Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Sitei151Important for catalytic activityBy similarity1
Sitei173Important for catalytic activityBy similarity1

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

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 36MitochondrionSequence analysisAdd BLAST36
ChainiPRO_000032263937 – 763Trifunctional enzyme subunit alpha, mitochondrialAdd BLAST727

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei46N6-acetyllysine; alternateCombined sources1
Modified residuei46N6-succinyllysine; alternateCombined sources1
Modified residuei60N6-acetyllysine; alternateCombined sources1
Modified residuei60N6-succinyllysine; alternateCombined sources1
Modified residuei129N6-acetyllysineCombined sources1
Modified residuei166N6-acetyllysine; alternateCombined sources1
Modified residuei166N6-succinyllysine; alternateCombined sources1
Modified residuei213N6-succinyllysineCombined sources1
Modified residuei214N6-acetyllysine; alternateCombined sources1
Modified residuei214N6-succinyllysine; alternateCombined sources1
Modified residuei230N6-succinyllysineCombined sources1
Modified residuei231PhosphoserineCombined sources1
Modified residuei249N6-acetyllysine; alternateCombined sources1
Modified residuei249N6-succinyllysine; alternateCombined sources1
Modified residuei289N6-acetyllysineCombined sources1
Modified residuei295N6-acetyllysineBy similarity1
Modified residuei303N6-acetyllysine; alternateCombined sources1
Modified residuei303N6-succinyllysine; alternateCombined sources1
Modified residuei316PhosphoserineCombined sources1
Modified residuei326N6-acetyllysine; alternateCombined sources1
Modified residuei326N6-succinyllysine; alternateCombined sources1
Modified residuei334N6-acetyllysine; alternateCombined sources1
Modified residuei334N6-succinyllysine; alternateCombined sources1
Modified residuei350N6-acetyllysine; alternateCombined sources1
Modified residuei350N6-succinyllysine; alternateCombined sources1
Modified residuei353N6-acetyllysineCombined sources1
Modified residuei395PhosphothreonineCombined sources1
Modified residuei399Omega-N-methylarginineCombined sources1
Modified residuei406N6-acetyllysine; alternateCombined sources1
Modified residuei406N6-succinyllysine; alternateCombined sources1
Modified residuei411N6-acetyllysine; alternateCombined sources1
Modified residuei411N6-succinyllysine; alternateCombined sources1
Modified residuei415N6-succinyllysineCombined sources1
Modified residuei419PhosphoserineBy similarity1
Modified residuei436N6-acetyllysine; alternateCombined sources1
Modified residuei436N6-succinyllysine; alternateCombined sources1
Modified residuei440N6-succinyllysineCombined sources1
Modified residuei460N6-acetyllysine; alternateCombined sources1
Modified residuei460N6-succinyllysine; alternateCombined sources1
Modified residuei505N6-acetyllysine; alternateCombined sources1
Modified residuei505N6-succinyllysine; alternateCombined sources1
Modified residuei519N6-acetyllysine; alternateCombined sources1
Modified residuei519N6-succinyllysine; alternateCombined sources1
Modified residuei540N6-acetyllysineCombined sources1
Modified residuei569N6-acetyllysine; alternateCombined sources1
Modified residuei569N6-succinyllysine; alternateCombined sources1
Modified residuei620N6-succinyllysineCombined sources1
Modified residuei634N6-succinyllysineCombined sources1
Modified residuei644N6-acetyllysine; alternateCombined sources1
Modified residuei644N6-succinyllysine; alternateCombined sources1
Modified residuei646N6-succinyllysineCombined sources1
Modified residuei647PhosphoserineCombined sources1
Modified residuei650PhosphoserineBy similarity1
Modified residuei664N6-acetyllysine; alternateCombined sources1
Modified residuei664N6-succinyllysine; alternateCombined sources1
Modified residuei728N6-acetyllysine; alternateCombined sources1
Modified residuei728N6-succinyllysine; alternateCombined sources1
Modified residuei735N6-acetyllysineCombined sources1
Modified residuei759N6-acetyllysine; alternateCombined sources1
Modified residuei759N6-succinyllysine; alternateCombined sources1

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, Methylation, Phosphoprotein

Proteomic databases

EPDiQ8BMS1.
MaxQBiQ8BMS1.
PaxDbiQ8BMS1.
PeptideAtlasiQ8BMS1.
PRIDEiQ8BMS1.

2D gel databases

REPRODUCTION-2DPAGEIPI00223092.

PTM databases

iPTMnetiQ8BMS1.
PhosphoSitePlusiQ8BMS1.
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. 6 interactors.
IntActiQ8BMS1. 8 interactors.
MINTiMINT-1860051.
STRINGi10090.ENSMUSP00000120976.

Structurei

3D structure databases

ProteinModelPortaliQ8BMS1.
SMRiQ8BMS1.
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. 2 hits.
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)DescriptionActionsGraphical viewLength
Sequence conflicti196A → D in BAE41822 (PubMed:16141072).Curated1
Sequence conflicti459L → S in AAH37009 (PubMed:15489334).Curated1

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi220648. 6 interactors.
IntActiQ8BMS1. 8 interactors.
MINTiMINT-1860051.
STRINGi10090.ENSMUSP00000120976.

PTM databases

iPTMnetiQ8BMS1.
PhosphoSitePlusiQ8BMS1.
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. 2 hits.
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: November 2, 2016
This is version 143 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.