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Q60587

- ECHB_RAT

UniProt

Q60587 - ECHB_RAT

Protein

Trifunctional enzyme subunit beta, mitochondrial

Gene

Hadhb

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei139 – 1391Acyl-thioester intermediateBy similarity
    Active sitei429 – 4291Proton acceptorPROSITE-ProRule annotation
    Active sitei459 – 4591Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. 3-hydroxyacyl-CoA dehydrogenase activity Source: RGD
    2. acetyl-CoA C-acyltransferase activity Source: RGD
    3. enoyl-CoA hydratase activity Source: RGD
    4. fatty-acyl-CoA binding Source: RGD
    5. long-chain-3-hydroxyacyl-CoA dehydrogenase activity Source: RGD
    6. long-chain-enoyl-CoA hydratase activity Source: RGD
    7. NAD binding Source: RGD
    8. protein complex binding Source: RGD

    GO - Biological processi

    1. fatty acid beta-oxidation Source: RGD

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Enzyme and pathway databases

    ReactomeiREACT_199139. Acyl chain remodeling of CL.
    UniPathwayiUPA00659.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trifunctional enzyme subunit beta, mitochondrial
    Alternative name(s):
    TP-beta
    Including the following 1 domains:
    3-ketoacyl-CoA thiolase (EC:2.3.1.16)
    Alternative name(s):
    Acetyl-CoA acyltransferase
    Beta-ketothiolase
    Gene namesi
    Name:Hadhb
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 6

    Organism-specific databases

    RGDi620513. Hadhb.

    Subcellular locationi

    Mitochondrion By similarity. Mitochondrion inner membrane By similarity. Mitochondrion outer membrane By similarity. Endoplasmic reticulum By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. mitochondrial fatty acid beta-oxidation multienzyme complex Source: RGD
    3. mitochondrial inner membrane Source: UniProtKB
    4. mitochondrial nucleoid Source: Ensembl
    5. mitochondrial outer membrane Source: UniProtKB
    6. mitochondrion Source: RGD

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion inner membrane, Mitochondrion outer membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3434MitochondrionBy similarityAdd
    BLAST
    Chaini35 – 475441Trifunctional enzyme subunit beta, mitochondrialPRO_0000034084Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei53 – 531N6-succinyllysineBy similarity
    Modified residuei73 – 731N6-acetyllysine; alternateBy similarity
    Modified residuei73 – 731N6-succinyllysine; alternateBy similarity
    Modified residuei189 – 1891N6-acetyllysine; alternateBy similarity
    Modified residuei189 – 1891N6-succinyllysine; alternateBy similarity
    Modified residuei191 – 1911N6-succinyllysineBy similarity
    Modified residuei273 – 2731N6-succinyllysineBy similarity
    Modified residuei292 – 2921N6-succinyllysineBy similarity
    Modified residuei294 – 2941N6-acetyllysine; alternateBy similarity
    Modified residuei294 – 2941N6-succinyllysine; alternateBy similarity
    Modified residuei299 – 2991N6-acetyllysineBy similarity
    Modified residuei333 – 3331N6-acetyllysine; alternateBy similarity
    Modified residuei333 – 3331N6-succinyllysine; alternateBy similarity
    Modified residuei349 – 3491N6-acetyllysineBy similarity
    Modified residuei362 – 3621N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ60587.
    PRIDEiQ60587.

    Expressioni

    Gene expression databases

    GenevestigatoriQ60587.

    Interactioni

    Subunit structurei

    Octamer of 4 alpha (HADHA) and 4 beta (HADHB) subunits. Interacts with RSAD2/viperin By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ60587. 2 interactions.
    MINTiMINT-4596988.
    STRINGi10116.ENSRNOP00000014637.

    Structurei

    3D structure databases

    ProteinModelPortaliQ60587.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thiolase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0183.
    GeneTreeiENSGT00390000009412.
    HOGENOMiHOG000012240.
    HOVERGENiHBG104782.
    InParanoidiQ60587.
    KOiK07509.
    OMAiMIVERYP.
    OrthoDBiEOG7DRJ2Z.
    PhylomeDBiQ60587.
    TreeFamiTF315243.

    Family and domain databases

    Gene3Di3.40.47.10. 4 hits.
    InterProiIPR002155. Thiolase.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    IPR020615. Thiolase_acyl_enz_int_AS.
    IPR020610. Thiolase_AS.
    IPR020617. Thiolase_C.
    IPR020613. Thiolase_CS.
    IPR020616. Thiolase_N.
    [Graphical view]
    PfamiPF02803. Thiolase_C. 1 hit.
    PF00108. Thiolase_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF53901. SSF53901. 2 hits.
    TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
    PROSITEiPS00098. THIOLASE_1. 1 hit.
    PS00737. THIOLASE_2. 1 hit.
    PS00099. THIOLASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q60587-1 [UniParc]FASTAAdd to Basket

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    MTTILTSTFR NLSTTSKWAL RFSVRPLSCS SQVQSAPAVQ TKSKKTLAKP    50
    NLKNIVVVEG VRIPFLLSGT SYKDLMPHDL ARAALSGLLY RTNIPKDVVD 100
    YIIFGTVIQE VKTSNVAREA ALGAGFSDKT PAHTVTMACI SSNQAMTTAV 150
    GLIASGQCDV VVAGGVELMS DVPIRHSRNM RKMMLDLNKA KTLAQRLSLL 200
    TKFRLNFLSP ELPAVAEFST NETMGHSADR LAAAFAVSRM EQDKYALRSH 250
    SLAKKAQDEG HLSDIVPFKV PGKDTVSKDN GIRPSSLEQM AKLKPAFIKP 300
    YGTVTAANSS FLTDGASAML IMSEDRALAM GYKPKAYLRD FIYVSQDPKD 350
    QLLLGPTYAT PKVLEKAGLT MNDIDAFEFH EAFSGQILAN FKAMDSDWFA 400
    QNYMGRKTKV GAPPLEKFNI WGGSLSLGHP FGATGCRLVM AAANRLRKDG 450
    GQYALVAACA AGGQGHAMIV EAYPK 475
    Length:475
    Mass (Da):51,414
    Last modified:November 1, 1997 - v1
    Checksum:i59231029C8BA2A13
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16479 mRNA. Translation: BAA03940.1.
    BC060545 mRNA. Translation: AAH60545.1.
    PIRiB49681.
    RefSeqiNP_598302.1. NM_133618.2.
    XP_006239850.1. XM_006239788.1.
    XP_006239851.1. XM_006239789.1.
    UniGeneiRn.11253.

    Genome annotation databases

    EnsembliENSRNOT00000014637; ENSRNOP00000014637; ENSRNOG00000010800.
    GeneIDi171155.
    KEGGirno:171155.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16479 mRNA. Translation: BAA03940.1 .
    BC060545 mRNA. Translation: AAH60545.1 .
    PIRi B49681.
    RefSeqi NP_598302.1. NM_133618.2.
    XP_006239850.1. XM_006239788.1.
    XP_006239851.1. XM_006239789.1.
    UniGenei Rn.11253.

    3D structure databases

    ProteinModelPortali Q60587.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q60587. 2 interactions.
    MINTi MINT-4596988.
    STRINGi 10116.ENSRNOP00000014637.

    Proteomic databases

    PaxDbi Q60587.
    PRIDEi Q60587.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000014637 ; ENSRNOP00000014637 ; ENSRNOG00000010800 .
    GeneIDi 171155.
    KEGGi rno:171155.

    Organism-specific databases

    CTDi 3032.
    RGDi 620513. Hadhb.

    Phylogenomic databases

    eggNOGi COG0183.
    GeneTreei ENSGT00390000009412.
    HOGENOMi HOG000012240.
    HOVERGENi HBG104782.
    InParanoidi Q60587.
    KOi K07509.
    OMAi MIVERYP.
    OrthoDBi EOG7DRJ2Z.
    PhylomeDBi Q60587.
    TreeFami TF315243.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    Reactomei REACT_199139. Acyl chain remodeling of CL.

    Miscellaneous databases

    NextBioi 621992.
    PROi Q60587.

    Gene expression databases

    Genevestigatori Q60587.

    Family and domain databases

    Gene3Di 3.40.47.10. 4 hits.
    InterProi IPR002155. Thiolase.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    IPR020615. Thiolase_acyl_enz_int_AS.
    IPR020610. Thiolase_AS.
    IPR020617. Thiolase_C.
    IPR020613. Thiolase_CS.
    IPR020616. Thiolase_N.
    [Graphical view ]
    Pfami PF02803. Thiolase_C. 1 hit.
    PF00108. Thiolase_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53901. SSF53901. 2 hits.
    TIGRFAMsi TIGR01930. AcCoA-C-Actrans. 1 hit.
    PROSITEi PS00098. THIOLASE_1. 1 hit.
    PS00737. THIOLASE_2. 1 hit.
    PS00099. THIOLASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of the cDNAs for the subunits of rat mitochondrial fatty acid beta-oxidation multienzyme complex. Structural and functional relationships to other mitochondrial and peroxisomal beta-oxidation enzymes."
      Kamijo T., Aoyama T., Miyazaki J., Hashimoto T.
      J. Biol. Chem. 268:26452-26460(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Wistar.
    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: Pituitary.
    3. "Novel fatty acid beta-oxidation enzymes in rat liver mitochondria. II. Purification and properties of enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein."
      Uchida Y., Izai K., Orii T., Hashimoto T.
      J. Biol. Chem. 267:1034-1041(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.

    Entry informationi

    Entry nameiECHB_RAT
    AccessioniPrimary (citable) accession number: Q60587
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 114 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, 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