SubmitCancel

Skip Header

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

P00348

- HCDH_PIG

UniProt

P00348 - HCDH_PIG

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial

Gene
HADH, HAD, HADHSC, SCHAD
Organism
Sus scrofa (Pig)
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei57 – 571NAD
Binding sitei73 – 731Coenzyme A By similarity
Binding sitei80 – 801Coenzyme A By similarity
Binding sitei122 – 1221NAD
Binding sitei127 – 1271NAD
Binding sitei149 – 1491Coenzyme A By similarity
Binding sitei149 – 1491NAD
Sitei170 – 1701Important for catalytic activity By similarity
Binding sitei173 – 1731NAD By similarity
Binding sitei305 – 3051NAD By similarity

Regions

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

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

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: Chromosome 8

Subcellular locationi

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 – 1212Mitochondrion By similarityAdd
BLAST
Chaini13 – 314302Hydroxyacyl-coenzyme A dehydrogenase, mitochondrialPRO_0000007408Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP00348.
PRIDEiP00348.

Interactioni

Subunit structurei

Homodimer.

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 – 335
Helixi37 – 4812
Beta strandi52 – 565
Helixi60 – 8122
Turni82 – 843
Helixi86 – 9813
Beta strandi100 – 1045
Helixi106 – 1083
Beta strandi110 – 1123
Beta strandi114 – 1185
Helixi124 – 13714
Beta strandi143 – 1464
Beta strandi149 – 1513
Helixi153 – 1575
Helixi163 – 1653
Beta strandi166 – 1705
Turni175 – 1773
Beta strandi180 – 1856
Helixi191 – 20313
Beta strandi207 – 2137
Turni215 – 2184
Helixi219 – 23517
Helixi241 – 25212
Helixi258 – 2658
Helixi267 – 27913
Turni280 – 2834
Helixi285 – 2873
Helixi291 – 2988
Turni304 – 3074
Beta strandi308 – 3125

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HDHX-ray2.80A/B/C13-314[»]
ProteinModelPortaliP00348.
SMRiP00348. Positions 24-314.

Miscellaneous databases

EvolutionaryTraceiP00348.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1250.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000141498.
HOVERGENiHBG000832.
KOiK00022.
OMAiNEAIFAY.
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

MAFATRQLVR SLSSSSTAAA SAKKILVKHV TVIGGGLMGA GIAQVAAATG    50
HTVVLVDQTE DILAKSKKGI EESLRKVAKK KFAENPKAGD EFVEKTLSSI 100
STSTDAASVV HSTDLVVEAI VENLKVKSEL FKRLDKFAAE HTIFASNTSS 150
LQITSLANAT TRQDRFAGLH FFNPVPLMKL VEVVKTPMTS QKTLESLVDF 200
SKTLGKHPVS CKDTPGFIVN RLLVPYLIEA VRLYERGDAS KEDIDTAMKL 250
GAGYPMGPFE LLDYVGLDTT KFIIDGWHEM DSQNPLFQPS PAMNKLVAEN 300
KFGKKTGEGF YKYK 314
Length:314
Mass (Da):34,161
Last modified:May 30, 2000 - v2
Checksum:i596CBFD227214C3B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti108 – 1081S → A AA sequence 1 Publication
Sequence conflicti122 – 1221E → EQLKVVGE AA sequence 1 Publication
Sequence conflicti172 – 1743FNP → N AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF027652 mRNA. Translation: AAD20939.1 .
PIRi T46866.
RefSeqi NP_999496.1. NM_214331.1.
UniGenei Ssc.12507.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3HDH X-ray 2.80 A/B/C 13-314 [» ]
ProteinModelPortali P00348.
SMRi P00348. Positions 24-314.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9823.ENSSSCP00000009757.

Proteomic databases

PaxDbi P00348.
PRIDEi P00348.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSSSCT00000010020 ; ENSSSCP00000009757 ; ENSSSCG00000009150 .
GeneIDi 397604.
KEGGi ssc:397604.

Organism-specific databases

CTDi 3033.

Phylogenomic databases

eggNOGi COG1250.
GeneTreei ENSGT00720000108673.
HOGENOMi HOG000141498.
HOVERGENi HBG000832.
KOi K00022.
OMAi NEAIFAY.
OrthoDBi EOG7K3TMS.
TreeFami TF300886.

Enzyme and pathway databases

UniPathwayi UPA00659 .

Miscellaneous databases

EvolutionaryTracei P00348.

Family and domain databases

Gene3Di 1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProi 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 ]
Pfami PF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000105. HCDH. 1 hit.
SUPFAMi SSF48179. SSF48179. 1 hit.
PROSITEi PS00067. 3HCDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1998) [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(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.

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: September 3, 2014
This is version 123 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