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Protein

Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial

Gene

Hadh

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

Pathwayi

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 396NADBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. fatty acid beta-oxidation Source: RGD
  2. negative regulation of insulin secretion Source: RGD
  3. response to activity Source: RGD
  4. response to drug Source: RGD
  5. response to hormone Source: RGD
  6. response to insulin Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiREACT_236885. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
REACT_244557. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
REACT_253744. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
REACT_253915. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
REACT_263676. Beta oxidation of butanoyl-CoA to acetyl-CoA.
SABIO-RKQ9WVK7.
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 2

Organism-specific databases

RGDi69321. Hadh.

Subcellular locationi

GO - Cellular componenti

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

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_0000007409Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei75 – 751N6-acetyllysineBy similarity
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

PaxDbiQ9WVK7.
PRIDEiQ9WVK7.

PTM databases

PhosphoSiteiQ9WVK7.

Expressioni

Gene expression databases

GenevestigatoriQ9WVK7.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ9WVK7. 1 interaction.
STRINGi10116.ENSRNOP00000014658.

Structurei

3D structure databases

ProteinModelPortaliQ9WVK7.
SMRiQ9WVK7. Positions 24-314.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1250.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000141498.
HOVERGENiHBG000832.
InParanoidiQ9WVK7.
KOiK00022.
OMAiCPLLKEM.
OrthoDBiEOG7K3TMS.
PhylomeDBiQ9WVK7.
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.

Q9WVK7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFVTRQFVR SMSSSSSASA AAKKILIKHV TVIGGGLMGA GIAQVAAATG
60 70 80 90 100
HTVVLVDQTE DILAKSKKGI EESLKRMAKK KFTENPKAAD EFVEKTLSSL
110 120 130 140 150
STSTDAASVV HSTDLVVEAI VENLKLKNEL FQRLDKFAAE HTIFASNTSS
160 170 180 190 200
LQITNIANAT TRQDRFAGLH FFNPVPMMKL VEVIKTPMTS QKTFESLVDF
210 220 230 240 250
CKTLGKHPVS CKDTPGFIVN RLLVPYLIEA IRLHERGDAS KEDIDTAMKL
260 270 280 290 300
GAGYPMGPFE LLDYVGLDTT KFILDGWHEM DPENPLFQPS PSMNNLVAQK
310
KLGKKTGEGF YKYK
Length:314
Mass (Da):34,448
Last modified:November 1, 1999 - v1
Checksum:iB36518766D6C3828
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF095449 mRNA. Translation: AAD42162.1.
PIRiS74114.
RefSeqiNP_476534.1. NM_057186.2.
UniGeneiRn.92789.

Genome annotation databases

EnsembliENSRNOT00000014658; ENSRNOP00000014658; ENSRNOG00000010697.
GeneIDi113965.
KEGGirno:113965.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF095449 mRNA. Translation: AAD42162.1.
PIRiS74114.
RefSeqiNP_476534.1. NM_057186.2.
UniGeneiRn.92789.

3D structure databases

ProteinModelPortaliQ9WVK7.
SMRiQ9WVK7. Positions 24-314.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9WVK7. 1 interaction.
STRINGi10116.ENSRNOP00000014658.

Chemistry

ChEMBLiCHEMBL2176821.

PTM databases

PhosphoSiteiQ9WVK7.

Proteomic databases

PaxDbiQ9WVK7.
PRIDEiQ9WVK7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000014658; ENSRNOP00000014658; ENSRNOG00000010697.
GeneIDi113965.
KEGGirno:113965.

Organism-specific databases

CTDi3033.
RGDi69321. Hadh.

Phylogenomic databases

eggNOGiCOG1250.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000141498.
HOVERGENiHBG000832.
InParanoidiQ9WVK7.
KOiK00022.
OMAiCPLLKEM.
OrthoDBiEOG7K3TMS.
PhylomeDBiQ9WVK7.
TreeFamiTF300886.

Enzyme and pathway databases

UniPathwayiUPA00659.
ReactomeiREACT_236885. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
REACT_244557. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
REACT_253744. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
REACT_253915. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
REACT_263676. Beta oxidation of butanoyl-CoA to acetyl-CoA.
SABIO-RKQ9WVK7.

Miscellaneous databases

NextBioi618105.
PROiQ9WVK7.

Gene expression databases

GenevestigatoriQ9WVK7.

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]
ProtoNetiSearch...

Publicationsi

  1. "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: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Heart muscle and Liver.

Entry informationi

Entry nameiHCDH_RAT
AccessioniPrimary (citable) accession number: Q9WVK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: March 4, 2015
This is version 125 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.