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P00348

- HCDH_PIG

UniProt

P00348 - HCDH_PIG

Protein

Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial

Gene

HADH

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    Plays an essential role in the mitochondrial beta-oxidation of short chain fatty acids. Exerts it highest activity toward 3-hydroxybutyryl-CoA.1 Publication

    Catalytic activityi

    (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei57 – 571NAD1 Publication
    Binding sitei73 – 731Coenzyme ABy similarity
    Binding sitei80 – 801Coenzyme ABy similarity
    Binding sitei122 – 1221NAD1 Publication
    Binding sitei127 – 1271NAD1 Publication
    Binding sitei149 – 1491Coenzyme ABy similarity
    Binding sitei149 – 1491NAD1 Publication
    Sitei170 – 1701Important for catalytic activityBy similarity
    Binding sitei173 – 1731NADBy similarity
    Binding sitei305 – 3051NADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi34 – 396NAD1 Publication

    GO - Molecular functioni

    1. 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB-EC
    2. NAD+ binding Source: InterPro

    GO - Biological processi

    1. fatty acid beta-oxidation Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    UniPathwayiUPA00659.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial (EC:1.1.1.35)
    Short name:
    HCDH
    Alternative name(s):
    Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase
    Short-chain 3-hydroxyacyl-CoA dehydrogenase
    Gene namesi
    Name:HADH
    Synonyms:HAD, HADHSC, SCHAD
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Chromosome 8

    Subcellular locationi

    Mitochondrion matrix 1 Publication

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: Ensembl
    2. mitochondrial matrix Source: UniProtKB-SubCell
    3. nucleus Source: Ensembl

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1212MitochondrionBy similarityAdd
    BLAST
    Chaini13 – 314302Hydroxyacyl-coenzyme A dehydrogenase, mitochondrialPRO_0000007408Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei80 – 801N6-succinyllysineBy similarity
    Modified residuei81 – 811N6-acetyllysine; alternateBy similarity
    Modified residuei81 – 811N6-succinyllysine; alternateBy similarity
    Modified residuei87 – 871N6-acetyllysine; alternateBy similarity
    Modified residuei87 – 871N6-succinyllysine; alternateBy similarity
    Modified residuei125 – 1251N6-acetyllysineBy similarity
    Modified residuei136 – 1361N6-acetyllysine; alternateBy similarity
    Modified residuei136 – 1361N6-succinyllysine; alternateBy similarity
    Modified residuei179 – 1791N6-acetyllysineBy similarity
    Modified residuei185 – 1851N6-acetyllysine; alternateBy similarity
    Modified residuei185 – 1851N6-succinyllysine; alternateBy similarity
    Modified residuei192 – 1921N6-acetyllysine; alternateBy similarity
    Modified residuei192 – 1921N6-succinyllysine; alternateBy similarity
    Modified residuei202 – 2021N6-acetyllysine; alternateBy similarity
    Modified residuei202 – 2021N6-succinyllysine; alternateBy similarity
    Modified residuei206 – 2061N6-succinyllysineBy similarity
    Modified residuei212 – 2121N6-acetyllysine; alternateBy similarity
    Modified residuei212 – 2121N6-succinyllysine; alternateBy similarity
    Modified residuei241 – 2411N6-acetyllysine; alternateBy similarity
    Modified residuei241 – 2411N6-succinyllysine; alternateBy similarity
    Modified residuei312 – 3121N6-acetyllysine; alternateBy similarity
    Modified residuei312 – 3121N6-succinyllysine; alternateBy similarity

    Post-translational modificationi

    Succinylation at Lys-81, adjacent to a coenzyme A binding site. Desuccinylated by SIRT5 By similarity.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP00348.
    PRIDEiP00348.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000009757.

    Structurei

    Secondary structure

    1
    314
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi29 – 335
    Helixi37 – 4812
    Beta strandi52 – 565
    Helixi60 – 8122
    Turni82 – 843
    Helixi86 – 9813
    Beta strandi100 – 1045
    Helixi106 – 1083
    Beta strandi110 – 1123
    Beta strandi114 – 1185
    Helixi124 – 13714
    Beta strandi143 – 1464
    Beta strandi149 – 1513
    Helixi153 – 1575
    Helixi163 – 1653
    Beta strandi166 – 1705
    Turni175 – 1773
    Beta strandi180 – 1856
    Helixi191 – 20313
    Beta strandi207 – 2137
    Turni215 – 2184
    Helixi219 – 23517
    Helixi241 – 25212
    Helixi258 – 2658
    Helixi267 – 27913
    Turni280 – 2834
    Helixi285 – 2873
    Helixi291 – 2988
    Turni304 – 3074
    Beta strandi308 – 3125

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HDHX-ray2.80A/B/C13-314[»]
    ProteinModelPortaliP00348.
    SMRiP00348. Positions 24-314.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00348.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1250.
    GeneTreeiENSGT00720000108673.
    HOGENOMiHOG000141498.
    HOVERGENiHBG000832.
    KOiK00022.
    OMAiNEAIFAY.
    OrthoDBiEOG7K3TMS.
    TreeFamiTF300886.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR022694. 3-OHacyl-CoA_DH.
    IPR006180. 3-OHacyl-CoA_DH_CS.
    IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
    IPR006108. 3HC_DH_C.
    IPR008927. 6-PGluconate_DH_C-like.
    IPR013328. DH_multihelical.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00725. 3HCDH. 1 hit.
    PF02737. 3HCDH_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000105. HCDH. 1 hit.
    SUPFAMiSSF48179. SSF48179. 1 hit.
    PROSITEiPS00067. 3HCDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P00348-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAFATRQLVR SLSSSSTAAA SAKKILVKHV TVIGGGLMGA GIAQVAAATG    50
    HTVVLVDQTE DILAKSKKGI EESLRKVAKK KFAENPKAGD EFVEKTLSSI 100
    STSTDAASVV HSTDLVVEAI VENLKVKSEL FKRLDKFAAE HTIFASNTSS 150
    LQITSLANAT TRQDRFAGLH FFNPVPLMKL VEVVKTPMTS QKTLESLVDF 200
    SKTLGKHPVS CKDTPGFIVN RLLVPYLIEA VRLYERGDAS KEDIDTAMKL 250
    GAGYPMGPFE LLDYVGLDTT KFIIDGWHEM DSQNPLFQPS PAMNKLVAEN 300
    KFGKKTGEGF YKYK 314
    Length:314
    Mass (Da):34,161
    Last modified:May 30, 2000 - v2
    Checksum:i596CBFD227214C3B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti108 – 1081S → A AA sequence (PubMed:7409145)Curated
    Sequence conflicti122 – 1221E → EQLKVVGE AA sequence (PubMed:7409145)Curated
    Sequence conflicti172 – 1743FNP → N AA sequence (PubMed:7409145)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF027652 mRNA. Translation: AAD20939.1.
    PIRiT46866.
    RefSeqiNP_999496.1. NM_214331.1.
    UniGeneiSsc.12507.

    Genome annotation databases

    EnsembliENSSSCT00000010020; ENSSSCP00000009757; ENSSSCG00000009150.
    GeneIDi397604.
    KEGGissc:397604.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF027652 mRNA. Translation: AAD20939.1 .
    PIRi T46866.
    RefSeqi NP_999496.1. NM_214331.1.
    UniGenei Ssc.12507.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3HDH X-ray 2.80 A/B/C 13-314 [» ]
    ProteinModelPortali P00348.
    SMRi P00348. Positions 24-314.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9823.ENSSSCP00000009757.

    Proteomic databases

    PaxDbi P00348.
    PRIDEi P00348.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSSSCT00000010020 ; ENSSSCP00000009757 ; ENSSSCG00000009150 .
    GeneIDi 397604.
    KEGGi ssc:397604.

    Organism-specific databases

    CTDi 3033.

    Phylogenomic databases

    eggNOGi COG1250.
    GeneTreei ENSGT00720000108673.
    HOGENOMi HOG000141498.
    HOVERGENi HBG000832.
    KOi K00022.
    OMAi NEAIFAY.
    OrthoDBi EOG7K3TMS.
    TreeFami TF300886.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .

    Miscellaneous databases

    EvolutionaryTracei P00348.

    Family and domain databases

    Gene3Di 1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProi IPR022694. 3-OHacyl-CoA_DH.
    IPR006180. 3-OHacyl-CoA_DH_CS.
    IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
    IPR006108. 3HC_DH_C.
    IPR008927. 6-PGluconate_DH_C-like.
    IPR013328. DH_multihelical.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00725. 3HCDH. 1 hit.
    PF02737. 3HCDH_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000105. HCDH. 1 hit.
    SUPFAMi SSF48179. SSF48179. 1 hit.
    PROSITEi PS00067. 3HCDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning, expression in Escherichia coli, and characterization of a novel L-3-hydroxyacyl coenzyme A dehydrogenase from pig liver."
      He X.-Y., Yang S.-Y.
      Biochim. Biophys. Acta 1392:119-126(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
      Tissue: Liver.
    2. "Amino acid sequence of L-3-hydroxyacyl CoA dehydrogenase from pig heart muscle."
      Bitar K.G., Perez-Aranda A., Bradshaw R.A.
      FEBS Lett. 116:196-198(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 13-314.
      Tissue: Heart.
    3. Fang J.-K., Bradshaw R.A.
      Submitted (OCT-1982) to the PIR data bank
      Cited for: SEQUENCE REVISION TO 16 AND 21.
    4. "Identity of heart and liver L-3-hydroxyacyl coenzyme A dehydrogenase."
      He X.-Y., Zhang G., Blecha F., Yang S.-Y.
      Biochim. Biophys. Acta 1437:119-123(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SHOWS THAT HEART AND LIVER ENZYMES ARE IDENTICAL.
    5. "Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary chain tracing at 2.8-A resolution."
      Birktoff J.J., Holden H.M., Hamlin R., Xuong N.H., Banaszak L.J.
      Proc. Natl. Acad. Sci. U.S.A. 84:8262-8266(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 13-314 IN COMPLEX WITH NAD.
    6. "Pig heart short chain L-3-hydroxyacyl-CoA dehydrogenase revisited: sequence analysis and crystal structure determination."
      Barycki J.J., O'Brien L.K., Birktoft J.J., Strauss A.W., Banaszak L.J.
      Protein Sci. 8:2010-2018(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 13-314.
      Tissue: Heart.

    Entry informationi

    Entry nameiHCDH_PIG
    AccessioniPrimary (citable) accession number: P00348
    Secondary accession number(s): Q9XS66
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 124 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, 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