P00348 (HCDH_PIG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	314 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Sequence similarities	Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid beta-oxidation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	mitochondrial inner membrane Inferred from electronic annotation. Source: Compara mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	3-hydroxyacyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: EC NAD+ binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 12

12

Mitochondrion By similarity

Chain

13 – 314

302

Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial

PRO_0000007408

Regions

Nucleotide binding

34 – 39

6

NAD

Sites

Binding site

57

1

NAD

Binding site

73

1

Coenzyme A By similarity

Binding site

80

1

Coenzyme A By similarity

Binding site

122

1

NAD

Binding site

127

1

NAD

Binding site

149

1

Coenzyme A By similarity

Binding site

149

1

NAD

Binding site

173

1

NAD By similarity

Binding site

305

1

NAD By similarity

Site

170

1

Important for catalytic activity By similarity

Amino acid modifications

Modified residue

185

1

N6-acetyllysine By similarity

Modified residue

202

1

N6-acetyllysine By similarity

Modified residue

241

1

N6-acetyllysine By similarity

Modified residue

312

1

N6-acetyllysine By similarity

Experimental info

Sequence conflict

108

1

S → A AA sequence Ref.2

Sequence conflict

122

1

E → EQLKVVGE AA sequence Ref.2

Sequence conflict

172 – 174

3

FNP → N AA sequence Ref.2

Secondary structure

1

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314

Helix Strand Turn

Details...

Beta strand

29 – 33

5

Helix

37 – 48

12

Beta strand

52 – 56

5

Helix

60 – 81

22

Turn

82 – 84

3

Helix

86 – 98

13

Beta strand

100 – 104

5

Helix

106 – 108

3

Beta strand

110 – 112

3

Beta strand

114 – 118

5

Helix

124 – 137

14

Beta strand

143 – 146

4

Beta strand

149 – 151

3

Helix

153 – 157

5

Helix

163 – 165

3

Beta strand

166 – 170

5

Turn

175 – 177

3

Beta strand

180 – 185

6

Helix

191 – 203

13

Beta strand

207 – 213

7

Turn

215 – 218

4

Helix

219 – 235

17

Helix

241 – 252

12

Helix

258 – 265

8

Helix

267 – 279

13

Turn

280 – 283

4

Helix

285 – 287

3

Helix

291 – 298

8

Turn

304 – 307

4

Beta strand

308 – 312

5

Sequences

	Sequence		Length	Mass (Da)
	P00348 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 596CBFD227214C3B	FASTA	314	34,161
	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

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.

PIR

T46866.

RefSeq

NP_999496.1. NM_214331.1.

UniGene

Ssc.12507.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3HDH	X-ray	2.80	A/B/C	13-314	[»]

ProteinModelPortal

P00348.

SMR

P00348. Positions 24-314.

ModBase

Search...

Protein-protein interaction databases

STRING

9823.ENSSSCP00000009757.

Proteomic databases

PaxDb

P00348.

PRIDE

P00348.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSSSCT00000010020; ENSSSCP00000009757; ENSSSCG00000009150.

GeneID

397604.

KEGG

ssc:397604.

Organism-specific databases

CTD

3033.

Phylogenomic databases

eggNOG

COG1250.

GeneTree

ENSGT00700000104363.

HOGENOM

HOG000141498.

HOVERGEN

HBG000832.

KO

K00022.

OMA

QITNIAN.

OrthoDB

EOG44BB2Z.

Enzyme and pathway databases

UniPathway

UPA00659.

Family and domain databases

Gene3D

1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.

InterPro

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]

Pfam

PF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000105. HCDH. 1 hit.

SUPFAM

SSF48179. 6DGDH_C_like. 1 hit.

PROSITE

PS00067. 3HCDH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00348.

Entry information

Entry name

HCDH_PIG

Accession

Primary (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:	April 3, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program