UniProtKB - Q99JY0 (ECHB_MOUSE)
Protein
Trifunctional enzyme subunit beta, mitochondrial
Gene
Hadhb
Organism
Mus musculus (Mouse)
Status
Functioni
Mitochondrial trifunctional enzyme catalyzes the last three of the four reactions of the mitochondrial beta-oxidation pathway. The mitochondrial beta-oxidation pathway is the major energy-producing process in tissues and is performed through four consecutive reactions breaking down fatty acids into acetyl-CoA. Among the enzymes involved in this pathway, the trifunctional enzyme exhibits specificity for long-chain fatty acids. Mitochondrial trifunctional enzyme is a heterotetrameric complex composed of two proteins, the trifunctional enzyme subunit alpha/HADHA carries the 2,3-enoyl-CoA hydratase and the 3-hydroxyacyl-CoA dehydrogenase activities, while the trifunctional enzyme subunit beta/HADHB described here bears the 3-ketoacyl-CoA thiolase activity.By similarity
Catalytic activityi
- EC:2.3.1.16By similarityThis reaction proceeds in the backwardBy similarity direction.
- This reaction proceeds in the backwardBy similarity direction.
- This reaction proceeds in the backwardBy similarity direction.
- This reaction proceeds in the backwardBy similarity direction.
- This reaction proceeds in the backwardBy similarity direction.
- This reaction proceeds in the backwardBy similarity direction.
- EC:2.3.1.155By similarityThis reaction proceeds in the backwardBy similarity direction.
: fatty acid beta-oxidation Pathwayi
This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.By similarityView all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 139 | Acyl-thioester intermediateBy similarity | 1 | |
Sitei | 429 | Increases nucleophilicity of active site CysBy similarity | 1 | |
Active sitei | 459 | Proton donor/acceptorBy similarity | 1 |
GO - Molecular functioni
- acetyl-CoA C-acyltransferase activity Source: MGI
- acetyl-CoA C-myristoyltransferase activity Source: UniProtKB-EC
- protein-containing complex binding Source: MGI
GO - Biological processi
- fatty acid beta-oxidation Source: MGI
Keywordsi
Molecular function | Acyltransferase, Transferase |
Biological process | Fatty acid metabolism, Lipid metabolism |
Enzyme and pathway databases
Reactomei | R-MMU-1482798, Acyl chain remodeling of CL R-MMU-77285, Beta oxidation of myristoyl-CoA to lauroyl-CoA R-MMU-77305, Beta oxidation of palmitoyl-CoA to myristoyl-CoA R-MMU-77310, Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA R-MMU-77346, Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA R-MMU-77348, Beta oxidation of octanoyl-CoA to hexanoyl-CoA R-MMU-77350, Beta oxidation of hexanoyl-CoA to butanoyl-CoA |
UniPathwayi | UPA00659 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:Hadhb |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:2136381, Hadhb |
Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum By similarity
Mitochondrion
- Mitochondrion By similarity
- Mitochondrion inner membrane By similarity
- Mitochondrion outer membrane By similarity
Note: Protein stability and association with membranes require HADHA.By similarity
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB
Mitochondrion
- mitochondrial fatty acid beta-oxidation multienzyme complex Source: MGI
- mitochondrial inner membrane Source: MGI
- mitochondrial nucleoid Source: MGI
- mitochondrial outer membrane Source: UniProtKB
- mitochondrion Source: MGI
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Intramembranei | 174 – 221 | By similarityAdd BLAST | 48 |
Keywords - Cellular componenti
Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion inner membrane, Mitochondrion outer membranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 34 | MitochondrionBy similarityAdd BLAST | 34 | |
ChainiPRO_0000034082 | 35 – 475 | Trifunctional enzyme subunit beta, mitochondrialAdd BLAST | 441 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 53 | N6-succinyllysineCombined sources | 1 | |
Modified residuei | 73 | N6-acetyllysine; alternateCombined sources | 1 | |
Modified residuei | 73 | N6-succinyllysine; alternateCombined sources | 1 | |
Modified residuei | 189 | N6-acetyllysine; alternateCombined sources | 1 | |
Modified residuei | 189 | N6-succinyllysine; alternateCombined sources | 1 | |
Modified residuei | 191 | N6-succinyllysineCombined sources | 1 | |
Modified residuei | 273 | N6-succinyllysineCombined sources | 1 | |
Modified residuei | 292 | N6-succinyllysineCombined sources | 1 | |
Modified residuei | 294 | N6-acetyllysine; alternateCombined sources | 1 | |
Modified residuei | 294 | N6-succinyllysine; alternateCombined sources | 1 | |
Modified residuei | 299 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 333 | N6-acetyllysine; alternateCombined sources | 1 | |
Modified residuei | 333 | N6-succinyllysine; alternateCombined sources | 1 | |
Modified residuei | 349 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 362 | N6-acetyllysineCombined sources | 1 |
Post-translational modificationi
Acetylation of Lys-202 is observed in liver mitochondria from fasted mice but not from fed mice.
Keywords - PTMi
AcetylationProteomic databases
EPDi | Q99JY0 |
jPOSTi | Q99JY0 |
MaxQBi | Q99JY0 |
PaxDbi | Q99JY0 |
PeptideAtlasi | Q99JY0 |
PRIDEi | Q99JY0 |
PTM databases
iPTMneti | Q99JY0 |
PhosphoSitePlusi | Q99JY0 |
SwissPalmi | Q99JY0 |
Expressioni
Gene expression databases
Bgeei | ENSMUSG00000059447, Expressed in brown adipose tissue and 206 other tissues |
Genevisiblei | Q99JY0, MM |
Interactioni
Subunit structurei
Heterotetramer of 2 alpha/HADHA and 2 beta/HADHB subunits; forms the mitochondrial trifunctional enzyme. Also purified as higher order heterooligomers including a 4 alpha/HADHA and 4 beta/HADHB heterooligomer which physiological significance remains unclear.
Interacts with RSAD2/viperin.
By similarityProtein-protein interaction databases
BioGRIDi | 231080, 27 interactors |
IntActi | Q99JY0, 8 interactors |
MINTi | Q99JY0 |
STRINGi | 10090.ENSMUSP00000110434 |
Miscellaneous databases
RNActi | Q99JY0, protein |
Family & Domainsi
Sequence similaritiesi
Keywords - Domaini
Transit peptidePhylogenomic databases
eggNOGi | KOG1392, Eukaryota |
GeneTreei | ENSGT01010000222371 |
HOGENOMi | CLU_031026_2_0_1 |
InParanoidi | Q99JY0 |
OMAi | MTAFPEP |
OrthoDBi | 1129049at2759 |
PhylomeDBi | Q99JY0 |
TreeFami | TF315243 |
Family and domain databases
CDDi | cd00751, thiolase, 1 hit |
Gene3Di | 3.40.47.10, 1 hit |
InterProi | View protein in InterPro IPR002155, Thiolase IPR016039, Thiolase-like IPR020615, Thiolase_acyl_enz_int_AS IPR020610, Thiolase_AS IPR020617, Thiolase_C IPR020613, Thiolase_CS IPR020616, Thiolase_N |
Pfami | View protein in Pfam PF02803, Thiolase_C, 1 hit PF00108, Thiolase_N, 1 hit |
SUPFAMi | SSF53901, SSF53901, 2 hits |
TIGRFAMsi | TIGR01930, AcCoA-C-Actrans, 1 hit |
PROSITEi | View protein in PROSITE PS00098, THIOLASE_1, 1 hit PS00737, THIOLASE_2, 1 hit PS00099, THIOLASE_3, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
Q99JY0-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTTILTSTFR NLSTTSKWAL RSSIRPLSCS SQLHSAPAVQ TKSKKTLAKP
60 70 80 90 100
NMKNIVVVEG VRIPFLLSGT SYKDLMPHDL ARAALSGLLH RTNIPKDVVD
110 120 130 140 150
YIIFGTVIQE VKTSNVAREA ALGAGFSDKT PAHTVTMACI SSNQAMTTAV
160 170 180 190 200
GLIASGQCDV VVAGGVELMS DVPIRHSRNM RKMMLDLNKA KTLGQRLSLL
210 220 230 240 250
SKFRLNFLSP ELPAVAEFST NETMGHSADR LAAAFAVSRM EQDEYALRSH
260 270 280 290 300
SLAKKAQDEG HLSDIVPFKV PGKDTVTKDN 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 GSPPLEKFNI WGGSLSLGHP FGATGCRLVM AAANRLRKDG
460 470
GQYALVAACA AGGQGHAMIV EAYPK
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketD3YXU1 | D3YXU1_MOUSE | Trifunctional enzyme subunit beta, ... | Hadhb | 173 | Annotation score: | ||
A0A0G2JER1 | A0A0G2JER1_MOUSE | Trifunctional enzyme subunit beta, ... | Hadhb | 41 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 24 – 25 | IR → HK in BAC36493 (PubMed:16141072).Curated | 2 | |
Sequence conflicti | 425 | L → M in BAC38790 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 450 | G → R in BAC38790 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 450 | G → V in BAC39015 (PubMed:16141072).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AK033462 mRNA Translation: BAC28300.1 AK076814 mRNA Translation: BAC36493.1 AK083164 mRNA Translation: BAC38790.1 AK083767 mRNA Translation: BAC39015.1 AK150889 mRNA Translation: BAE29936.1 AK169637 mRNA Translation: BAE41269.1 BC005585 mRNA Translation: AAH05585.1 |
CCDSi | CCDS39045.1 |
RefSeqi | NP_001276727.1, NM_001289798.1 NP_001276728.1, NM_001289799.1 NP_663533.1, NM_145558.2 XP_017176317.1, XM_017320828.1 XP_017176318.1, XM_017320829.1 |
Genome annotation databases
Ensembli | ENSMUST00000026841; ENSMUSP00000026841; ENSMUSG00000059447 ENSMUST00000114783; ENSMUSP00000110431; ENSMUSG00000059447 ENSMUST00000114786; ENSMUSP00000110434; ENSMUSG00000059447 |
GeneIDi | 231086 |
KEGGi | mmu:231086 |
UCSCi | uc008wve.2, mouse |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AK033462 mRNA Translation: BAC28300.1 AK076814 mRNA Translation: BAC36493.1 AK083164 mRNA Translation: BAC38790.1 AK083767 mRNA Translation: BAC39015.1 AK150889 mRNA Translation: BAE29936.1 AK169637 mRNA Translation: BAE41269.1 BC005585 mRNA Translation: AAH05585.1 |
CCDSi | CCDS39045.1 |
RefSeqi | NP_001276727.1, NM_001289798.1 NP_001276728.1, NM_001289799.1 NP_663533.1, NM_145558.2 XP_017176317.1, XM_017320828.1 XP_017176318.1, XM_017320829.1 |
3D structure databases
SMRi | Q99JY0 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 231080, 27 interactors |
IntActi | Q99JY0, 8 interactors |
MINTi | Q99JY0 |
STRINGi | 10090.ENSMUSP00000110434 |
PTM databases
iPTMneti | Q99JY0 |
PhosphoSitePlusi | Q99JY0 |
SwissPalmi | Q99JY0 |
Proteomic databases
EPDi | Q99JY0 |
jPOSTi | Q99JY0 |
MaxQBi | Q99JY0 |
PaxDbi | Q99JY0 |
PeptideAtlasi | Q99JY0 |
PRIDEi | Q99JY0 |
Protocols and materials databases
Antibodypediai | 27848, 231 antibodies |
Genome annotation databases
Ensembli | ENSMUST00000026841; ENSMUSP00000026841; ENSMUSG00000059447 ENSMUST00000114783; ENSMUSP00000110431; ENSMUSG00000059447 ENSMUST00000114786; ENSMUSP00000110434; ENSMUSG00000059447 |
GeneIDi | 231086 |
KEGGi | mmu:231086 |
UCSCi | uc008wve.2, mouse |
Organism-specific databases
CTDi | 3032 |
MGIi | MGI:2136381, Hadhb |
Phylogenomic databases
eggNOGi | KOG1392, Eukaryota |
GeneTreei | ENSGT01010000222371 |
HOGENOMi | CLU_031026_2_0_1 |
InParanoidi | Q99JY0 |
OMAi | MTAFPEP |
OrthoDBi | 1129049at2759 |
PhylomeDBi | Q99JY0 |
TreeFami | TF315243 |
Enzyme and pathway databases
UniPathwayi | UPA00659 |
Reactomei | R-MMU-1482798, Acyl chain remodeling of CL R-MMU-77285, Beta oxidation of myristoyl-CoA to lauroyl-CoA R-MMU-77305, Beta oxidation of palmitoyl-CoA to myristoyl-CoA R-MMU-77310, Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA R-MMU-77346, Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA R-MMU-77348, Beta oxidation of octanoyl-CoA to hexanoyl-CoA R-MMU-77350, Beta oxidation of hexanoyl-CoA to butanoyl-CoA |
Miscellaneous databases
BioGRID-ORCSi | 231086, 0 hits in 17 CRISPR screens |
ChiTaRSi | Hadhb, mouse |
PROi | PR:Q99JY0 |
RNActi | Q99JY0, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000059447, Expressed in brown adipose tissue and 206 other tissues |
Genevisiblei | Q99JY0, MM |
Family and domain databases
CDDi | cd00751, thiolase, 1 hit |
Gene3Di | 3.40.47.10, 1 hit |
InterProi | View protein in InterPro IPR002155, Thiolase IPR016039, Thiolase-like IPR020615, Thiolase_acyl_enz_int_AS IPR020610, Thiolase_AS IPR020617, Thiolase_C IPR020613, Thiolase_CS IPR020616, Thiolase_N |
Pfami | View protein in Pfam PF02803, Thiolase_C, 1 hit PF00108, Thiolase_N, 1 hit |
SUPFAMi | SSF53901, SSF53901, 2 hits |
TIGRFAMsi | TIGR01930, AcCoA-C-Actrans, 1 hit |
PROSITEi | View protein in PROSITE PS00098, THIOLASE_1, 1 hit PS00737, THIOLASE_2, 1 hit PS00099, THIOLASE_3, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ECHB_MOUSE | |
Accessioni | Q99JY0Primary (citable) accession number: Q99JY0 Secondary accession number(s): Q3TEH9 Q8BK52 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 16, 2004 |
Last sequence update: | June 1, 2001 | |
Last modified: | December 2, 2020 | |
This is version 154 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families