ID   DLDH_SYNY3              Reviewed;         474 AA.
AC   P72740; Q53395;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 76.
DE   RecName: Full=Dihydrolipoyl dehydrogenase;
DE            EC=1.8.1.4;
DE   AltName: Full=Dihydrolipoamide dehydrogenase;
DE            Short=LPD;
DE   AltName: Full=E3 component of pyruvate complex;
GN   Name=lpdA; Synonyms=pdhD; OrderedLocusNames=slr1096;
OS   Synechocystis sp. (strain PCC 6803).
OC   Bacteria; Cyanobacteria; Chroococcales; Synechocystis.
OX   NCBI_TaxID=1148;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=97061201; PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
RA   Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
RA   Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
RA   Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the
RT   entire genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-18, AND
RP   CHARACTERIZATION.
RX   MEDLINE=98048479; PubMed=9387233;
RA   Engels A., Pistorius E.K.;
RT   "Characterization of a gene encoding dihydrolipoamide dehydrogenase of
RT   the cyanobacterium Synechocystis sp. strain PCC 6803.";
RL   Microbiology 143:3543-3553(1997).
CC   -!- FUNCTION: Lipoamide dehydrogenase is a component of the alpha-
CC       ketoacid dehydrogenase 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: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane
CC       protein; Periplasmic side (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; BA000022; BAA16755.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z48564; CAA88451.1; -; Genomic_DNA.
DR   PIR; S74603; S74603.
DR   RefSeq; NP_440075.1; -.
DR   HSSP; P09624; 1JEH.
DR   IntAct; P72740; 2.
DR   GeneID; 953374; -.
DR   GenomeReviews; BA000022_GR; slr1096.
DR   KEGG; syn:slr1096; -.
DR   NMPDR; fig|1148.1.peg.176; -.
DR   HOGENOM; P72740; -.
DR   BioCyc; SSP1148:SLR1096-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; 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:0006096; P:glycolysis; IEA:UniProtKB-KW.
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   Cell inner membrane; Cell membrane; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW   Glycolysis; Membrane; NAD; Oxidoreductase; Redox-active center.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    474       Dihydrolipoyl dehydrogenase.
FT                                /FTId=PRO_0000068051.
FT   NP_BIND      36     44       FAD (By similarity).
FT   NP_BIND     184    188       NAD (By similarity).
FT   NP_BIND     275    278       NAD (By similarity).
FT   ACT_SITE    459    459       Proton acceptor (By similarity).
FT   BINDING      53     53       FAD (By similarity).
FT   BINDING     119    119       FAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     207    207       NAD (By similarity).
FT   BINDING     323    323       FAD (By similarity).
FT   BINDING     331    331       FAD; via amide nitrogen (By similarity).
FT   DISULFID     44     49       Redox-active (By similarity).
SQ   SEQUENCE   474 AA;  50832 MW;  A2EFD28D8D9C69E1 CRC64;
     MSQDFDYDLV IIGAGVGGHG AALHAVKCGL KTAIIEAKDM GGTCVNRGCI PSKALLAASG
     RVREMSDQDH LQQLGIQING VTFTREAIAA HANDLVSKIQ SDLTNSLTRL KVDTIRGWGK
     VSGPQEVTVI GDNETRILKA KEIMLCPGSV PFVPPGIEID HKTVFTSDEA VKLETLPQWI
     AIIGSGYIGL EFSDVYTALG CEVTMIEALP DLMPGFDPEI AKIAERVLIK SRDIETYTGV
     FATKIKAGSP VEIELTDAKT KEVIDTLEVD ACLVATGRIP ATKNLGLETV GVETDRRGFI
     EVNDQMQVIK DGKPVPHLWA VGDATGKMML AHAASGQGVV AVENICGRKT EVDYRAIPAA
     AFTHPEISYV GLTEAQAKEL GEKEGFVVST AKTYFKGNSK ALAEKETDGI AKVVYRQDTG
     ELLGAHIIGI HASDLIQEAA QAIADRKSVR ELAFHVHAHP TLSEVLDEAY KRAV
//