Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial

Gene

Hadh

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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

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 sitei57NADBy similarity1
Binding sitei73Coenzyme ABy similarity1
Binding sitei80Coenzyme ABy similarity1
Binding sitei122NADBy similarity1
Binding sitei127NADBy similarity1
Binding sitei149Coenzyme ABy similarity1
Binding sitei149NADBy similarity1
Sitei170Important for catalytic activityBy similarity1
Binding sitei173NADBy similarity1
Binding sitei305NADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi34 – 39NADBy similarity6

GO - Molecular functioni

  • 3-hydroxyacyl-CoA dehydrogenase activity Source: RGD
  • NAD+ binding Source: InterPro

GO - Biological processi

  • fatty acid beta-oxidation Source: RGD
  • negative regulation of insulin secretion Source: RGD
  • response to activity Source: RGD
  • response to drug Source: RGD
  • response to hormone Source: RGD
  • response to insulin Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiR-RNO-77310. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
R-RNO-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-RNO-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
R-RNO-77350. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
R-RNO-77352. Beta oxidation of butanoyl-CoA to acetyl-CoA.
SABIO-RKQ9WVK7.
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi69321. Hadh.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2176821.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 12MitochondrionBy similarityAdd BLAST12
ChainiPRO_000000740913 – 314Hydroxyacyl-coenzyme A dehydrogenase, mitochondrialAdd BLAST302

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei75N6-acetyllysineBy similarity1
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

PaxDbiQ9WVK7.
PRIDEiQ9WVK7.

PTM databases

iPTMnetiQ9WVK7.
PhosphoSitePlusiQ9WVK7.

Expressioni

Gene expression databases

BgeeiENSRNOG00000010697.
GenevisibleiQ9WVK7. RN.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ9WVK7. 1 interactor.
STRINGi10116.ENSRNOP00000014658.

Structurei

3D structure databases

ProteinModelPortaliQ9WVK7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2304. Eukaryota.
COG1250. LUCA.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000141498.
HOVERGENiHBG000832.
InParanoidiQ9WVK7.
KOiK00022.
OMAiSPVPMMQ.
OrthoDBiEOG091G089P.
PhylomeDBiQ9WVK7.
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.

Q9WVK7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFVTRQFVR SMSSSSSASA AAKKILIKHV TVIGGGLMGA GIAQVAAATG
60 70 80 90 100
HTVVLVDQTE DILAKSKKGI EESLKRMAKK KFTENPKAAD EFVEKTLSSL
110 120 130 140 150
STSTDAASVV HSTDLVVEAI VENLKLKNEL FQRLDKFAAE HTIFASNTSS
160 170 180 190 200
LQITNIANAT TRQDRFAGLH FFNPVPMMKL VEVIKTPMTS QKTFESLVDF
210 220 230 240 250
CKTLGKHPVS CKDTPGFIVN RLLVPYLIEA IRLHERGDAS KEDIDTAMKL
260 270 280 290 300
GAGYPMGPFE LLDYVGLDTT KFILDGWHEM DPENPLFQPS PSMNNLVAQK
310
KLGKKTGEGF YKYK
Length:314
Mass (Da):34,448
Last modified:November 1, 1999 - v1
Checksum:iB36518766D6C3828
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF095449 mRNA. Translation: AAD42162.1.
PIRiS74114.
RefSeqiNP_476534.1. NM_057186.2.
UniGeneiRn.92789.

Genome annotation databases

EnsembliENSRNOT00000014658; ENSRNOP00000014658; ENSRNOG00000010697.
GeneIDi113965.
KEGGirno:113965.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF095449 mRNA. Translation: AAD42162.1.
PIRiS74114.
RefSeqiNP_476534.1. NM_057186.2.
UniGeneiRn.92789.

3D structure databases

ProteinModelPortaliQ9WVK7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9WVK7. 1 interactor.
STRINGi10116.ENSRNOP00000014658.

Chemistry databases

ChEMBLiCHEMBL2176821.

PTM databases

iPTMnetiQ9WVK7.
PhosphoSitePlusiQ9WVK7.

Proteomic databases

PaxDbiQ9WVK7.
PRIDEiQ9WVK7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000014658; ENSRNOP00000014658; ENSRNOG00000010697.
GeneIDi113965.
KEGGirno:113965.

Organism-specific databases

CTDi3033.
RGDi69321. Hadh.

Phylogenomic databases

eggNOGiKOG2304. Eukaryota.
COG1250. LUCA.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000141498.
HOVERGENiHBG000832.
InParanoidiQ9WVK7.
KOiK00022.
OMAiSPVPMMQ.
OrthoDBiEOG091G089P.
PhylomeDBiQ9WVK7.
TreeFamiTF300886.

Enzyme and pathway databases

UniPathwayiUPA00659.
ReactomeiR-RNO-77310. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
R-RNO-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-RNO-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
R-RNO-77350. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
R-RNO-77352. Beta oxidation of butanoyl-CoA to acetyl-CoA.
SABIO-RKQ9WVK7.

Miscellaneous databases

PROiQ9WVK7.

Gene expression databases

BgeeiENSRNOG00000010697.
GenevisibleiQ9WVK7. RN.

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_RAT
AccessioniPrimary (citable) accession number: Q9WVK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: November 2, 2016
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.