Reviewed, UniProtKB/Swiss-Prot Q29554 (ECHA_PIG)

Names and origin

Protein names

Recommended name:
    Trifunctional enzyme subunit alpha, mitochondrial
Alternative name(s):
    TP-alpha
    78 kDa gastrin-binding protein
Including the following 2 domains:
    1- Recommended name:
            Long-chain enoyl-CoA hydratase
              EC=4.2.1.17
    2- Recommended name:
            Long chain 3-hydroxyacyl-CoA dehydrogenase
              EC=1.1.1.211

Gene names

Name:	HADHA
Synonyms:	LCHYD-HAD

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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; cannot use crotonyl-CoA or 3-hydroxybutyryl-CoA as substrate.
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 By similarity.
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.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NAD
Molecular function	Lyase Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	fatty acid beta-oxidation multienzyme complex Inferred from electronic annotation. Source: InterPro
Molecular function	3-hydroxyacyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: InterPro coenzyme binding Inferred from electronic annotation. Source: InterPro enoyl-CoA hydratase activity Inferred from electronic annotation. Source: EC long-chain-3-hydroxyacyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 36	36	Mitochondrion Potential
	Chain	37 – 763	727	Trifunctional enzyme subunit alpha, mitochondrial		PRO_0000007404
Sites
	Active site	151	1	By similarity
	Active site	173	1	Proton donor By similarity
Amino acid modifications
	Modified residue	569	1	N6-acetyllysine By similarity
	Modified residue	728	1	N6-acetyllysine By similarity
	Modified residue	756	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q29554-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: DD0C6E7AE6B3D0F4	FASTA	763	83,107
	10 20 30 40 50 60 MVASRAIGSL RRFTASQTLR CPGYICRNFT RSSALLTRTH INYGVKGDVA VIRINSPNSK 70 80 90 100 110 120 VNTLGQELHS EFIEVMNEVW SSSQIRSAVL ISSKPGCFIA GADINMLSAC TTSQEVTQIS 130 140 150 160 170 180 QEAQRTFEKL EKSTKPIVAA INGTCLGGGL ELAISCQYRI ATKDKKTVLG APEVLLGILP 190 200 210 220 230 240 GAGGTQRLPK MVGVPAAFDM MLTGRGIRAD KAKKMGLVDQ LVEPLGPGLK PPEERTIEYL 250 260 270 280 290 300 EEVAVTFAKG LADKKISPKR DKGLVEKLTS YAMSIPFVRQ QIYKKVEEKV RKQTKGLYPA 310 320 330 340 350 360 PLKIIDVVKT GIEQGSDAGY LSESQKFGEL AMTKESKALM GLYRGQTLCK KNKFGAPQKE 370 380 390 400 410 420 VKHLAILGAG LMGAGIAQVS VDKHLKTILK DASLPALGRG QQQVFKGLND KVRKKALTSF 430 440 450 460 470 480 ERDSLFSNLT GQLDYQGFEK ADMVIEAVFE ELSLKHKVLK EVEAVIPDHC VFASNTSALP 490 500 510 520 530 540 ISEIAAVSKR PEKVIGMHYF SPVDKMQLLE IITTEKTSKD STASAVEVGL KQGKVIIVVK 550 560 570 580 590 600 DGPGFYTTRC LAPMMSEVLR ILQEGVGPKK LDSLTTSFGF PVGAATLMDE VGMDVAKHVA 610 620 630 640 650 660 ENLGKIFGER FAGGNLDVLK QMISKGFLGR KSGKGFYVYQ EGVKNRNVNS DTESILASLK 670 680 690 700 710 720 IPSRPDISSD EDIQYRLVTR FVNEAVLCLQ EGILATPAEG DIGAVFGLGF PPCLGGPFRF 730 740 750 760 VDLYGAQKVV DRLRKYEAIY GKQFTPCQLL IDHASSPNKK FFQ

References

[1]	"Nucleotide sequence encoding a novel member of the hydratase/dehydrogenase family." Mantamadiotis T., Sobieszczuk P., Weinstock J., Baldwin G.S. Biochim. Biophys. Acta 1170:211-215(1993) [PubMed: 8399347] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Stomach.
[2]	"Primary structure of the large subunit of trifunctional beta-oxidation complex from pig heart mitochondria." Yang S.-Y., He X.-Y., Styles J., Luo M.J., Schulz H., Elzinga M. Biochem. Biophys. Res. Commun. 198:431-437(1994) [PubMed: 8297352] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[3]	"Partial structure of the gene encoding the 78 kDa gastrin binding protein excludes a close relationship with the peroxisomal trifunctional enzyme." Baldwin G.S., Casey A., Weinstock J. Biochem. Biophys. Res. Commun. 193:560-564(1993) [PubMed: 8512557] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE. Tissue: Liver.
[4]	"The large subunit of the pig heart mitochondrial membrane-bound beta-oxidation complex is a long-chain enoyl-CoA hydratase: 3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme." Yang S.-Y. Comp. Biochem. Physiol. 109B:557-566(1994) [PubMed: 7881821] [Abstract] Cited for: CHARACTERIZATION. Tissue: Heart.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L12581 mRNA. Translation: AAA03733.1. AF028609 mRNA. Translation: AAB84118.1.
PIR	PN0511.
RefSeq	NP_999127.1.
UniGene	Ssc.11580
3D structure databases
HSSP	HSSP built from PDB template 1MJ3 based on UniProtKB P14604.
ModBase	Search...
Genome annotation databases
GeneID	397012.
KEGG	ssc:397012.
Phylogenomic databases
HOVERGEN	Q29554.
Enzyme and pathway databases
BRENDA	1.1.1.211. 249. 4.2.1.17. 249.
Family and domain databases
InterPro	IPR006180. 3-OHacyl-CoA_DH_CS. IPR006176. 3-OHacyl-CoA_DH_NAD-bd. IPR006108. 3HC_DH_C. IPR001753. Crotonase_core. IPR013328. DH_multihelical. IPR018376. Enoyl-CoA_hyd/isom_CS. IPR012803. Fa_ox_alpha_mit. [Graphical view]
Gene3D	G3DSA:1.10.1040.10. Opine_DH. 1 hit.
Pfam	PF00725. 3HCDH. 1 hit. PF02737. 3HCDH_N. 1 hit. PF00378. ECH. 1 hit. [Graphical view]
TIGRFAMs	TIGR02441. fa_ox_alpha_mit. 1 hit.
PROSITE	PS00067. 3HCDH. 1 hit. PS00166. ENOYL_COA_HYDRATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ECHA_PIG

Accession

Primary (citable) accession number: Q29554

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)