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Protein

Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial

Gene

HADH

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiREACT_278620. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
REACT_300505. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
REACT_308866. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
REACT_321991. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
REACT_340318. Beta oxidation of butanoyl-CoA to acetyl-CoA.
SABIO-RKP00348.
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 Componenti: 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
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_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 – 335Combined sources
Helixi37 – 4812Combined sources
Beta strandi52 – 565Combined sources
Helixi60 – 8122Combined sources
Turni82 – 843Combined sources
Helixi86 – 9813Combined sources
Beta strandi100 – 1045Combined sources
Helixi106 – 1083Combined sources
Beta strandi110 – 1123Combined sources
Beta strandi114 – 1185Combined sources
Helixi124 – 13714Combined sources
Beta strandi143 – 1464Combined sources
Beta strandi149 – 1513Combined sources
Helixi153 – 1575Combined sources
Helixi163 – 1653Combined sources
Beta strandi166 – 1705Combined sources
Turni175 – 1773Combined sources
Beta strandi180 – 1856Combined sources
Helixi191 – 20313Combined sources
Beta strandi207 – 2137Combined sources
Turni215 – 2184Combined sources
Helixi219 – 23517Combined sources
Helixi241 – 25212Combined sources
Helixi258 – 2658Combined sources
Helixi267 – 27913Combined sources
Turni280 – 2834Combined sources
Helixi285 – 2873Combined sources
Helixi291 – 2988Combined sources
Turni304 – 3074Combined sources
Beta strandi308 – 3125Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP00348.
KOiK00022.
OMAiCPLLKEM.
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

        10         20         30         40         50
MAFATRQLVR SLSSSSTAAA SAKKILVKHV TVIGGGLMGA GIAQVAAATG
60 70 80 90 100
HTVVLVDQTE DILAKSKKGI EESLRKVAKK KFAENPKAGD EFVEKTLSSI
110 120 130 140 150
STSTDAASVV HSTDLVVEAI VENLKVKSEL FKRLDKFAAE HTIFASNTSS
160 170 180 190 200
LQITSLANAT TRQDRFAGLH FFNPVPLMKL VEVVKTPMTS QKTLESLVDF
210 220 230 240 250
SKTLGKHPVS CKDTPGFIVN RLLVPYLIEA VRLYERGDAS KEDIDTAMKL
260 270 280 290 300
GAGYPMGPFE LLDYVGLDTT KFIIDGWHEM DSQNPLFQPS PAMNKLVAEN
310
KFGKKTGEGF YKYK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AF027652 mRNA. Translation: AAD20939.1.
PIRiT46866.
RefSeqiNP_999496.1. NM_214331.1.
UniGeneiSsc.12507.

3D structure databases

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

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000009757.

Proteomic databases

PaxDbiP00348.
PRIDEiP00348.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3033.

Phylogenomic databases

eggNOGiCOG1250.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000141498.
HOVERGENiHBG000832.
InParanoidiP00348.
KOiK00022.
OMAiCPLLKEM.
OrthoDBiEOG7K3TMS.
TreeFamiTF300886.

Enzyme and pathway databases

UniPathwayiUPA00659.
ReactomeiREACT_278620. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
REACT_300505. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
REACT_308866. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
REACT_321991. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
REACT_340318. Beta oxidation of butanoyl-CoA to acetyl-CoA.
SABIO-RKP00348.

Miscellaneous databases

EvolutionaryTraceiP00348.

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. "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(1997) [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(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 13-314.
    Tissue: Heart.
  3. Fang J.-K., Bradshaw R.A.
    Submitted (SEP-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(1998) [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(1986) [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(1998) [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: April 1, 2015
This is version 129 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

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.