ID ECHA_PIG Reviewed; 763 AA. AC Q29554; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 72. DE RecName: Full=Trifunctional enzyme subunit alpha, mitochondrial; DE AltName: Full=TP-alpha; DE AltName: Full=78 kDa gastrin-binding protein; DE Includes: DE RecName: Full=Long-chain enoyl-CoA hydratase; DE EC=4.2.1.17; DE Includes: DE RecName: Full=Long chain 3-hydroxyacyl-CoA dehydrogenase; DE EC=1.1.1.211; DE Flags: Precursor; GN Name=HADHA; Synonyms=LCHYD-HAD; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Stomach; RX MEDLINE=94002212; PubMed=8399347; DOI=10.1016/0005-2760(93)90073-I; RA Mantamadiotis T., Sobieszczuk P., Weinstock J., Baldwin G.S.; RT "Nucleotide sequence encoding a novel member of the RT hydratase/dehydrogenase family."; RL Biochim. Biophys. Acta 1170:211-215(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Heart; RX MEDLINE=94128080; PubMed=8297352; DOI=10.1006/bbrc.1994.1063; RA Yang S.-Y., He X.-Y., Styles J., Luo M.J., Schulz H., Elzinga M.; RT "Primary structure of the large subunit of trifunctional beta- RT oxidation complex from pig heart mitochondria."; RL Biochem. Biophys. Res. Commun. 198:431-437(1994). RN [3] RP PARTIAL NUCLEOTIDE SEQUENCE. RC TISSUE=Liver; RX MEDLINE=93290643; PubMed=8512557; DOI=10.1006/bbrc.1993.1660; RA Baldwin G.S., Casey A., Weinstock J.; RT "Partial structure of the gene encoding the 78 kDa gastrin binding RT protein excludes a close relationship with the peroxisomal RT trifunctional enzyme."; RL Biochem. Biophys. Res. Commun. 193:560-564(1993). RN [4] RP CHARACTERIZATION. RC TISSUE=Heart; RX MEDLINE=95187623; PubMed=7881821; DOI=10.1016/0305-0491(94)90117-1; RA Yang S.-Y.; RT "The large subunit of the pig heart mitochondrial membrane-bound beta- RT oxidation complex is a long-chain enoyl-CoA hydratase: 3-hydroxyacyl- RT CoA dehydrogenase bifunctional enzyme."; RL Comp. Biochem. Physiol. 109B:557-566(1994). CC -!- FUNCTION: Bifunctional subunit; cannot use crotonyl-CoA or 3- CC hydroxybutyryl-CoA as substrate. CC -!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl- CC CoA + H(2)O. CC -!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA CC + NADH. CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC -!- SUBUNIT: Octamer of 4 alpha (HADHA) and 4 beta (HADHB) subunits CC (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA CC hydratase/isomerase family. CC -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl- CC CoA dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L12581; AAA03733.1; -; mRNA. DR EMBL; AF028609; AAB84118.1; -; mRNA. DR PIR; PN0511; PN0511. DR RefSeq; NP_999127.1; -. DR UniGene; Ssc.11580; -. DR HSSP; P14604; 1MJ3. DR GeneID; 397012; -. DR KEGG; ssc:397012; -. DR HOVERGEN; Q29554; -. DR BRENDA; 1.1.1.211; 249. DR BRENDA; 4.2.1.17; 249. DR GO; GO:0016507; C:fatty acid beta-oxidation multienzyme complex; IEA:InterPro. DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:InterPro. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:EC. DR GO; GO:0016509; F:long-chain-3-hydroxyacyl-CoA dehydrogenase ...; IEA:EC. DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS. DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd. DR InterPro; IPR006108; 3HC_DH_C. DR InterPro; IPR001753; Crotonase_core. DR InterPro; IPR013328; DH_multihelical. DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS. DR InterPro; IPR012803; Fa_ox_alpha_mit. DR Gene3D; G3DSA:1.10.1040.10; Opine_DH; 1. DR Pfam; PF00725; 3HCDH; 1. DR Pfam; PF02737; 3HCDH_N; 1. DR Pfam; PF00378; ECH; 1. DR TIGRFAMs; TIGR02441; fa_ox_alpha_mit; 1. DR PROSITE; PS00067; 3HCDH; 1. DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1. PE 1: Evidence at protein level; KW Acetylation; Fatty acid metabolism; Lipid metabolism; Lyase; KW Mitochondrion; Multifunctional enzyme; NAD; Oxidoreductase; KW Phosphoprotein; Transit peptide. FT TRANSIT 1 36 Mitochondrion (Potential). FT CHAIN 37 763 Trifunctional enzyme subunit alpha, FT mitochondrial. FT /FTId=PRO_0000007404. FT ACT_SITE 151 151 By similarity. FT ACT_SITE 173 173 Proton donor (By similarity). FT MOD_RES 569 569 N6-acetyllysine (By similarity). FT MOD_RES 728 728 N6-acetyllysine (By similarity). FT MOD_RES 756 756 Phosphoserine (By similarity). SQ SEQUENCE 763 AA; 83107 MW; DD0C6E7AE6B3D0F4 CRC64; MVASRAIGSL RRFTASQTLR CPGYICRNFT RSSALLTRTH INYGVKGDVA VIRINSPNSK VNTLGQELHS EFIEVMNEVW SSSQIRSAVL ISSKPGCFIA GADINMLSAC TTSQEVTQIS QEAQRTFEKL EKSTKPIVAA INGTCLGGGL ELAISCQYRI ATKDKKTVLG APEVLLGILP GAGGTQRLPK MVGVPAAFDM MLTGRGIRAD KAKKMGLVDQ LVEPLGPGLK PPEERTIEYL EEVAVTFAKG LADKKISPKR DKGLVEKLTS YAMSIPFVRQ QIYKKVEEKV RKQTKGLYPA PLKIIDVVKT GIEQGSDAGY LSESQKFGEL AMTKESKALM GLYRGQTLCK KNKFGAPQKE VKHLAILGAG LMGAGIAQVS VDKHLKTILK DASLPALGRG QQQVFKGLND KVRKKALTSF ERDSLFSNLT GQLDYQGFEK ADMVIEAVFE ELSLKHKVLK EVEAVIPDHC VFASNTSALP ISEIAAVSKR PEKVIGMHYF SPVDKMQLLE IITTEKTSKD STASAVEVGL KQGKVIIVVK DGPGFYTTRC LAPMMSEVLR ILQEGVGPKK LDSLTTSFGF PVGAATLMDE VGMDVAKHVA ENLGKIFGER FAGGNLDVLK QMISKGFLGR KSGKGFYVYQ EGVKNRNVNS DTESILASLK IPSRPDISSD EDIQYRLVTR FVNEAVLCLQ EGILATPAEG DIGAVFGLGF PPCLGGPFRF VDLYGAQKVV DRLRKYEAIY GKQFTPCQLL IDHASSPNKK FFQ //