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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: 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
Active sitei139Acyl-thioester intermediateBy similarity1
Active sitei429Proton acceptorPROSITE-ProRule annotation1
Active sitei459Proton acceptorPROSITE-ProRule annotation1

GO - Molecular functioni

  • 3-hydroxyacyl-CoA dehydrogenase activity Source: RGD
  • acetyl-CoA C-acyltransferase activity Source: RGD
  • enoyl-CoA hydratase activity Source: RGD
  • fatty-acyl-CoA binding Source: RGD
  • long-chain-3-hydroxyacyl-CoA dehydrogenase activity Source: RGD
  • long-chain-enoyl-CoA hydratase activity Source: RGD
  • NAD binding Source: RGD
  • protein complex binding Source: RGD

GO - Biological processi

  • 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

ReactomeiR-RNO-1482798. Acyl chain remodeling of CL.
R-RNO-77285. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
R-RNO-77305. Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
R-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.
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
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi620513. Hadhb.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • mitochondrial fatty acid beta-oxidation multienzyme complex Source: RGD
  • mitochondrial inner membrane Source: UniProtKB
  • mitochondrial outer membrane Source: UniProtKB
  • 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)DescriptionActionsGraphical viewLength
Transit peptidei1 – 34MitochondrionBy similarityAdd BLAST34
ChainiPRO_000003408435 – 475Trifunctional enzyme subunit beta, mitochondrialAdd BLAST441

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei53N6-succinyllysineBy similarity1
Modified residuei73N6-acetyllysine; alternateBy similarity1
Modified residuei73N6-succinyllysine; alternateBy similarity1
Modified residuei189N6-acetyllysine; alternateBy similarity1
Modified residuei189N6-succinyllysine; alternateBy similarity1
Modified residuei191N6-succinyllysineBy similarity1
Modified residuei273N6-succinyllysineBy similarity1
Modified residuei292N6-succinyllysineBy similarity1
Modified residuei294N6-acetyllysine; alternateBy similarity1
Modified residuei294N6-succinyllysine; alternateBy similarity1
Modified residuei299N6-acetyllysineBy similarity1
Modified residuei333N6-acetyllysine; alternateBy similarity1
Modified residuei333N6-succinyllysine; alternateBy similarity1
Modified residuei349N6-acetyllysineBy similarity1
Modified residuei362N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ60587.
PRIDEiQ60587.

PTM databases

iPTMnetiQ60587.
PhosphoSitePlusiQ60587.

Expressioni

Gene expression databases

BgeeiENSRNOG00000010800.
ExpressionAtlasiQ60587. baseline and differential.
GenevisibleiQ60587. RN.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • protein complex binding Source: RGD

Protein-protein interaction databases

IntActiQ60587. 2 interactors.
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

eggNOGiKOG1392. Eukaryota.
COG0183. LUCA.
GeneTreeiENSGT00760000119318.
HOGENOMiHOG000012240.
HOVERGENiHBG104782.
InParanoidiQ60587.
KOiK07509.
PhylomeDBiQ60587.
TreeFamiTF315243.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
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_006239848.2. XM_006239786.2.
XP_006239850.1. XM_006239788.1.
XP_006239851.1. XM_006239789.3.
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_006239848.2. XM_006239786.2.
XP_006239850.1. XM_006239788.1.
XP_006239851.1. XM_006239789.3.
UniGeneiRn.11253.

3D structure databases

ProteinModelPortaliQ60587.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ60587.
PhosphoSitePlusiQ60587.

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

eggNOGiKOG1392. Eukaryota.
COG0183. LUCA.
GeneTreeiENSGT00760000119318.
HOGENOMiHOG000012240.
HOVERGENiHBG104782.
InParanoidiQ60587.
KOiK07509.
PhylomeDBiQ60587.
TreeFamiTF315243.

Enzyme and pathway databases

UniPathwayiUPA00659.
ReactomeiR-RNO-1482798. Acyl chain remodeling of CL.
R-RNO-77285. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
R-RNO-77305. Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
R-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.

Miscellaneous databases

PROiQ60587.

Gene expression databases

BgeeiENSRNOG00000010800.
ExpressionAtlasiQ60587. baseline and differential.
GenevisibleiQ60587. RN.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
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...

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: November 2, 2016
This is version 129 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.