ID   DLDH_HALVO              Reviewed;         475 AA.
AC   Q04829;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 70.
DE   RecName: Full=Dihydrolipoyl dehydrogenase;
DE            EC=1.8.1.4;
DE   AltName: Full=Dihydrolipoamide dehydrogenase;
GN   Name=lpdA; Synonyms=lpd;
OS   Halobacterium volcanii (Haloferax volcanii).
OC   Archaea; Euryarchaeota; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Haloferax.
OX   NCBI_TaxID=2246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 326-348.
RC   STRAIN=ATCC 29605 / DS2 / DSM 3757 / IFO 14742 / NCIMB 2012;
RX   MEDLINE=93119588; PubMed=1339281;
RA   Vettakkorumakankav N.N., Stevenson K.J.;
RT   "Dihydrolipoamide dehydrogenase from Haloferax volcanii: gene cloning,
RT   complete primary structure, and comparison to other dihydrolipoamide
RT   dehydrogenases.";
RL   Biochem. Cell Biol. 70:656-663(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-49.
RX   MEDLINE=92255933; PubMed=1581034;
RA   Vettakkorumakankav N.N., Danson M.J., Hough D.W.;
RT   "Dihydrolipoamide dehydrogenase from the halophilic archaebacterium
RT   Haloferax volcanii: characterization and N-terminal sequence.";
RL   Biochem. Cell Biol. 70:70-75(1992).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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; L09733; AAA72340.1; -; Genomic_DNA.
DR   PIR; A56824; A56824.
DR   HSSP; P11959; 1EBD.
DR   BRENDA; 1.8.1.4; 430.
DR   GO; GO:0005737; C:cytoplasm; 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   Cytoplasm; Direct protein sequencing; Disulfide bond; FAD;
KW   Flavoprotein; Glycolysis; NAD; Oxidoreductase; Redox-active center.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    475       Dihydrolipoyl dehydrogenase.
FT                                /FTId=PRO_0000068058.
FT   NP_BIND      39     47       FAD (By similarity).
FT   NP_BIND     186    190       NAD (By similarity).
FT   NP_BIND     275    278       NAD (By similarity).
FT   ACT_SITE    451    451       Proton acceptor (By similarity).
FT   BINDING      56     56       FAD (By similarity).
FT   BINDING     118    118       FAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     209    209       NAD (By similarity).
FT   BINDING     318    318       FAD (By similarity).
FT   BINDING     327    327       FAD; via amide nitrogen (By similarity).
FT   DISULFID     47     52       Redox-active (By similarity).
SQ   SEQUENCE   475 AA;  49988 MW;  6894BDE536D205D5 CRC64;
     MVVGDIATGT ELLVIGAGPG GYVAAIRAAQ NGIDTTLVEK DAYGGTCLNY GCIPSKALIT
     GANLAHEAGN AEEMGIHADP VVDMSQLRDW KSGVVDQLTG GVEKLCKANG VNLVEGTARF
     KDENAVRIAH GGEGQGSETI EFEHCIIATG SRVIQIPGFD FGDEPVWSSR DALEADTVPE
     RLVVVGGGYI GMELSTTFAK LGADVTVVEM LDDILPGYES DVARVVRKRA EELGIDMHLG
     EGATGWREED DGIMVTTETE DGEENEYRAD KVLVAVGRSP VTDTMDIENA GLEADDRGFL
     SVDDRRRTDV EHIYAVGDVV EDTPMLAHVA SKEGIVAAEH VAGEPVAFDS QAVPAAVFTD
     PEIGTVGMTE ADAEEAGFTP VVGQMPFRAS GRALTTNHAD GFVRVVADEE SGFVLGAQIV
     GPEASELIAE LAFAIEMGAT LEDVASTIHT HPTLAEAVME AAENALGQAI HTLNR
//