Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9WVK7 (HCDH_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
Short name=HCDH
EC=1.1.1.35
Alternative name(s):
Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase
Short-chain 3-hydroxyacyl-CoA dehydrogenase
Gene names
Name:Hadh
Synonyms:Had, Hadhsc, Schad
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1212Mitochondrion By similarity
Chain13 – 314302Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
PRO_0000007409

Regions

Nucleotide binding34 – 396NAD By similarity

Sites

Binding site571NAD By similarity
Binding site731Coenzyme A By similarity
Binding site801Coenzyme A By similarity
Binding site1221NAD By similarity
Binding site1271NAD By similarity
Binding site1491Coenzyme A By similarity
Binding site1491NAD By similarity
Binding site1731NAD By similarity
Binding site3051NAD By similarity
Site1701Important for catalytic activity By similarity

Amino acid modifications

Modified residue1851N6-acetyllysine By similarity
Modified residue2021N6-acetyllysine By similarity
Modified residue2411N6-acetyllysine By similarity
Modified residue3121N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9WVK7 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: B36518766D6C3828

FASTA31434,448
        10         20         30         40         50         60 
MAFVTRQFVR SMSSSSSASA AAKKILIKHV TVIGGGLMGA GIAQVAAATG HTVVLVDQTE 

        70         80         90        100        110        120 
DILAKSKKGI EESLKRMAKK KFTENPKAAD EFVEKTLSSL STSTDAASVV HSTDLVVEAI 

       130        140        150        160        170        180 
VENLKLKNEL FQRLDKFAAE HTIFASNTSS LQITNIANAT TRQDRFAGLH FFNPVPMMKL 

       190        200        210        220        230        240 
VEVIKTPMTS QKTFESLVDF CKTLGKHPVS CKDTPGFIVN RLLVPYLIEA IRLHERGDAS 

       250        260        270        280        290        300 
KEDIDTAMKL GAGYPMGPFE LLDYVGLDTT KFILDGWHEM DPENPLFQPS PSMNNLVAQK 

       310 
KLGKKTGEGF YKYK

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF095449 mRNA. Translation: AAD42162.1.
IPIIPI00205157.
PIRS74114.
RefSeqNP_476534.1. NM_057186.2.
UniGeneRn.92789.

3D structure databases

ProteinModelPortalQ9WVK7.
SMRQ9WVK7. Positions 24-314.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9WVK7. 1 interaction.
STRING10116.ENSRNOP00000014658.

PTM databases

PhosphoSiteQ9WVK7.

Proteomic databases

PaxDbQ9WVK7.
PRIDEQ9WVK7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000014658; ENSRNOP00000014658; ENSRNOG00000010697.
GeneID113965.
KEGGrno:113965.

Organism-specific databases

CTD3033.
RGD69321. Hadh.

Phylogenomic databases

eggNOGCOG1250.
GeneTreeENSGT00700000104363.
HOGENOMHOG000141498.
HOVERGENHBG000832.
InParanoidQ9WVK7.
KOK00022.
OMAQITNIAN.
OrthoDBEOG44BB2Z.

Enzyme and pathway databases

SABIO-RKQ9WVK7.
UniPathwayUPA00659.

Gene expression databases

GenevestigatorQ9WVK7.
GermOnlineENSRNOG00000010697. Rattus norvegicus.

Family and domain databases

Gene3D1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProIPR022694. 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]
PfamPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
[Graphical view]
PIRSFPIRSF000105. HCDH. 1 hit.
SUPFAMSSF48179. 6DGDH_C_like. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio618105.

Entry information

Entry nameHCDH_RAT
AccessionPrimary (citable) accession number: Q9WVK7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: May 1, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents