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Protein

Trifunctional enzyme subunit alpha, mitochondrial

Gene

Hadha

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Bifunctional subunit.

Catalytic activityi

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.
A long-chain (S)-3-hydroxyacyl-CoA + NAD+ = a long-chain 3-oxoacyl-CoA + NADH.

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
Sitei151 – 1511Important for catalytic activityBy similarity
Sitei173 – 1731Important for catalytic activityBy similarity

GO - Molecular functioni

GO - Biological processi

  • fatty acid beta-oxidation Source: MGI
  • response to drug Source: Ensembl
  • response to insulin Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiR-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.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Trifunctional enzyme subunit alpha, mitochondrial
Alternative name(s):
TP-alpha
Including the following 2 domains:
Long-chain enoyl-CoA hydratase (EC:4.2.1.17)
Long chain 3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.211)
Gene namesi
Name:Hadha
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:2135593. Hadha.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial fatty acid beta-oxidation multienzyme complex Source: Ensembl
  • mitochondrial inner membrane Source: MGI
  • mitochondrial nucleoid Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3636MitochondrionSequence analysisAdd
BLAST
Chaini37 – 763727Trifunctional enzyme subunit alpha, mitochondrialPRO_0000322639Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461N6-acetyllysine; alternateCombined sources
Modified residuei46 – 461N6-succinyllysine; alternateCombined sources
Modified residuei60 – 601N6-acetyllysine; alternateCombined sources
Modified residuei60 – 601N6-succinyllysine; alternateCombined sources
Modified residuei129 – 1291N6-acetyllysineCombined sources
Modified residuei166 – 1661N6-acetyllysine; alternateCombined sources
Modified residuei166 – 1661N6-succinyllysine; alternateCombined sources
Modified residuei213 – 2131N6-succinyllysineCombined sources
Modified residuei214 – 2141N6-acetyllysine; alternateCombined sources
Modified residuei214 – 2141N6-succinyllysine; alternateCombined sources
Modified residuei230 – 2301N6-succinyllysineCombined sources
Modified residuei231 – 2311PhosphoserineCombined sources
Modified residuei249 – 2491N6-acetyllysine; alternateCombined sources
Modified residuei249 – 2491N6-succinyllysine; alternateCombined sources
Modified residuei289 – 2891N6-acetyllysineCombined sources
Modified residuei295 – 2951N6-acetyllysineBy similarity
Modified residuei303 – 3031N6-acetyllysine; alternateCombined sources
Modified residuei303 – 3031N6-succinyllysine; alternateCombined sources
Modified residuei316 – 3161PhosphoserineCombined sources
Modified residuei326 – 3261N6-acetyllysine; alternateCombined sources
Modified residuei326 – 3261N6-succinyllysine; alternateCombined sources
Modified residuei334 – 3341N6-acetyllysine; alternateCombined sources
Modified residuei334 – 3341N6-succinyllysine; alternateCombined sources
Modified residuei350 – 3501N6-acetyllysine; alternateCombined sources
Modified residuei350 – 3501N6-succinyllysine; alternateCombined sources
Modified residuei353 – 3531N6-acetyllysineCombined sources
Modified residuei395 – 3951PhosphothreonineCombined sources
Modified residuei406 – 4061N6-acetyllysine; alternateCombined sources
Modified residuei406 – 4061N6-succinyllysine; alternateCombined sources
Modified residuei411 – 4111N6-acetyllysine; alternateCombined sources
Modified residuei411 – 4111N6-succinyllysine; alternateCombined sources
Modified residuei415 – 4151N6-succinyllysineCombined sources
Modified residuei419 – 4191PhosphoserineBy similarity
Modified residuei436 – 4361N6-acetyllysine; alternateCombined sources
Modified residuei436 – 4361N6-succinyllysine; alternateCombined sources
Modified residuei440 – 4401N6-succinyllysineCombined sources
Modified residuei460 – 4601N6-acetyllysine; alternateCombined sources
Modified residuei460 – 4601N6-succinyllysine; alternateCombined sources
Modified residuei505 – 5051N6-acetyllysine; alternateCombined sources
Modified residuei505 – 5051N6-succinyllysine; alternateCombined sources
Modified residuei519 – 5191N6-acetyllysine; alternateCombined sources
Modified residuei519 – 5191N6-succinyllysine; alternateCombined sources
Modified residuei540 – 5401N6-acetyllysineCombined sources
Modified residuei569 – 5691N6-acetyllysine; alternateCombined sources
Modified residuei569 – 5691N6-succinyllysine; alternateCombined sources
Modified residuei620 – 6201N6-succinyllysineCombined sources
Modified residuei634 – 6341N6-succinyllysineCombined sources
Modified residuei644 – 6441N6-acetyllysine; alternateCombined sources
Modified residuei644 – 6441N6-succinyllysine; alternateCombined sources
Modified residuei646 – 6461N6-succinyllysineCombined sources
Modified residuei647 – 6471PhosphoserineCombined sources
Modified residuei650 – 6501PhosphoserineBy similarity
Modified residuei664 – 6641N6-acetyllysine; alternateCombined sources
Modified residuei664 – 6641N6-succinyllysine; alternateCombined sources
Modified residuei728 – 7281N6-acetyllysine; alternateCombined sources
Modified residuei728 – 7281N6-succinyllysine; alternateCombined sources
Modified residuei735 – 7351N6-acetyllysineCombined sources
Modified residuei759 – 7591N6-acetyllysine; alternateCombined sources
Modified residuei759 – 7591N6-succinyllysine; alternateCombined sources

Post-translational modificationi

Acetylation of Lys-569 and Lys-728 is observed in liver mitochondria from fasted mice but not from fed mice.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8BMS1.
MaxQBiQ8BMS1.
PaxDbiQ8BMS1.
PeptideAtlasiQ8BMS1.
PRIDEiQ8BMS1.

2D gel databases

REPRODUCTION-2DPAGEIPI00223092.

PTM databases

iPTMnetiQ8BMS1.
PhosphoSiteiQ8BMS1.
SwissPalmiQ8BMS1.

Expressioni

Gene expression databases

BgeeiENSMUSG00000025745.
ExpressionAtlasiQ8BMS1. baseline and differential.
GenevisibleiQ8BMS1. MM.

Interactioni

Subunit structurei

Octamer of 4 alpha (HADHA) and 4 beta (HADHB) subunits.By similarity

Protein-protein interaction databases

BioGridi220648. 5 interactions.
IntActiQ8BMS1. 8 interactions.
MINTiMINT-1860051.
STRINGi10090.ENSMUSP00000120976.

Structurei

3D structure databases

ProteinModelPortaliQ8BMS1.
SMRiQ8BMS1. Positions 44-763.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.Curated
In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1683. Eukaryota.
COG1024. LUCA.
COG1250. LUCA.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000261346.
HOVERGENiHBG005557.
InParanoidiQ8BMS1.
KOiK07515.
OMAiMMMLNEA.
OrthoDBiEOG091G02LF.
PhylomeDBiQ8BMS1.
TreeFamiTF352288.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR012803. Fa_ox_alpha_mit.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
SSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02441. fa_ox_alpha_mit. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8BMS1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVASRAIGSL SRFSAFRILR SRGCICRSFT TSSALLTRTH INYGVKGDVA
60 70 80 90 100
VIRINSPNSK VNTLNKEVQS EFIEVMNEIW ANDQIRSAVL ISSKPGCFVA
110 120 130 140 150
GADINMLSSC TTPQEATRIS QEGQRMFEKL EKSPKPVVAA ISGSCLGGGL
160 170 180 190 200
ELAIACQYRI ATKDRKTVLG VPEVLLGILP GAGGTQRLPK MVGVPAAFDM
210 220 230 240 250
MLTGRNIRAD RAKKMGLVDQ LVEPLGPGIK SPEERTIEYL EEVAVNFAKG
260 270 280 290 300
LADRKVSAKQ SKGLVEKLTT YAMTVPFVRQ QVYKTVEEKV KKQTKGLYPA
310 320 330 340 350
PLKIIDAVKA GLEQGSDAGY LAESQKFGEL ALTKESKALM GLYNGQVLCK
360 370 380 390 400
KNKFGAPQKN VQQLAILGAG LMGAGIAQVS VDKGLKTLLK DTTVTGLGRG
410 420 430 440 450
QQQVFKGLND KVKKKALTSF ERDSIFSNLI GQLDYKGFEK ADMVIEAVFE
460 470 480 490 500
DLGVKHKVLK EVESVTPEHC IFASNTSALP INQIAAVSKR PEKVIGMHYF
510 520 530 540 550
SPVDKMQLLE IITTDKTSKD TTASAVAVGL RQGKVIIVVK DGPGFYTTRC
560 570 580 590 600
LAPMMSEVMR ILQEGVDPKK LDALTTGFGF PVGAATLADE VGVDVAQHVA
610 620 630 640 650
EDLGKAFGER FGGGSVELLK QMVSKGFLGR KSGKGFYIYQ EGSKNKSLNS
660 670 680 690 700
EMDNILANLR LPAKPEVSSD EDVQYRVITR FVNEAVLCLQ EGILATPAEG
710 720 730 740 750
DIGAVFGLGF PPCLGGPFRF VDLYGAQKVV DRLRKYESAY GTQFTPCQLL
760
LDHANNSSKK FYQ
Length:763
Mass (Da):82,670
Last modified:March 1, 2003 - v1
Checksum:i73D203795D5C1141
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti196 – 1961A → D in BAE41822 (PubMed:16141072).Curated
Sequence conflicti459 – 4591L → S in AAH37009 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029017 mRNA. Translation: BAC26245.1.
AK170478 mRNA. Translation: BAE41822.1.
AK170683 mRNA. Translation: BAE41956.1.
BC027156 mRNA. Translation: AAH27156.1.
BC037009 mRNA. Translation: AAH37009.1.
BC046978 mRNA. Translation: AAH46978.1.
BC058569 mRNA. Translation: AAH58569.1.
CCDSiCCDS19155.1.
RefSeqiNP_849209.1. NM_178878.2.
UniGeneiMm.200497.

Genome annotation databases

EnsembliENSMUST00000156859; ENSMUSP00000120976; ENSMUSG00000025745.
GeneIDi97212.
KEGGimmu:97212.
UCSCiuc008wvc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029017 mRNA. Translation: BAC26245.1.
AK170478 mRNA. Translation: BAE41822.1.
AK170683 mRNA. Translation: BAE41956.1.
BC027156 mRNA. Translation: AAH27156.1.
BC037009 mRNA. Translation: AAH37009.1.
BC046978 mRNA. Translation: AAH46978.1.
BC058569 mRNA. Translation: AAH58569.1.
CCDSiCCDS19155.1.
RefSeqiNP_849209.1. NM_178878.2.
UniGeneiMm.200497.

3D structure databases

ProteinModelPortaliQ8BMS1.
SMRiQ8BMS1. Positions 44-763.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi220648. 5 interactions.
IntActiQ8BMS1. 8 interactions.
MINTiMINT-1860051.
STRINGi10090.ENSMUSP00000120976.

PTM databases

iPTMnetiQ8BMS1.
PhosphoSiteiQ8BMS1.
SwissPalmiQ8BMS1.

2D gel databases

REPRODUCTION-2DPAGEIPI00223092.

Proteomic databases

EPDiQ8BMS1.
MaxQBiQ8BMS1.
PaxDbiQ8BMS1.
PeptideAtlasiQ8BMS1.
PRIDEiQ8BMS1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000156859; ENSMUSP00000120976; ENSMUSG00000025745.
GeneIDi97212.
KEGGimmu:97212.
UCSCiuc008wvc.1. mouse.

Organism-specific databases

CTDi3030.
MGIiMGI:2135593. Hadha.

Phylogenomic databases

eggNOGiKOG1683. Eukaryota.
COG1024. LUCA.
COG1250. LUCA.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000261346.
HOVERGENiHBG005557.
InParanoidiQ8BMS1.
KOiK07515.
OMAiMMMLNEA.
OrthoDBiEOG091G02LF.
PhylomeDBiQ8BMS1.
TreeFamiTF352288.

Enzyme and pathway databases

UniPathwayiUPA00659.
ReactomeiR-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

ChiTaRSiHadha. mouse.
PROiQ8BMS1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000025745.
ExpressionAtlasiQ8BMS1. baseline and differential.
GenevisibleiQ8BMS1. MM.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR012803. Fa_ox_alpha_mit.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
SSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02441. fa_ox_alpha_mit. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiECHA_MOUSE
AccessioniPrimary (citable) accession number: Q8BMS1
Secondary accession number(s): Q3TCY3, Q5U5Y5, Q8QZU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 1, 2003
Last modified: September 7, 2016
This is version 141 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, Multifunctional enzyme, 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

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.