ID   DLDH_CRIGR              Reviewed;         509 AA.
AC   Q8CIZ7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 38.
DE   RecName: Full=Dihydrolipoyl dehydrogenase, mitochondrial;
DE            EC=1.8.1.4;
DE   AltName: Full=Dihydrolipoamide dehydrogenase;
DE   Flags: Precursor;
GN   Name=DLD;
OS   Cricetulus griseus (Chinese hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Keightley J.A., Shang L., Kinter M.;
RT   "2D gel analysis of the proteomic adaptation of a mammalian cell line
RT   to oxidative stress reveals changes in the expression of metabolically
RT   relevant enzymes.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Lipoamide dehydrogenase is a component of the glycine
CC       cleavage system as well as of the alpha-ketoacid dehydrogenase
CC       complexes (By similarity).
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: Homodimer. Eukaryotic pyruvate dehydrogenase complexes
CC       are organized about a core consisting of the oligomeric
CC       dihydrolipoamide acetyl-transferase, around which are arranged
CC       multiple copies of pyruvate dehydrogenase, dihydrolipoamide
CC       dehydrogenase and protein X bound by non-covalent bonds (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
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; AF539836; AAN15202.1; -; mRNA.
DR   HSSP; P31023; 1DXL.
DR   SMR; Q8CIZ7; 37-509.
DR   HOVERGEN; Q8CIZ7; -.
DR   BRENDA; 1.8.1.4; 18.
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   2: Evidence at transcript level;
KW   Acetylation; Disulfide bond; FAD; Flavoprotein; Mitochondrion; NAD;
KW   Oxidoreductase; Redox-active center; Transit peptide.
FT   TRANSIT       1     35       Mitochondrion (By similarity).
FT   CHAIN        36    509       Dihydrolipoyl dehydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000260226.
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).
SQ   SEQUENCE   509 AA;  54131 MW;  FADBCF01E42576AB CRC64;
     MQSWSRVYCS LAKRGHFNRI SHGLQGVSSV PLRTYADQPI DADVTVIGSG PGGYVAAIKA
     AQLGFKTVCI EKNDTLGGTC LNVGCIPSKA LLNNSHYYHL AHGRDFASRG IELSEVRLNL
     EKMMEQKSSA VKALIGGIAH LFKQNKVVHV NGFGKITGKN QVTATKADGS SQVIGTKNIL
     IATGSEVTPF PGITIDEDTI VSSTGALSLK KVPEKLVVIG AGVIGVELGS VWQRLGADVT
     AVEFLGHVGG IGIDMEISKN FQRILQKQGF KFKLNTKVTG ATKRSDGKID VSVEAASGGK
     AEVITCDVLL VCIGRRPFTQ NLGLEELGIE LDPRGRIPVN TRFQTKIPNI YAIGDVVAGP
     MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA WVGKSEEQLK EEGIEYKVGK
     FPFAANSRAK TNADTDGMVK ILGQKSTDRV LGAHILGPGA GEMVNEAALA LEYGASCEDI
     ARVCHAHPTL SEAFREANLA ASFGKPINF
//