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Q60587

- ECHB_RAT

UniProt

Q60587 - ECHB_RAT

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Protein
Trifunctional enzyme subunit beta, mitochondrial
Gene
Hadhb
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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 intermediate By similarity
Active sitei429 – 4291Proton acceptor By similarity
Active sitei459 – 4591Proton acceptor By similarity

GO - Molecular functioni

  1. 3-hydroxyacyl-CoA dehydrogenase activity Source: RGD
  2. NAD binding Source: RGD
  3. acetyl-CoA C-acyltransferase activity Source: RGD
  4. enoyl-CoA hydratase activity Source: RGD
  5. fatty-acyl-CoA binding Source: RGD
  6. long-chain-3-hydroxyacyl-CoA dehydrogenase activity Source: RGD
  7. long-chain-enoyl-CoA hydratase activity Source: RGD
  8. 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_199139. Acyl chain remodeling of CL.
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: 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. mitochondrial fatty acid beta-oxidation multienzyme complex Source: RGD
  3. mitochondrial inner membrane Source: UniProtKB
  4. mitochondrial nucleoid Source: Ensembl
  5. mitochondrial outer membrane Source: UniProtKB
  6. 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 – 3434Mitochondrion By similarity
Add
BLAST
Chaini35 – 475441Trifunctional enzyme subunit beta, mitochondrial
PRO_0000034084Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531N6-succinyllysine By similarity
Modified residuei73 – 731N6-acetyllysine; alternate By similarity
Modified residuei73 – 731N6-succinyllysine; alternate By similarity
Modified residuei189 – 1891N6-acetyllysine; alternate By similarity
Modified residuei189 – 1891N6-succinyllysine; alternate By similarity
Modified residuei191 – 1911N6-succinyllysine By similarity
Modified residuei273 – 2731N6-succinyllysine By similarity
Modified residuei292 – 2921N6-succinyllysine By similarity
Modified residuei294 – 2941N6-acetyllysine; alternate By similarity
Modified residuei294 – 2941N6-succinyllysine; alternate By similarity
Modified residuei299 – 2991N6-acetyllysine By similarity
Modified residuei333 – 3331N6-acetyllysine; alternate By similarity
Modified residuei333 – 3331N6-succinyllysine; alternate By similarity
Modified residuei349 – 3491N6-acetyllysine By similarity
Modified residuei362 – 3621N6-acetyllysine By 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.1 Publication

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ60587.

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0183.
GeneTreeiENSGT00390000009412.
HOGENOMiHOG000012240.
HOVERGENiHBG104782.
InParanoidiQ60587.
KOiK07509.
OMAiMIVERYP.
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

MTTILTSTFR NLSTTSKWAL RFSVRPLSCS SQVQSAPAVQ TKSKKTLAKP    50
NLKNIVVVEG VRIPFLLSGT SYKDLMPHDL ARAALSGLLY RTNIPKDVVD 100
YIIFGTVIQE VKTSNVAREA ALGAGFSDKT PAHTVTMACI SSNQAMTTAV 150
GLIASGQCDV VVAGGVELMS DVPIRHSRNM RKMMLDLNKA KTLAQRLSLL 200
TKFRLNFLSP ELPAVAEFST NETMGHSADR LAAAFAVSRM EQDKYALRSH 250
SLAKKAQDEG HLSDIVPFKV PGKDTVSKDN GIRPSSLEQM AKLKPAFIKP 300
YGTVTAANSS FLTDGASAML IMSEDRALAM GYKPKAYLRD FIYVSQDPKD 350
QLLLGPTYAT PKVLEKAGLT MNDIDAFEFH EAFSGQILAN FKAMDSDWFA 400
QNYMGRKTKV GAPPLEKFNI WGGSLSLGHP FGATGCRLVM AAANRLRKDG 450
GQYALVAACA AGGQGHAMIV EAYPK 475
Length:475
Mass (Da):51,414
Last modified:November 1, 1997 - v1
Checksum:i59231029C8BA2A13
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D16479 mRNA. Translation: BAA03940.1.
BC060545 mRNA. Translation: AAH60545.1.
PIRiB49681.
RefSeqiNP_598302.1. NM_133618.2.
XP_006239850.1. XM_006239788.1.
XP_006239851.1. XM_006239789.1.
UniGeneiRn.11253.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D16479 mRNA. Translation: BAA03940.1 .
BC060545 mRNA. Translation: AAH60545.1 .
PIRi B49681.
RefSeqi NP_598302.1. NM_133618.2.
XP_006239850.1. XM_006239788.1.
XP_006239851.1. XM_006239789.1.
UniGenei Rn.11253.

3D structure databases

ProteinModelPortali Q60587.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q60587. 2 interactions.
MINTi MINT-4596988.
STRINGi 10116.ENSRNOP00000014637.

Proteomic databases

PaxDbi Q60587.
PRIDEi Q60587.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000014637 ; ENSRNOP00000014637 ; ENSRNOG00000010800 .
GeneIDi 171155.
KEGGi rno:171155.

Organism-specific databases

CTDi 3032.
RGDi 620513. Hadhb.

Phylogenomic databases

eggNOGi COG0183.
GeneTreei ENSGT00390000009412.
HOGENOMi HOG000012240.
HOVERGENi HBG104782.
InParanoidi Q60587.
KOi K07509.
OMAi MIVERYP.
OrthoDBi EOG7DRJ2Z.
PhylomeDBi Q60587.
TreeFami TF315243.

Enzyme and pathway databases

UniPathwayi UPA00659 .
Reactomei REACT_199139. Acyl chain remodeling of CL.

Miscellaneous databases

NextBioi 621992.
PROi Q60587.

Gene expression databases

Genevestigatori Q60587.

Family and domain databases

Gene3Di 3.40.47.10. 4 hits.
InterProi IPR002155. 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 ]
Pfami PF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view ]
SUPFAMi SSF53901. SSF53901. 2 hits.
TIGRFAMsi TIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEi PS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1993) [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(2004) [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(1992) [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: September 3, 2014
This is version 113 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

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