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Q5R5M8

- ECHP_PONAB

UniProt

Q5R5M8 - ECHP_PONAB

Protein

Peroxisomal bifunctional enzyme

Gene

EHHADH

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      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 sitei101 – 1011Substrate; via amide nitrogenBy similarity
    Sitei104 – 1041Important for catalytic activityBy similarity
    Sitei124 – 1241Important 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
    Synonyms:ECHD
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    Subcellular locationi

    Peroxisome By similarity

    GO - Cellular componenti

    1. peroxisome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 723723Peroxisomal bifunctional enzymePRO_0000353181Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei38 – 381N6-succinyllysineBy similarity
    Modified residuei165 – 1651N6-acetyllysine; alternateBy similarity
    Modified residuei165 – 1651N6-succinyllysine; alternateBy similarity
    Modified residuei171 – 1711N6-acetyllysineBy similarity
    Modified residuei219 – 2191N6-acetyllysine; alternateBy similarity
    Modified residuei219 – 2191N6-succinyllysine; alternateBy similarity
    Modified residuei250 – 2501N6-acetyllysineBy similarity
    Modified residuei280 – 2801N6-succinyllysineBy similarity
    Modified residuei290 – 2901N6-succinyllysineBy similarity
    Modified residuei346 – 3461N6-acetyllysineBy similarity
    Modified residuei350 – 3501N6-acetyllysineBy similarity
    Modified residuei464 – 4641N6-acetyllysineBy similarity
    Modified residuei532 – 5321N6-succinyllysineBy similarity
    Modified residuei577 – 5771N6-succinyllysineBy similarity
    Modified residuei584 – 5841N6-acetyllysine; alternateBy similarity
    Modified residuei584 – 5841N6-succinyllysine; alternateBy similarity
    Modified residuei591 – 5911N6-acetyllysine; alternateBy similarity
    Modified residuei591 – 5911N6-succinyllysine; alternateBy similarity
    Modified residuei710 – 7101N6-acetyllysine; alternateBy similarity
    Modified residuei710 – 7101N6-succinyllysine; alternateBy similarity
    Modified residuei722 – 7221N6-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-346. Acetylation and enzyme activity increased by about 1.5% on addition of fatty acids By similarity.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiQ5R5M8.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ5R5M8.
    SMRiQ5R5M8. Positions 262-717.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 282282Enoyl-CoA hydratase / isomeraseAdd
    BLAST
    Regioni283 – 5722903-hydroxyacyl-CoA dehydrogenaseAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi721 – 7233Microbody 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

    HOGENOMiHOG000261347.
    HOVERGENiHBG104990.
    InParanoidiQ5R5M8.
    KOiK07514.

    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.

    Q5R5M8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEYTRLHNA LALIRLRNPP VNAISTALLR DIKEGLQKAV IDHTIKAIVI    50
    CGAEGKFSAG ADIHGFSAPR TFGFTLGHVV DEIQRNEKPV VAAIQGMAFG 100
    GGLELALGCH YRIAHSEAQV GLPEVTLGLL PGARGTQLLP RLIGVPAALD 150
    LITSGRHILA DEALKLGILD KVVNSDPVEE AIRFAQRVSD QPLESRRLCN 200
    KPIQSLPNMD TIFSEALLKM RRQHPGCLAQ EACVRAVQAA VQYPYEVGVK 250
    KEEELFLYLF QSGQARALQY AFLAERKANK WSTPSGASWK TASARPVSSV 300
    GVVGLGTMGR GIVISFARAR IPVIAVDSDK NQLATANKMI TSVLEKEASK 350
    MQQSGHPWSG PKPRLTSSMK ELGGVDLVIE AVFEEMSLKK QVFAELSAIC 400
    KPEAFLCTNT SALDVDEIAS STDRPHLVIG THFFSPAHVM KLLEVIPSQY 450
    SSPTTIATVM NLSKKIKKIG VVVGNCFGFV GNRMLNPYYN QAYFLLEEGS 500
    KPEEVDQVLE EFGFKMGPFR VSDLAGLDVG WKSRKGQGLT GPTLPPGTPA 550
    RKRGNRRYCP IPDVLCELGR FGQKTGKGWY QYDKPLGRIH KADPWLSKFL 600
    SQYRETHHIE PRTISQDEIL ERCLYSLINE AFRILGEGIA ASPEHIDVVY 650
    LHGYGWPRHK GGPMFYASTV GLPTVLEKLQ KYYRQNPDIP QLEPSDYLKK 700
    LASQGNPPQK EWQSLAGSPS SKL 723
    Length:723
    Mass (Da):79,481
    Last modified:December 21, 2004 - v1
    Checksum:i8CAE3A1578A147C6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR860829 mRNA. Translation: CAH92938.1.
    RefSeqiNP_001127606.1. NM_001134134.1.

    Genome annotation databases

    GeneIDi100174685.
    KEGGipon:100174685.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR860829 mRNA. Translation: CAH92938.1 .
    RefSeqi NP_001127606.1. NM_001134134.1.

    3D structure databases

    ProteinModelPortali Q5R5M8.
    SMRi Q5R5M8. Positions 262-717.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q5R5M8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100174685.
    KEGGi pon:100174685.

    Organism-specific databases

    CTDi 1962.

    Phylogenomic databases

    HOGENOMi HOG000261347.
    HOVERGENi HBG104990.
    InParanoidi Q5R5M8.
    KOi K07514.

    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 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. The German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.

    Entry informationi

    Entry nameiECHP_PONAB
    AccessioniPrimary (citable) accession number: Q5R5M8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 4, 2008
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 74 of the entry and version 1 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