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Protein

Trifunctional enzyme subunit beta, mitochondrial

Gene

Hadhb

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

Functioni

Catalytic activityi

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei139 – 1391Acyl-thioester intermediateBy similarity
Active sitei429 – 4291Proton acceptorPROSITE-ProRule annotation
Active sitei459 – 4591Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. 3-hydroxyacyl-CoA dehydrogenase activity Source: RGD
  2. acetyl-CoA C-acyltransferase activity Source: RGD
  3. enoyl-CoA hydratase activity Source: RGD
  4. fatty-acyl-CoA binding Source: RGD
  5. long-chain-3-hydroxyacyl-CoA dehydrogenase activity Source: RGD
  6. long-chain-enoyl-CoA hydratase activity Source: RGD
  7. NAD binding Source: RGD
  8. poly(A) RNA binding Source: Ensembl
  9. protein complex binding Source: RGD

GO - Biological processi

  1. fatty acid beta-oxidation Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

ReactomeiREACT_275090. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
REACT_279487. Acyl chain remodeling of CL.
REACT_289411. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
REACT_292108. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
REACT_299914. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
REACT_312223. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
REACT_354247. Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Trifunctional enzyme subunit beta, mitochondrial
Alternative name(s):
TP-beta
Including the following 1 domains:
3-ketoacyl-CoA thiolase (EC:2.3.1.16)
Alternative name(s):
Acetyl-CoA acyltransferase
Beta-ketothiolase
Gene namesi
Name:Hadhb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi620513. Hadhb.

Subcellular locationi

Mitochondrion By similarity. Mitochondrion inner membrane By similarity. Mitochondrion outer membrane By similarity. Endoplasmic reticulum By similarity

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. extracellular vesicular exosome Source: Ensembl
  3. mitochondrial fatty acid beta-oxidation multienzyme complex Source: RGD
  4. mitochondrial inner membrane Source: UniProtKB
  5. mitochondrial nucleoid Source: Ensembl
  6. mitochondrial outer membrane Source: UniProtKB
  7. mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion inner membrane, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3434MitochondrionBy similarityAdd
BLAST
Chaini35 – 475441Trifunctional enzyme subunit beta, mitochondrialPRO_0000034084Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531N6-succinyllysineBy similarity
Modified residuei73 – 731N6-acetyllysine; alternateBy similarity
Modified residuei73 – 731N6-succinyllysine; alternateBy similarity
Modified residuei189 – 1891N6-acetyllysine; alternateBy similarity
Modified residuei189 – 1891N6-succinyllysine; alternateBy similarity
Modified residuei191 – 1911N6-succinyllysineBy similarity
Modified residuei273 – 2731N6-succinyllysineBy similarity
Modified residuei292 – 2921N6-succinyllysineBy similarity
Modified residuei294 – 2941N6-acetyllysine; alternateBy similarity
Modified residuei294 – 2941N6-succinyllysine; alternateBy similarity
Modified residuei299 – 2991N6-acetyllysineBy similarity
Modified residuei333 – 3331N6-acetyllysine; alternateBy similarity
Modified residuei333 – 3331N6-succinyllysine; alternateBy similarity
Modified residuei349 – 3491N6-acetyllysineBy similarity
Modified residuei362 – 3621N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ60587.
PRIDEiQ60587.

Expressioni

Gene expression databases

GenevestigatoriQ60587.

Interactioni

Subunit structurei

Octamer of 4 alpha (HADHA) and 4 beta (HADHB) subunits. Interacts with RSAD2/viperin (By similarity).By similarity

Protein-protein interaction databases

IntActiQ60587. 2 interactions.
MINTiMINT-4596988.
STRINGi10116.ENSRNOP00000014637.

Structurei

3D structure databases

ProteinModelPortaliQ60587.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0183.
GeneTreeiENSGT00760000119318.
HOGENOMiHOG000012240.
HOVERGENiHBG104782.
InParanoidiQ60587.
KOiK07509.
OMAiIDVWEDM.
OrthoDBiEOG7DRJ2Z.
PhylomeDBiQ60587.
TreeFamiTF315243.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q60587-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTILTSTFR NLSTTSKWAL RFSVRPLSCS SQVQSAPAVQ TKSKKTLAKP
60 70 80 90 100
NLKNIVVVEG VRIPFLLSGT SYKDLMPHDL ARAALSGLLY RTNIPKDVVD
110 120 130 140 150
YIIFGTVIQE VKTSNVAREA ALGAGFSDKT PAHTVTMACI SSNQAMTTAV
160 170 180 190 200
GLIASGQCDV VVAGGVELMS DVPIRHSRNM RKMMLDLNKA KTLAQRLSLL
210 220 230 240 250
TKFRLNFLSP ELPAVAEFST NETMGHSADR LAAAFAVSRM EQDKYALRSH
260 270 280 290 300
SLAKKAQDEG HLSDIVPFKV PGKDTVSKDN GIRPSSLEQM AKLKPAFIKP
310 320 330 340 350
YGTVTAANSS FLTDGASAML IMSEDRALAM GYKPKAYLRD FIYVSQDPKD
360 370 380 390 400
QLLLGPTYAT PKVLEKAGLT MNDIDAFEFH EAFSGQILAN FKAMDSDWFA
410 420 430 440 450
QNYMGRKTKV GAPPLEKFNI WGGSLSLGHP FGATGCRLVM AAANRLRKDG
460 470
GQYALVAACA AGGQGHAMIV EAYPK
Length:475
Mass (Da):51,414
Last modified:November 1, 1997 - v1
Checksum:i59231029C8BA2A13
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16479 mRNA. Translation: BAA03940.1.
BC060545 mRNA. Translation: AAH60545.1.
PIRiB49681.
RefSeqiNP_598302.1. NM_133618.3.
XP_006239850.1. XM_006239788.1.
XP_006239851.1. XM_006239789.2.
UniGeneiRn.11253.

Genome annotation databases

EnsembliENSRNOT00000014637; ENSRNOP00000014637; ENSRNOG00000010800.
GeneIDi171155.
KEGGirno:171155.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16479 mRNA. Translation: BAA03940.1.
BC060545 mRNA. Translation: AAH60545.1.
PIRiB49681.
RefSeqiNP_598302.1. NM_133618.3.
XP_006239850.1. XM_006239788.1.
XP_006239851.1. XM_006239789.2.
UniGeneiRn.11253.

3D structure databases

ProteinModelPortaliQ60587.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ60587. 2 interactions.
MINTiMINT-4596988.
STRINGi10116.ENSRNOP00000014637.

Proteomic databases

PaxDbiQ60587.
PRIDEiQ60587.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000014637; ENSRNOP00000014637; ENSRNOG00000010800.
GeneIDi171155.
KEGGirno:171155.

Organism-specific databases

CTDi3032.
RGDi620513. Hadhb.

Phylogenomic databases

eggNOGiCOG0183.
GeneTreeiENSGT00760000119318.
HOGENOMiHOG000012240.
HOVERGENiHBG104782.
InParanoidiQ60587.
KOiK07509.
OMAiIDVWEDM.
OrthoDBiEOG7DRJ2Z.
PhylomeDBiQ60587.
TreeFamiTF315243.

Enzyme and pathway databases

UniPathwayiUPA00659.
ReactomeiREACT_275090. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
REACT_279487. Acyl chain remodeling of CL.
REACT_289411. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
REACT_292108. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
REACT_299914. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
REACT_312223. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
REACT_354247. Beta oxidation of palmitoyl-CoA to myristoyl-CoA.

Miscellaneous databases

NextBioi621992.
PROiQ60587.

Gene expression databases

GenevestigatoriQ60587.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the cDNAs for the subunits of rat mitochondrial fatty acid beta-oxidation multienzyme complex. Structural and functional relationships to other mitochondrial and peroxisomal beta-oxidation enzymes."
    Kamijo T., Aoyama T., Miyazaki J., Hashimoto T.
    J. Biol. Chem. 268:26452-26460(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
  2. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary.
  3. "Novel fatty acid beta-oxidation enzymes in rat liver mitochondria. II. Purification and properties of enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein."
    Uchida Y., Izai K., Orii T., Hashimoto T.
    J. Biol. Chem. 267:1034-1041(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.

Entry informationi

Entry nameiECHB_RAT
AccessioniPrimary (citable) accession number: Q60587
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 1, 2015
This is version 119 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

External Data

Dasty 3

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 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.