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Protein

Trifunctional enzyme subunit beta, mitochondrial

Gene

HADHB

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei139 – 1391Acyl-thioester intermediateBy similarity
Active sitei429 – 4291Proton acceptorPROSITE-ProRule annotation
Active sitei459 – 4591Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-BTA-1482798. Acyl chain remodeling of CL.
R-BTA-77285. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
R-BTA-77305. Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
R-BTA-77310. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
R-BTA-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-BTA-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
R-BTA-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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 11

Subcellular locationi

GO - Cellular componenti

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 – 3434MitochondrionSequence analysisAdd
BLAST
Chaini35 – 475441Trifunctional enzyme subunit beta, mitochondrialPRO_0000034079Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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 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

PaxDbiO46629.
PRIDEiO46629.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000013310.

Structurei

3D structure databases

ProteinModelPortaliO46629.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1392. Eukaryota.
COG0183. LUCA.
GeneTreeiENSGT00760000119318.
HOVERGENiHBG104782.
InParanoidiO46629.
KOiK07509.
OMAiMTAFPEP.
OrthoDBiEOG7DRJ2Z.
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.

O46629-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISLLTYTLK NLPNTSKWAL RFCMRPLSSS SQLQAAAASQ TKSKKTLAKP
60 70 80 90 100
NIRNIVVVDG VRTPFLLSGT SYKDLMPHDL ARAALSGLLH RTSVPKDVVD
110 120 130 140 150
YIIFGTVIQE VKTSNVAREA ALGAGFSDKT PAHTVTMACI SSNQAMTTAV
160 170 180 190 200
GLIASGQCDV VVAGGVELMS DIPIRHSRKM RKMMLDLNKA KTLAQRLSII
210 220 230 240 250
SKFRLNFLSP ELPAVSEFST SETMGHSADR LAAAFAISRE EQDEYALRSH
260 270 280 290 300
SLAKKAQDEG LLSDVVPFKV PGRDTVTQDN GIRPSSLDQM AKLKPAFIKP
310 320 330 340 350
YGTVTAANSS FLTDGASAVL IMAEEKALAM GYKPKAYLRD FMYVSQDPKD
360 370 380 390 400
QLLLGPTYAT PKVLEKAGLT MNDIDVFEFH EAFSGQILAN LKAMDSDWFA
410 420 430 440 450
QNYMGRKAKV GLPPLEKFNN WGGSLSLGHP FGATGCRLVM AAANRLRKEG
460 470
GQYGLVAACA AGGQGHAMIV EAYPK
Length:475
Mass (Da):51,345
Last modified:June 1, 1998 - v1
Checksum:i5B55321E0337E197
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ003066 mRNA. Translation: CAA05840.1.
BC102638 mRNA. Translation: AAI02639.1.
RefSeqiNP_776761.1. NM_174336.3.
XP_005212988.1. XM_005212931.2.
UniGeneiBt.52915.

Genome annotation databases

EnsembliENSBTAT00000013310; ENSBTAP00000013310; ENSBTAG00000010083.
ENSBTAT00000063404; ENSBTAP00000055705; ENSBTAG00000010083.
GeneIDi281811.
KEGGibta:281811.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ003066 mRNA. Translation: CAA05840.1.
BC102638 mRNA. Translation: AAI02639.1.
RefSeqiNP_776761.1. NM_174336.3.
XP_005212988.1. XM_005212931.2.
UniGeneiBt.52915.

3D structure databases

ProteinModelPortaliO46629.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000013310.

Proteomic databases

PaxDbiO46629.
PRIDEiO46629.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000013310; ENSBTAP00000013310; ENSBTAG00000010083.
ENSBTAT00000063404; ENSBTAP00000055705; ENSBTAG00000010083.
GeneIDi281811.
KEGGibta:281811.

Organism-specific databases

CTDi3032.

Phylogenomic databases

eggNOGiKOG1392. Eukaryota.
COG0183. LUCA.
GeneTreeiENSGT00760000119318.
HOVERGENiHBG104782.
InParanoidiO46629.
KOiK07509.
OMAiMTAFPEP.
OrthoDBiEOG7DRJ2Z.
TreeFamiTF315243.

Enzyme and pathway databases

UniPathwayiUPA00659.
ReactomeiR-BTA-1482798. Acyl chain remodeling of CL.
R-BTA-77285. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
R-BTA-77305. Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
R-BTA-77310. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
R-BTA-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-BTA-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
R-BTA-77350. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.

Miscellaneous databases

NextBioi20805723.

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...

Publicationsi

« Hide 'large scale' publications
  1. Cailleret K., Chevet E., Lemaitre G., Dahan S., Bergeron J.J., Katinka M.D.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.

Entry informationi

Entry nameiECHB_BOVIN
AccessioniPrimary (citable) accession number: O46629
Secondary accession number(s): Q3SZZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: November 11, 2015
This is version 112 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.