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Protein

Trifunctional enzyme subunit beta, mitochondrial

Gene

Hadhb

Organism
Mus musculus (Mouse)
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. acetyl-CoA C-acyltransferase activity Source: MGI
  2. enoyl-CoA hydratase activity Source: Ensembl
  3. fatty-acyl-CoA binding Source: Ensembl
  4. long-chain-3-hydroxyacyl-CoA dehydrogenase activity Source: MGI
  5. long-chain-enoyl-CoA hydratase activity Source: Ensembl
  6. NAD binding Source: Ensembl
  7. poly(A) RNA binding Source: MGI

GO - Biological processi

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

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

ReactomeiREACT_199034. Acyl chain remodeling of CL.
REACT_236353. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
REACT_237597. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
REACT_239107. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
REACT_251878. Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
REACT_256910. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
REACT_261839. Beta oxidation of decanoyl-CoA to octanoyl-CoA-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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:2136381. 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: MGI
  3. mitochondrial fatty acid beta-oxidation multienzyme complex Source: MGI
  4. mitochondrial inner membrane Source: MGI
  5. mitochondrial nucleoid Source: MGI
  6. mitochondrial outer membrane Source: UniProtKB
  7. mitochondrion Source: MGI
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_0000034082Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531N6-succinyllysine1 Publication
Modified residuei73 – 731N6-acetyllysine; alternate1 Publication
Modified residuei73 – 731N6-succinyllysine; alternate1 Publication
Modified residuei189 – 1891N6-acetyllysine; alternate1 Publication
Modified residuei189 – 1891N6-succinyllysine; alternate1 Publication
Modified residuei191 – 1911N6-succinyllysine1 Publication
Modified residuei273 – 2731N6-succinyllysine1 Publication
Modified residuei292 – 2921N6-succinyllysine1 Publication
Modified residuei294 – 2941N6-acetyllysine; alternate1 Publication
Modified residuei294 – 2941N6-succinyllysine; alternate1 Publication
Modified residuei299 – 2991N6-acetyllysine1 Publication
Modified residuei333 – 3331N6-acetyllysine; alternate1 Publication
Modified residuei333 – 3331N6-succinyllysine; alternate1 Publication
Modified residuei349 – 3491N6-acetyllysine1 Publication
Modified residuei362 – 3621N6-acetyllysine1 Publication

Post-translational modificationi

Acetylation of Lys-202 is observed in liver mitochondria from fasted mice but not from fed mice.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ99JY0.
PaxDbiQ99JY0.
PRIDEiQ99JY0.

PTM databases

PhosphoSiteiQ99JY0.

Expressioni

Gene expression databases

BgeeiQ99JY0.
ExpressionAtlasiQ99JY0. baseline and differential.
GenevestigatoriQ99JY0.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi231080. 1 interaction.
IntActiQ99JY0. 6 interactions.
MINTiMINT-1839643.
STRINGi10090.ENSMUSP00000110434.

Structurei

3D structure databases

ProteinModelPortaliQ99JY0.
SMRiQ99JY0. Positions 57-472.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0183.
GeneTreeiENSGT00760000119318.
HOGENOMiHOG000012240.
HOVERGENiHBG104782.
InParanoidiQ99JY0.
KOiK07509.
OMAiIDVWEDM.
OrthoDBiEOG7DRJ2Z.
PhylomeDBiQ99JY0.
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.

Q99JY0-1 [UniParc]FASTAAdd to Basket

« Hide

        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
Length:475
Mass (Da):51,386
Last modified:June 1, 2001 - v1
Checksum:iF131B497C4F5FAF4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 252IR → HK in BAC36493. (PubMed:16141072)Curated
Sequence conflicti425 – 4251L → M in BAC38790. (PubMed:16141072)Curated
Sequence conflicti450 – 4501G → R in BAC38790. (PubMed:16141072)Curated
Sequence conflicti450 – 4501G → V in BAC39015. (PubMed:16141072)Curated

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.
CCDSiCCDS39045.1.
RefSeqiNP_001276727.1. NM_001289798.1.
NP_001276728.1. NM_001289799.1.
NP_663533.1. NM_145558.2.
UniGeneiMm.291463.
Mm.389348.

Genome annotation databases

EnsembliENSMUST00000026841; ENSMUSP00000026841; ENSMUSG00000059447.
ENSMUST00000114783; ENSMUSP00000110431; ENSMUSG00000059447.
ENSMUST00000114786; ENSMUSP00000110434; ENSMUSG00000059447.
GeneIDi231086.
KEGGimmu:231086.
UCSCiuc008wve.1. mouse.

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.
CCDSiCCDS39045.1.
RefSeqiNP_001276727.1. NM_001289798.1.
NP_001276728.1. NM_001289799.1.
NP_663533.1. NM_145558.2.
UniGeneiMm.291463.
Mm.389348.

3D structure databases

ProteinModelPortaliQ99JY0.
SMRiQ99JY0. Positions 57-472.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231080. 1 interaction.
IntActiQ99JY0. 6 interactions.
MINTiMINT-1839643.
STRINGi10090.ENSMUSP00000110434.

PTM databases

PhosphoSiteiQ99JY0.

Proteomic databases

MaxQBiQ99JY0.
PaxDbiQ99JY0.
PRIDEiQ99JY0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026841; ENSMUSP00000026841; ENSMUSG00000059447.
ENSMUST00000114783; ENSMUSP00000110431; ENSMUSG00000059447.
ENSMUST00000114786; ENSMUSP00000110434; ENSMUSG00000059447.
GeneIDi231086.
KEGGimmu:231086.
UCSCiuc008wve.1. mouse.

Organism-specific databases

CTDi3032.
MGIiMGI:2136381. Hadhb.

Phylogenomic databases

eggNOGiCOG0183.
GeneTreeiENSGT00760000119318.
HOGENOMiHOG000012240.
HOVERGENiHBG104782.
InParanoidiQ99JY0.
KOiK07509.
OMAiIDVWEDM.
OrthoDBiEOG7DRJ2Z.
PhylomeDBiQ99JY0.
TreeFamiTF315243.

Enzyme and pathway databases

UniPathwayiUPA00659.
ReactomeiREACT_199034. Acyl chain remodeling of CL.
REACT_236353. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
REACT_237597. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
REACT_239107. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
REACT_251878. Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
REACT_256910. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
REACT_261839. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.

Miscellaneous databases

ChiTaRSiHadhb. mouse.
NextBioi380391.
PROiQ99JY0.
SOURCEiSearch...

Gene expression databases

BgeeiQ99JY0.
ExpressionAtlasiQ99JY0. baseline and differential.
GenevestigatoriQ99JY0.

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

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow, Colon, Hippocampus, Spinal ganglion, Testis and Thymus.
  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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-53; LYS-73; LYS-189; LYS-191; LYS-273; LYS-292; LYS-294 AND LYS-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  4. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-189; LYS-294; LYS-299; LYS-333; LYS-349 AND LYS-362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiECHB_MOUSE
AccessioniPrimary (citable) accession number: Q99JY0
Secondary accession number(s): Q3TEH9
, Q8BJI5, Q8BJM0, Q8BK52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 1, 2001
Last modified: February 4, 2015
This is version 114 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.