family and domain databases

    Gene3Di 1.10.1040.10. 2 hits.
    3.40.50.720. 1 hit.
    3.90.226.10. 1 hit.
    InterProi 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 PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and tissue expression of two cDNAs encoding the peroxisomal 2-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase in the guinea pig liver."
      Caira F., Cherkaoui-Malki M., Hoefler G., Latruffe N.
      FEBS Lett. 378:57-60(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.

    Entry informationi

    Entry nameiECHP_CAVPO
    AccessioniPrimary (citable) accession number: P55100
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 106 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

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3