Trifunctional enzyme subunit alpha, mitochondrial precursor

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Q64428 (ECHA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:

Hadha

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	763 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Bifunctional subunit.
Catalytic activity	(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H₂O. (S)-3-hydroxyacyl-CoA + NAD⁺ = 3-oxoacyl-CoA + NADH.
Pathway	Lipid metabolism; fatty acid beta-oxidation.
Subunit structure	Octamer of 4 alpha (HADHA) and 4 beta (HADHB) subunits. Ref.3
Subcellular location	Mitochondrion matrix.
Sequence similarities	In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
Sequence caution	The sequence BAA03939.1 differs from that shown. Reason: Frameshift at positions 27, 33, 277 and 283.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NAD
Molecular function	Lyase Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Inferred from direct assay Ref.3. Source: RGD response to drug Inferred from direct assay. Source: RGD
Cellular component	fatty acid beta-oxidation multienzyme complex Inferred from direct assay Ref.3. Source: RGD
Molecular function	3-hydroxyacyl-CoA dehydrogenase activity Inferred from direct assay Ref.3. Source: RGD NAD binding Inferred from direct assay Ref.3. Source: RGD acetyl-CoA C-acyltransferase activity Inferred from direct assay Ref.3. Source: RGD enoyl-CoA hydratase activity Inferred from direct assay Ref.3. Source: RGD fatty-acyl-CoA binding Inferred from direct assay Ref.3. Source: RGD long-chain-3-hydroxyacyl-CoA dehydrogenase activity Inferred from direct assay Ref.3. Source: RGD long-chain-enoyl-CoA hydratase activity Inferred from direct assay Ref.3. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 36

Mitochondrion Potential

Chain

37 – 763

727

Trifunctional enzyme subunit alpha, mitochondrial

PRO_0000007405

Sites

Site

151

Important for catalytic activity By similarity

Site

173

Important for catalytic activity By similarity

Amino acid modifications

Modified residue

129

N6-acetyllysine By similarity

Modified residue

295

N6-acetyllysine By similarity

Modified residue

303

N6-acetyllysine By similarity

Modified residue

326

N6-acetyllysine By similarity

Modified residue

350

N6-acetyllysine By similarity

Modified residue

353

N6-acetyllysine By similarity

Modified residue

359

N6-acetyllysine By similarity

Modified residue

406

N6-acetyllysine By similarity

Modified residue

505

N6-acetyllysine By similarity

Modified residue

540

N6-acetyllysine By similarity

Modified residue

569

N6-acetyllysine By similarity

Modified residue

644

N6-acetyllysine By similarity

Modified residue

728

N6-acetyllysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q64428 [UniParc].

Last modified March 18, 2008. Version 2.
Checksum: A16648B82AE7D62E
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FASTA

763

82,665

        10         20         30         40         50         60 
MVASRAIGSL SRFSAFRILR SRGCICHSFT TSSALLSRTH INYGVKGDVA VIRINSPNSK 

        70         80         90        100        110        120 
VNTLNKEVQS EFVEVMNEIW ANDQIRSAVL ISSKPGCFVA GADINMLASC TTPQEAARIS 

       130        140        150        160        170        180 
QEGQKMFEKL EKSPKPVVAA ISGSCLGGGL ELAIACQYRI ATKDRKTVLG VPEVLLGILP 

       190        200        210        220        230        240 
GAGGTQRLPK MVGVPAAFDM MLTGRNIRAD RAKKMGLVDQ LVDPLGPGIK SPEERTIEYL 

       250        260        270        280        290        300 
EEVAVNFAKG LADRKVSAKQ SKGLMEKLTS YAMTIPFVRQ QVYKTVEEKV KKQTKGLYPA 

       310        320        330        340        350        360 
PLKIIDAVKT GLEQGNDAGY LAESEKFGEL ALTKESKALM GLYNGQVLCK KNKFGAPQKT 

       370        380        390        400        410        420 
VQQLAILGAG LMGAGIAQVS VDKGLKTLLK DTTVTGLGRG QQQVFKGLND KVKKKALTSF 

       430        440        450        460        470        480 
ERDSIFSNLI GQLDYKGFEK ADMVIEAVFE DLAVKHKVLK EVESVTPEHC IFASNTSALP 

       490        500        510        520        530        540 
INQIAAVSQR PEKVIGMHYF SPVDKMQLLE IITTDKTSKD TTASAVAVGL KQGKVIIVVK 

       550        560        570        580        590        600 
DGPGFYTTRC LAPMMSEVIR ILQEGVDPKK LDALTTGFGF PVGAATLADE VGIDVAQHVA 

       610        620        630        640        650        660 
EDLGKAFGER FGGGSVELLK LMVSKGFLGR KSGKGFYIYQ SGSKNKNLNS EIDNILVNLR 

       670        680        690        700        710        720 
LPAKPEVSSD EDIQYRVITR FVNEAVLCLQ EGILATPEEG DIGAVFGLGF PPCLGGPFRF 

       730        740        750        760 
VDLYGAQKVV DRLRKYESAY GTQFTPCQLL RDLANNSSKK FYQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of the cDNAs for the subunits of rat mitochondrial fatty acid beta-oxidation multienzyme complex. Structural and functional relationships to other mitochondrial and peroxisomal beta-oxidation enzymes." Kamijo T., Aoyama T., Miyazaki J., Hashimoto T. J. Biol. Chem. 268:26452-26460(1993) [PubMed: 8253773] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Wistar.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary.
[3]	"Novel fatty acid beta-oxidation enzymes in rat liver mitochondria. II. Purification and properties of enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein." Uchida Y., Izai K., Orii T., Hashimoto T. J. Biol. Chem. 267:1034-1041(1992) [PubMed: 1730633] [Abstract] Cited for: SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D16478 mRNA. Translation: BAA03939.1. Frameshift. BC091697 mRNA. Translation: AAH91697.1.
IPI	IPI00212622.
PIR	A49681.
RefSeq	NP_570839.2. NM_130826.2.
UniGene	Rn.3340. Rn.34751.
3D structure databases
ProteinModelPortal	Q64428.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q64428. 1 interaction.
MINT	MINT-4599643.
STRING	Q64428.
PTM databases
PhosphoSite	Q64428.
Proteomic databases
PRIDE	Q64428.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	170670.
KEGG	rno:170670.
Organism-specific databases
CTD	3030.
RGD	620512. Hadha.
Phylogenomic databases
eggNOG	maNOG12377.
HOVERGEN	HBG005557.
InParanoid	Q64428.
OrthoDB	EOG4FBHSD.
Enzyme and pathway databases
BRENDA	1.1.1.211. 5301.
Gene expression databases
ArrayExpress	Q64428.
Genevestigator	Q64428.
GermOnline	ENSRNOG00000024629. Rattus norvegicus.
Family and domain databases
InterPro	IPR006180. 3-OHacyl-CoA_DH_CS. IPR006176. 3-OHacyl-CoA_DH_NAD-bd. IPR006108. 3HC_DH_C. IPR008927. 6-PGluconate_DH_C-like. IPR001753. Crotonase_core. IPR013328. DH_multihelical. IPR018376. Enoyl-CoA_hyd/isom_CS. IPR012803. Fa_ox_alpha_mit. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 2 hits.
KO	K07515.
Pfam	PF00725. 3HCDH. 2 hits. PF02737. 3HCDH_N. 1 hit. PF00378. ECH. 1 hit. [Graphical view]
SUPFAM	SSF48179. 6DGDH_C_like. 2 hits.
TIGRFAMs	TIGR02441. Fa_ox_alpha_mit. 1 hit.
PROSITE	PS00067. 3HCDH. 1 hit. PS00166. ENOYL_COA_HYDRATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	621163.

Entry information

Entry name

ECHA_RAT

Accession

Primary (citable) accession number: Q64428
Secondary accession number(s): Q5BIZ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	March 18, 2008
Last modified:	November 16, 2011
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents