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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: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei57NAD1 Publication1
Binding sitei73Coenzyme ABy similarity1
Binding sitei80Coenzyme ABy similarity1
Binding sitei122NAD1 Publication1
Binding sitei127NAD1 Publication1
Binding sitei149Coenzyme ABy similarity1
Binding sitei149NAD1 Publication1
Sitei170Important for catalytic activityBy similarity1
Binding sitei173NADBy similarity1
Binding sitei305NADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi34 – 39NAD1 Publication6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiR-SSC-77310. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
R-SSC-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-SSC-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
R-SSC-77350. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
R-SSC-77352. 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
Proteomesi
  • UP000008227 Componenti: Chromosome 8

Subcellular locationi

  • Mitochondrion matrix 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 12MitochondrionBy similarityAdd BLAST12
ChainiPRO_000000740813 – 314Hydroxyacyl-coenzyme A dehydrogenase, mitochondrialAdd BLAST302

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei80N6-succinyllysineBy similarity1
Modified residuei81N6-acetyllysine; alternateBy similarity1
Modified residuei81N6-succinyllysine; alternateBy similarity1
Modified residuei87N6-acetyllysine; alternateBy similarity1
Modified residuei87N6-succinyllysine; alternateBy similarity1
Modified residuei125N6-acetyllysineBy similarity1
Modified residuei136N6-acetyllysine; alternateBy similarity1
Modified residuei136N6-succinyllysine; alternateBy similarity1
Modified residuei179N6-acetyllysineBy similarity1
Modified residuei185N6-acetyllysine; alternateBy similarity1
Modified residuei185N6-succinyllysine; alternateBy similarity1
Modified residuei192N6-acetyllysine; alternateBy similarity1
Modified residuei192N6-succinyllysine; alternateBy similarity1
Modified residuei202N6-acetyllysine; alternateBy similarity1
Modified residuei202N6-succinyllysine; alternateBy similarity1
Modified residuei206N6-succinyllysineBy similarity1
Modified residuei212N6-acetyllysine; alternateBy similarity1
Modified residuei212N6-succinyllysine; alternateBy similarity1
Modified residuei241N6-acetyllysine; alternateBy similarity1
Modified residuei241N6-succinyllysine; alternateBy similarity1
Modified residuei312N6-acetyllysine; alternateBy similarity1
Modified residuei312N6-succinyllysine; alternateBy similarity1

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.
PeptideAtlasiP00348.
PRIDEiP00348.

Expressioni

Gene expression databases

BgeeiENSSSCG00000009150.
GenevisibleiP00348. SS.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000009757.

Structurei

Secondary structure

1314
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 33Combined sources5
Helixi37 – 48Combined sources12
Beta strandi52 – 56Combined sources5
Helixi60 – 81Combined sources22
Turni82 – 84Combined sources3
Helixi86 – 98Combined sources13
Beta strandi100 – 104Combined sources5
Helixi106 – 108Combined sources3
Beta strandi110 – 112Combined sources3
Beta strandi114 – 118Combined sources5
Helixi124 – 137Combined sources14
Beta strandi143 – 146Combined sources4
Beta strandi149 – 151Combined sources3
Helixi153 – 157Combined sources5
Helixi163 – 165Combined sources3
Beta strandi166 – 170Combined sources5
Turni175 – 177Combined sources3
Beta strandi180 – 185Combined sources6
Helixi191 – 203Combined sources13
Beta strandi207 – 213Combined sources7
Turni215 – 218Combined sources4
Helixi219 – 235Combined sources17
Helixi241 – 252Combined sources12
Helixi258 – 265Combined sources8
Helixi267 – 279Combined sources13
Turni280 – 283Combined sources4
Helixi285 – 287Combined sources3
Helixi291 – 298Combined sources8
Turni304 – 307Combined sources4
Beta strandi308 – 312Combined sources5

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP00348.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2304. Eukaryota.
COG1250. LUCA.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000141498.
HOVERGENiHBG000832.
InParanoidiP00348.
KOiK00022.
OMAiSPVPMMQ.
OrthoDBiEOG091G089P.
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. 6PGD_dom_2.
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.
SSF51735. SSF51735. 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)DescriptionActionsGraphical viewLength
Sequence conflicti108S → A AA sequence (PubMed:7409145).Curated1
Sequence conflicti122E → EQLKVVGE AA sequence (PubMed:7409145).Curated1
Sequence conflicti172 – 174FNP → N AA sequence (PubMed:7409145).Curated3

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HDHX-ray2.80A/B/C13-314[»]
ProteinModelPortaliP00348.
SMRiP00348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000009757.

Proteomic databases

PaxDbiP00348.
PeptideAtlasiP00348.
PRIDEiP00348.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3033.

Phylogenomic databases

eggNOGiKOG2304. Eukaryota.
COG1250. LUCA.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000141498.
HOVERGENiHBG000832.
InParanoidiP00348.
KOiK00022.
OMAiSPVPMMQ.
OrthoDBiEOG091G089P.
TreeFamiTF300886.

Enzyme and pathway databases

UniPathwayiUPA00659.
ReactomeiR-SSC-77310. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
R-SSC-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-SSC-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
R-SSC-77350. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
R-SSC-77352. Beta oxidation of butanoyl-CoA to acetyl-CoA.
SABIO-RKP00348.

Miscellaneous databases

EvolutionaryTraceiP00348.

Gene expression databases

BgeeiENSSSCG00000009150.
GenevisibleiP00348. SS.

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. 6PGD_dom_2.
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.
SSF51735. SSF51735. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 142 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

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 one 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.