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Protein

Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial

Gene

Hadh

Organism
Mus musculus (Mouse)
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.

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei57 – 571NADBy similarity
Binding sitei73 – 731Coenzyme ABy similarity
Binding sitei80 – 801Coenzyme ABy similarity
Binding sitei122 – 1221NADBy similarity
Binding sitei127 – 1271NADBy similarity
Binding sitei149 – 1491Coenzyme ABy similarity
Binding sitei149 – 1491NADBy similarity
Sitei170 – 1701Important for catalytic activityBy similarity
Binding sitei173 – 1731NADBy similarity
Binding sitei305 – 3051NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 396NADBy similarity

GO - Molecular functioni

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

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-MMU-77310. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
R-MMU-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-MMU-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
R-MMU-77350. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
R-MMU-77352. Beta oxidation of butanoyl-CoA to acetyl-CoA.
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:Hadhsc, Mschad, Schad
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:96009. Hadh.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • mitochondrial inner membrane Source: MGI
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
  • nucleoplasm Source: MGI
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_0000007407Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei75 – 751N6-acetyllysineCombined sources
Modified residuei80 – 801N6-succinyllysineCombined sources
Modified residuei81 – 811N6-acetyllysine; alternateCombined sources
Modified residuei81 – 811N6-succinyllysine; alternateCombined sources
Modified residuei87 – 871N6-acetyllysine; alternateCombined sources
Modified residuei87 – 871N6-succinyllysine; alternateCombined sources
Modified residuei125 – 1251N6-acetyllysineCombined sources
Modified residuei136 – 1361N6-acetyllysine; alternateCombined sources
Modified residuei136 – 1361N6-succinyllysine; alternateCombined sources
Modified residuei179 – 1791N6-acetyllysineCombined sources
Modified residuei185 – 1851N6-acetyllysine; alternateCombined sources
Modified residuei185 – 1851N6-succinyllysine; alternateCombined sources
Modified residuei192 – 1921N6-acetyllysine; alternateCombined sources
Modified residuei192 – 1921N6-succinyllysine; alternateCombined sources
Modified residuei202 – 2021N6-acetyllysine; alternateCombined sources
Modified residuei202 – 2021N6-succinyllysine; alternateCombined sources
Modified residuei206 – 2061N6-succinyllysineCombined sources
Modified residuei212 – 2121N6-acetyllysine; alternateCombined sources
Modified residuei212 – 2121N6-succinyllysine; alternateCombined sources
Modified residuei241 – 2411N6-acetyllysine; alternateCombined sources
Modified residuei241 – 2411N6-succinyllysine; alternateCombined sources
Modified residuei312 – 3121N6-acetyllysine; alternateBy similarity
Modified residuei312 – 3121N6-succinyllysine; alternateCombined sources

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ61425.
MaxQBiQ61425.
PaxDbiQ61425.
PeptideAtlasiQ61425.
PRIDEiQ61425.

2D gel databases

REPRODUCTION-2DPAGEQ61425.
SWISS-2DPAGEQ61425.

PTM databases

iPTMnetiQ61425.
PhosphoSiteiQ61425.
SwissPalmiQ61425.

Expressioni

Gene expression databases

BgeeiQ61425.
CleanExiMM_HADH.
GenevisibleiQ61425. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ61425. 4 interactions.
MINTiMINT-1859897.
STRINGi10090.ENSMUSP00000029610.

Structurei

3D structure databases

ProteinModelPortaliQ61425.
SMRiQ61425. Positions 23-314.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2304. Eukaryota.
COG1250. LUCA.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000141498.
HOVERGENiHBG000832.
InParanoidiQ61425.
KOiK00022.
OMAiCPLLKEM.
OrthoDBiEOG7K3TMS.
PhylomeDBiQ61425.
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.

Q61425-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFVTRQFLR SMSSSSSASA AAKKILIKHV TVIGGGLMGA GIAQVAAATG
60 70 80 90 100
HTVVLVDQTE DILAKSKKGI EESLKRMAKK KFTENPKAGD EFVEKTLSCL
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 VRLHERGDAS KEDIDTAMKL
260 270 280 290 300
GAGYPMGPFE LLDYVGLDTT KFILDGWHEM EPENPLFQPS PSMNNLVAQK
310
KLGKKTGEGF YKYK
Length:314
Mass (Da):34,464
Last modified:June 6, 2002 - v2
Checksum:i366A4C075F708BC1
GO

Sequence cautioni

The sequence BAA06122.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111S → Y in BAE40188 (PubMed:16141072).Curated
Sequence conflicti56 – 561V → M in BAE41023 (PubMed:16141072).Curated
Sequence conflicti111 – 1111H → D in BAA06122 (PubMed:7642117).Curated
Sequence conflicti146 – 1461S → G in BAE40188 (PubMed:16141072).Curated
Sequence conflicti211 – 2111C → S in BAA06122 (PubMed:7642117).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D29639 mRNA. Translation: BAA06122.1. Different initiation.
AF375597, AF375596 Genomic DNA. Translation: AAK54642.1.
AK132260 mRNA. Translation: BAE21064.1.
AK148486 mRNA. Translation: BAE28581.1.
AK167024 mRNA. Translation: BAE39197.1.
AK168238 mRNA. Translation: BAE40188.1.
AK168877 mRNA. Translation: BAE40695.1.
AK169261 mRNA. Translation: BAE41023.1.
BC028833 mRNA. Translation: AAH28833.1.
BC064712 mRNA. Translation: AAH64712.1.
CCDSiCCDS38640.1.
PIRiJC4210.
RefSeqiNP_032238.2. NM_008212.4.
UniGeneiMm.260164.

Genome annotation databases

EnsembliENSMUST00000029610; ENSMUSP00000029610; ENSMUSG00000027984.
GeneIDi15107.
KEGGimmu:15107.
UCSCiuc008rjl.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D29639 mRNA. Translation: BAA06122.1. Different initiation.
AF375597, AF375596 Genomic DNA. Translation: AAK54642.1.
AK132260 mRNA. Translation: BAE21064.1.
AK148486 mRNA. Translation: BAE28581.1.
AK167024 mRNA. Translation: BAE39197.1.
AK168238 mRNA. Translation: BAE40188.1.
AK168877 mRNA. Translation: BAE40695.1.
AK169261 mRNA. Translation: BAE41023.1.
BC028833 mRNA. Translation: AAH28833.1.
BC064712 mRNA. Translation: AAH64712.1.
CCDSiCCDS38640.1.
PIRiJC4210.
RefSeqiNP_032238.2. NM_008212.4.
UniGeneiMm.260164.

3D structure databases

ProteinModelPortaliQ61425.
SMRiQ61425. Positions 23-314.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ61425. 4 interactions.
MINTiMINT-1859897.
STRINGi10090.ENSMUSP00000029610.

PTM databases

iPTMnetiQ61425.
PhosphoSiteiQ61425.
SwissPalmiQ61425.

2D gel databases

REPRODUCTION-2DPAGEQ61425.
SWISS-2DPAGEQ61425.

Proteomic databases

EPDiQ61425.
MaxQBiQ61425.
PaxDbiQ61425.
PeptideAtlasiQ61425.
PRIDEiQ61425.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029610; ENSMUSP00000029610; ENSMUSG00000027984.
GeneIDi15107.
KEGGimmu:15107.
UCSCiuc008rjl.2. mouse.

Organism-specific databases

CTDi3033.
MGIiMGI:96009. Hadh.

Phylogenomic databases

eggNOGiKOG2304. Eukaryota.
COG1250. LUCA.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000141498.
HOVERGENiHBG000832.
InParanoidiQ61425.
KOiK00022.
OMAiCPLLKEM.
OrthoDBiEOG7K3TMS.
PhylomeDBiQ61425.
TreeFamiTF300886.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiHadh. mouse.
PROiQ61425.
SOURCEiSearch...

Gene expression databases

BgeeiQ61425.
CleanExiMM_HADH.
GenevisibleiQ61425. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of a cDNA clone encoding mouse 3-hydroxyacyl CoA dehydrogenase."
    Nomura M., Takihara Y., Shimada K.
    Gene 160:309-310(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Mouse medium and short chain L-3-hydroxyacyl-coenzyme A dehydrogenase gene."
    O'Brien L.K., Sims H.F., Strauss A.W.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Amnion, Extraembryonic tissue, Pancreas and Placenta.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney and Liver.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION AT LYS-81, DESUCCINYLATION BY SIRT5, ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-241, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-80; LYS-81; LYS-87; LYS-136; LYS-185; LYS-192; LYS-202; LYS-206; LYS-212; LYS-241 AND LYS-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  7. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-75; LYS-81; LYS-87; LYS-125; LYS-136; LYS-179; LYS-185; LYS-192; LYS-202; LYS-212 AND LYS-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiHCDH_MOUSE
AccessioniPrimary (citable) accession number: Q61425
Secondary accession number(s): Q3TF75
, Q3THK8, Q3UFI0, Q8K149, Q925U9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 6, 2002
Last modified: July 6, 2016
This is version 147 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.