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P00348 (HCDH_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

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

Subcellular location

Mitochondrion matrix.

Post-translational modification

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

Sequence similarities

Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid beta-oxidation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function3-hydroxyacyl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

NAD+ binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1212Mitochondrion By similarity
Chain13 – 314302Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
PRO_0000007408

Regions

Nucleotide binding34 – 396NAD

Sites

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

Amino acid modifications

Modified residue801N6-succinyllysine By similarity
Modified residue811N6-acetyllysine; alternate By similarity
Modified residue811N6-succinyllysine; alternate By similarity
Modified residue871N6-acetyllysine; alternate By similarity
Modified residue871N6-succinyllysine; alternate By similarity
Modified residue1251N6-acetyllysine By similarity
Modified residue1361N6-acetyllysine; alternate By similarity
Modified residue1361N6-succinyllysine; alternate By similarity
Modified residue1791N6-acetyllysine By similarity
Modified residue1851N6-acetyllysine; alternate By similarity
Modified residue1851N6-succinyllysine; alternate By similarity
Modified residue1921N6-acetyllysine; alternate By similarity
Modified residue1921N6-succinyllysine; alternate By similarity
Modified residue2021N6-acetyllysine; alternate By similarity
Modified residue2021N6-succinyllysine; alternate By similarity
Modified residue2061N6-succinyllysine By similarity
Modified residue2121N6-acetyllysine; alternate By similarity
Modified residue2121N6-succinyllysine; alternate By similarity
Modified residue2411N6-acetyllysine; alternate By similarity
Modified residue2411N6-succinyllysine; alternate By similarity
Modified residue3121N6-acetyllysine; alternate By similarity
Modified residue3121N6-succinyllysine; alternate By similarity

Experimental info

Sequence conflict1081S → A AA sequence Ref.2
Sequence conflict1221E → EQLKVVGE AA sequence Ref.2
Sequence conflict172 – 1743FNP → N AA sequence Ref.2

Secondary structure

........................................................ 314
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00348 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 596CBFD227214C3B

FASTA31434,161
        10         20         30         40         50         60 
MAFATRQLVR SLSSSSTAAA SAKKILVKHV TVIGGGLMGA GIAQVAAATG HTVVLVDQTE 

        70         80         90        100        110        120 
DILAKSKKGI EESLRKVAKK KFAENPKAGD EFVEKTLSSI STSTDAASVV HSTDLVVEAI 

       130        140        150        160        170        180 
VENLKVKSEL FKRLDKFAAE HTIFASNTSS LQITSLANAT TRQDRFAGLH FFNPVPLMKL 

       190        200        210        220        230        240 
VEVVKTPMTS QKTLESLVDF SKTLGKHPVS CKDTPGFIVN RLLVPYLIEA VRLYERGDAS 

       250        260        270        280        290        300 
KEDIDTAMKL GAGYPMGPFE LLDYVGLDTT KFIIDGWHEM DSQNPLFQPS PAMNKLVAEN 

       310 
KFGKKTGEGF YKYK 

« Hide

References

[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].
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF027652 mRNA. Translation: AAD20939.1.
PIRT46866.
RefSeqNP_999496.1. NM_214331.1.
UniGeneSsc.12507.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HDHX-ray2.80A/B/C13-314[»]
ProteinModelPortalP00348.
SMRP00348. Positions 24-314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000009757.

Proteomic databases

PaxDbP00348.
PRIDEP00348.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000010020; ENSSSCP00000009757; ENSSSCG00000009150.
GeneID397604.
KEGGssc:397604.

Organism-specific databases

CTD3033.

Phylogenomic databases

eggNOGCOG1250.
GeneTreeENSGT00720000108673.
HOGENOMHOG000141498.
HOVERGENHBG000832.
KOK00022.
OMAAGFVTTR.
OrthoDBEOG7K3TMS.
TreeFamTF300886.

Enzyme and pathway databases

UniPathwayUPA00659.

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. SSF48179. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00348.

Entry information

Entry nameHCDH_PIG
AccessionPrimary (citable) accession number: P00348
Secondary accession number(s): Q9XS66
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 30, 2000
Last modified: March 19, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways