ID   DLDH_PIG                Reviewed;         509 AA.
AC   P09623;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   16-JUN-2009, entry version 90.
DE   RecName: Full=Dihydrolipoyl dehydrogenase, mitochondrial;
DE            EC=1.8.1.4;
DE   AltName: Full=Dihydrolipoamide dehydrogenase;
DE   Flags: Precursor;
GN   Name=DLD; Synonyms=LAD;
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].
RX   MEDLINE=88087005; PubMed=3693355;
RA   Otulakowski G., Robinson B.H.;
RT   "Isolation and sequence determination of cDNA clones for porcine and
RT   human lipoamide dehydrogenase. Homology to other disulfide
RT   oxidoreductases.";
RL   J. Biol. Chem. 262:17313-17318(1987).
RN   [2]
RP   PROTEIN SEQUENCE OF 36-89; 91-104; 317-331; 346-360; 388-417 AND
RP   450-482.
RC   TISSUE=Heart;
RX   MEDLINE=82247969; PubMed=6954534; DOI=10.1073/pnas.79.7.2199;
RA   Williams C.H. Jr., Arscott L.D., Schulz G.E.;
RT   "Amino acid sequence homology between pig heart lipoamide
RT   dehydrogenase and human erythrocyte glutathione reductase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 79:2199-2201(1982).
CC   -!- FUNCTION: Lipoamide dehydrogenase is a component of the glycine
CC       cleavage system as well as of the alpha-ketoacid dehydrogenase
CC       complexes.
CC   -!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
CC       protein N(6)-(lipoyl)lysine + NADH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SUBUNIT: Eukaryotic pyruvate dehydrogenase complexes are organized
CC       about a core consisting of the oligomeric dihydrolipoamide acetyl-
CC       transferase, around which are arranged multiple copies of pyruvate
CC       dehydrogenase, dihydrolipoamide dehydrogenase and protein X bound
CC       by non-covalent bonds (By similarity). Homodimer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family.
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DR   EMBL; J03489; AAA31069.1; -; mRNA.
DR   PIR; A28448; DEPGLP.
DR   RefSeq; NP_999227.1; -.
DR   UniGene; Ssc.224; -.
DR   HSSP; P09624; 1JEH.
DR   SMR; P09623; 37-509.
DR   GeneID; 397129; -.
DR   KEGG; ssc:397129; -.
DR   HOVERGEN; P09623; -.
DR   BRENDA; 1.8.1.4; 249.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:EC.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR000815; Hg_reductase.
DR   InterPro; IPR006258; Lipoamide_DH.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   Gene3D; G3DSA:3.30.390.30; Pyr_redox_dim; 1.
DR   PANTHER; PTHR22912:SF20; Lipoamide_DH; 1.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00945; HGRDTASE.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
DR   TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Disulfide bond; FAD;
KW   Flavoprotein; Mitochondrion; NAD; Oxidoreductase; Redox-active center;
KW   Transit peptide.
FT   TRANSIT       1     35       Mitochondrion.
FT   CHAIN        36    509       Dihydrolipoyl dehydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000030298.
FT   NP_BIND      71     80       FAD (By similarity).
FT   NP_BIND     183    185       FAD (By similarity).
FT   NP_BIND     220    227       NAD (By similarity).
FT   NP_BIND     361    364       FAD (By similarity).
FT   ACT_SITE    487    487       Proton acceptor (By similarity).
FT   BINDING      89     89       FAD (By similarity).
FT   BINDING     154    154       FAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     243    243       NAD (By similarity).
FT   BINDING     278    278       NAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     314    314       NAD; via amide nitrogen (By similarity).
FT   BINDING     355    355       FAD (By similarity).
FT   MOD_RES     127    127       N6-acetyllysine (By similarity).
FT   DISULFID     80     85       Redox-active (By similarity).
FT   CONFLICT     95     97       SHY -> GHA (in Ref. 2; AA sequence).
FT   CONFLICT    346    346       K -> R (in Ref. 2; AA sequence).
FT   CONFLICT    351    351       Y -> A (in Ref. 2; AA sequence).
SQ   SEQUENCE   509 AA;  54185 MW;  38A0469FED071300 CRC64;
     MQSWSRVYCT LAKRGHFNRI AHGLQGVSAV PLRTYADQPI DADVTVIGSG PGGYVAAIKA
     AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHM AHGKDFASRG IEMSEVRLNL
     EKMMEQKSNA VKALTGGIAH LFKQNKVVRV NGYGKITGKN QVTATKADGS TEVINTKNIL
     IATGSEVTPF PGITIDEDTV VSSTGALSLK KVPEKMVVIG AGVIGVELGS VWQRLGADVT
     AVELLGHVGG IGIDMEVSKN FQRILQKQGF KFKLNTKVIG ATKKSDGNID VSIEAASGGK
     AEVITCDVLL VCIGRRPFTQ NLGLEELGIE LDPRGRIPVN TRFQTKIPNI YAIGDVVAGP
     MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA WVGKSEEQLK EEGIEYKVGK
     FPFAANSRAK TNADTDGMVK ILGQKSTDRV LGAHIIGPGA GEMINEAALA LEYGASCEDI
     ARVCHAHPTL SEAFREANLA ASFGKAINF
//