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Protein

Trifunctional enzyme subunit alpha, mitochondrial

Gene

Hadha

Organism
Rattus norvegicus (Rat)
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

  • 3-hydroxyacyl-CoA dehydrogenase activity Source: RGD
  • acetyl-CoA C-acyltransferase activity Source: RGD
  • enoyl-CoA hydratase activity Source: RGD
  • fatty-acyl-CoA binding Source: RGD
  • long-chain-3-hydroxyacyl-CoA dehydrogenase activity Source: RGD
  • long-chain-enoyl-CoA hydratase activity Source: RGD
  • NAD binding Source: RGD
  • protein complex binding Source: RGD

GO - Biological processi

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

Keywords - Molecular functioni

Lyase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.1.1.211. 5301.
2.3.1.16. 5301.
ReactomeiR-RNO-1482798. Acyl chain remodeling of CL.
R-RNO-77285. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
R-RNO-77305. Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
R-RNO-77310. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
R-RNO-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-RNO-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
R-RNO-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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi620512. Hadha.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 36MitochondrionSequence analysisAdd BLAST36
ChainiPRO_000000740537 – 763Trifunctional enzyme subunit alpha, mitochondrialAdd BLAST727

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei46N6-acetyllysine; alternateBy similarity1
Modified residuei46N6-succinyllysine; alternateBy similarity1
Modified residuei60N6-acetyllysine; alternateBy similarity1
Modified residuei60N6-succinyllysine; alternateBy similarity1
Modified residuei129N6-acetyllysineBy similarity1
Modified residuei166N6-acetyllysine; alternateBy similarity1
Modified residuei166N6-succinyllysine; alternateBy similarity1
Modified residuei213N6-succinyllysineBy similarity1
Modified residuei214N6-acetyllysine; alternateBy similarity1
Modified residuei214N6-succinyllysine; alternateBy similarity1
Modified residuei230N6-succinyllysineBy similarity1
Modified residuei231PhosphoserineBy similarity1
Modified residuei249N6-acetyllysine; alternateBy similarity1
Modified residuei249N6-succinyllysine; alternateBy similarity1
Modified residuei289N6-acetyllysineBy similarity1
Modified residuei295N6-acetyllysineBy similarity1
Modified residuei303N6-acetyllysine; alternateBy similarity1
Modified residuei303N6-succinyllysine; alternateBy similarity1
Modified residuei326N6-acetyllysine; alternateBy similarity1
Modified residuei326N6-succinyllysine; alternateBy similarity1
Modified residuei334N6-acetyllysine; alternateBy similarity1
Modified residuei334N6-succinyllysine; alternateBy similarity1
Modified residuei350N6-acetyllysine; alternateBy similarity1
Modified residuei350N6-succinyllysine; alternateBy similarity1
Modified residuei353N6-acetyllysineBy similarity1
Modified residuei395PhosphothreonineBy similarity1
Modified residuei399Omega-N-methylarginineBy similarity1
Modified residuei406N6-acetyllysine; alternateBy similarity1
Modified residuei406N6-succinyllysine; alternateBy similarity1
Modified residuei411N6-acetyllysine; alternateBy similarity1
Modified residuei411N6-succinyllysine; alternateBy similarity1
Modified residuei415N6-succinyllysineBy similarity1
Modified residuei419PhosphoserineCombined sources1
Modified residuei436N6-acetyllysine; alternateBy similarity1
Modified residuei436N6-succinyllysine; alternateBy similarity1
Modified residuei440N6-succinyllysineBy similarity1
Modified residuei460N6-acetyllysine; alternateBy similarity1
Modified residuei460N6-succinyllysine; alternateBy similarity1
Modified residuei505N6-acetyllysine; alternateBy similarity1
Modified residuei505N6-succinyllysine; alternateBy similarity1
Modified residuei519N6-acetyllysine; alternateBy similarity1
Modified residuei519N6-succinyllysine; alternateBy similarity1
Modified residuei540N6-acetyllysineBy similarity1
Modified residuei569N6-acetyllysine; alternateBy similarity1
Modified residuei569N6-succinyllysine; alternateBy similarity1
Modified residuei620N6-succinyllysineBy similarity1
Modified residuei634N6-succinyllysineBy similarity1
Modified residuei644N6-acetyllysine; alternateBy similarity1
Modified residuei644N6-succinyllysine; alternateBy similarity1
Modified residuei646N6-succinyllysineBy similarity1
Modified residuei650PhosphoserineCombined sources1
Modified residuei664N6-acetyllysine; alternateBy similarity1
Modified residuei664N6-succinyllysine; alternateBy similarity1
Modified residuei728N6-acetyllysine; alternateBy similarity1
Modified residuei728N6-succinyllysine; alternateBy similarity1
Modified residuei735N6-acetyllysineBy similarity1
Modified residuei759N6-acetyllysine; alternateBy similarity1
Modified residuei759N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ64428.
PRIDEiQ64428.

PTM databases

iPTMnetiQ64428.
PhosphoSitePlusiQ64428.
SwissPalmiQ64428.

Expressioni

Gene expression databases

BgeeiENSRNOG00000024629.
GenevisibleiQ64428. RN.

Interactioni

Subunit structurei

Octamer of 4 alpha (HADHA) and 4 beta (HADHB) subunits.1 Publication

GO - Molecular functioni

  • protein complex binding Source: RGD

Protein-protein interaction databases

BioGridi250974. 2 interactors.
IntActiQ64428. 2 interactors.
MINTiMINT-4599643.
STRINGi10116.ENSRNOP00000038073.

Structurei

3D structure databases

ProteinModelPortaliQ64428.
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.
HOGENOMiHOG000027939.
HOVERGENiHBG005557.
InParanoidiQ64428.
KOiK07515.
OMAiMMMLNEA.
OrthoDBiEOG091G02LF.
PhylomeDBiQ64428.

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.

Q64428-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVASRAIGSL SRFSAFRILR SRGCICHSFT TSSALLSRTH INYGVKGDVA
60 70 80 90 100
VIRINSPNSK VNTLNKEVQS EFVEVMNEIW ANDQIRSAVL ISSKPGCFVA
110 120 130 140 150
GADINMLASC TTPQEAARIS QEGQKMFEKL EKSPKPVVAA ISGSCLGGGL
160 170 180 190 200
ELAIACQYRI ATKDRKTVLG VPEVLLGILP GAGGTQRLPK MVGVPAAFDM
210 220 230 240 250
MLTGRNIRAD RAKKMGLVDQ LVDPLGPGIK SPEERTIEYL EEVAVNFAKG
260 270 280 290 300
LADRKVSAKQ SKGLMEKLTS YAMTIPFVRQ QVYKTVEEKV KKQTKGLYPA
310 320 330 340 350
PLKIIDAVKT GLEQGNDAGY LAESEKFGEL ALTKESKALM GLYNGQVLCK
360 370 380 390 400
KNKFGAPQKT VQQLAILGAG LMGAGIAQVS VDKGLKTLLK DTTVTGLGRG
410 420 430 440 450
QQQVFKGLND KVKKKALTSF ERDSIFSNLI GQLDYKGFEK ADMVIEAVFE
460 470 480 490 500
DLAVKHKVLK EVESVTPEHC IFASNTSALP INQIAAVSQR PEKVIGMHYF
510 520 530 540 550
SPVDKMQLLE IITTDKTSKD TTASAVAVGL KQGKVIIVVK DGPGFYTTRC
560 570 580 590 600
LAPMMSEVIR ILQEGVDPKK LDALTTGFGF PVGAATLADE VGIDVAQHVA
610 620 630 640 650
EDLGKAFGER FGGGSVELLK LMVSKGFLGR KSGKGFYIYQ SGSKNKNLNS
660 670 680 690 700
EIDNILVNLR LPAKPEVSSD EDIQYRVITR FVNEAVLCLQ EGILATPEEG
710 720 730 740 750
DIGAVFGLGF PPCLGGPFRF VDLYGAQKVV DRLRKYESAY GTQFTPCQLL
760
RDLANNSSKK FYQ
Length:763
Mass (Da):82,665
Last modified:March 18, 2008 - v2
Checksum:iA16648B82AE7D62E
GO

Sequence cautioni

The sequence BAA03939 differs from that shown. Reason: Frameshift at positions 27, 33, 277 and 283.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16478 mRNA. Translation: BAA03939.1. Frameshift.
BC091697 mRNA. Translation: AAH91697.1.
PIRiA49681.
RefSeqiNP_570839.2. NM_130826.2.
UniGeneiRn.3340.
Rn.34751.

Genome annotation databases

EnsembliENSRNOT00000038649; ENSRNOP00000038073; ENSRNOG00000024629.
GeneIDi170670.
KEGGirno:170670.
UCSCiRGD:620512. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16478 mRNA. Translation: BAA03939.1. Frameshift.
BC091697 mRNA. Translation: AAH91697.1.
PIRiA49681.
RefSeqiNP_570839.2. NM_130826.2.
UniGeneiRn.3340.
Rn.34751.

3D structure databases

ProteinModelPortaliQ64428.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250974. 2 interactors.
IntActiQ64428. 2 interactors.
MINTiMINT-4599643.
STRINGi10116.ENSRNOP00000038073.

PTM databases

iPTMnetiQ64428.
PhosphoSitePlusiQ64428.
SwissPalmiQ64428.

Proteomic databases

PaxDbiQ64428.
PRIDEiQ64428.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000038649; ENSRNOP00000038073; ENSRNOG00000024629.
GeneIDi170670.
KEGGirno:170670.
UCSCiRGD:620512. rat.

Organism-specific databases

CTDi3030.
RGDi620512. Hadha.

Phylogenomic databases

eggNOGiKOG1683. Eukaryota.
COG1024. LUCA.
COG1250. LUCA.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000027939.
HOVERGENiHBG005557.
InParanoidiQ64428.
KOiK07515.
OMAiMMMLNEA.
OrthoDBiEOG091G02LF.
PhylomeDBiQ64428.

Enzyme and pathway databases

UniPathwayiUPA00659.
BRENDAi1.1.1.211. 5301.
2.3.1.16. 5301.
ReactomeiR-RNO-1482798. Acyl chain remodeling of CL.
R-RNO-77285. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
R-RNO-77305. Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
R-RNO-77310. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
R-RNO-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-RNO-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
R-RNO-77350. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.

Miscellaneous databases

PROiQ64428.

Gene expression databases

BgeeiENSRNOG00000024629.
GenevisibleiQ64428. RN.

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_RAT
AccessioniPrimary (citable) accession number: Q64428
Secondary accession number(s): Q5BIZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 18, 2008
Last modified: November 30, 2016
This is version 140 of the entry and version 2 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.