ID DLDH_AZOVI STANDARD; PRT; 477 AA. AC P18925; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 25-OCT-2004 (Rel. 45, Last annotation update) DE Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of pyruvate DE complex) (Dihydrolipoamide dehydrogenase). OS Azotobacter vinelandii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=354; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=88166699; PubMed=2832161; RA Westphal A.H., de Kok A.; RT "Lipoamide dehydrogenase from Azotobacter vinelandii. Molecular RT cloning, organization and sequence analysis of the gene."; RL Eur. J. Biochem. 172:299-305(1988). RN [2] RP NUCLEOTIDE SEQUENCE OF 1-21. RX MEDLINE=90126825; PubMed=2404760; RA Westphal A.H., de Kok A.; RT "The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. RT 2. Molecular cloning and sequence analysis of the gene encoding the RT succinyltransferase component."; RL Eur. J. Biochem. 187:235-239(1990). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX MEDLINE=91350192; PubMed=1880807; RA Mattevi A., Schierbeek A.J., Hol W.G.J.; RT "Refined crystal structure of lipoamide dehydrogenase from Azotobacter RT vinelandii at 2.2-A resolution. A comparison with the structure of RT glutathione reductase."; RL J. Mol. Biol. 220:975-994(1991). CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall CC conversion of pyruvate to acetyl-CoA and CO(2). It contains CC multiple copies of three enzymatic components: pyruvate CC dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and CC lipoamide dehydrogenase (E3). CC -!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = CC protein N(6)-(lipoyl)lysine + NADH. CC -!- COFACTOR: Binds 1 FAD per subunit. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide CC oxidoreductase family. CC -------------------------------------------------------------------------- CC This Swiss-Prot entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use as long as its content is in no way modified and this statement is not CC removed. CC -------------------------------------------------------------------------- DR EMBL; M37307; AAA22139.1; -. DR EMBL; X52432; CAA36679.1; -. DR PIR; S00360; DEAVHL. DR PDB; 3LAD; X-ray; A/B=2-477. DR InterPro; IPR001327; FAD_pyr_redox. DR InterPro; IPR000815; Hg_reductase. DR InterPro; IPR006258; Lipoamide_dh. DR InterPro; IPR001100; Pyr_redox. DR InterPro; IPR004099; Pyr_redox_dim. DR InterPro; IPR003042; Rng_mnoxygenase. DR Pfam; PF00070; Pyr_redox; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR PRINTS; PR00368; FADPNR. DR PRINTS; PR00945; HGRDTASE. DR PRINTS; PR00411; PNDRDTASEI. DR PRINTS; PR00420; RNGMNOXGNASE. DR ProDom; PD000139; FAD_pyr_redox; 1. DR TIGRFAMs; TIGR01350; lipoamide_DH; 1. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. KW 3D-structure; FAD; Flavoprotein; Glycolysis; NAD; Oxidoreductase; KW Redox-active center. FT NP_BIND 34 49 FAD (ADP part) (By similarity). FT DISULFID 49 54 Redox-active. FT NP_BIND 188 190 Pyrophosphate (By similarity). FT ACT_SITE 451 451 Proton acceptor. FT STRAND 7 10 FT HELIX 14 25 FT TURN 26 27 FT STRAND 30 34 FT STRAND 37 37 FT TURN 39 40 FT STRAND 43 43 FT HELIX 47 52 FT HELIX 54 72 FT TURN 73 73 FT HELIX 74 77 FT TURN 78 78 FT STRAND 79 80 FT STRAND 85 86 FT HELIX 88 112 FT TURN 113 114 FT STRAND 116 119 FT STRAND 121 124 FT TURN 126 127 FT STRAND 130 134 FT TURN 135 137 FT STRAND 138 138 FT STRAND 141 142 FT STRAND 146 149 FT STRAND 153 155 FT STRAND 158 158 FT TURN 159 160 FT STRAND 161 161 FT STRAND 168 169 FT HELIX 171 175 FT TURN 176 176 FT STRAND 183 187 FT HELIX 191 203 FT TURN 204 204 FT STRAND 206 210 FT TURN 218 219 FT HELIX 222 234 FT TURN 235 236 FT STRAND 237 240 FT TURN 241 242 FT STRAND 244 251 FT TURN 252 253 FT STRAND 254 260 FT STRAND 264 270 FT STRAND 272 275 FT STRAND 279 281 FT TURN 284 285 FT STRAND 287 287 FT STRAND 295 295 FT TURN 297 298 FT STRAND 301 301 FT STRAND 303 303 FT TURN 305 306 FT STRAND 308 309 FT TURN 312 313 FT STRAND 314 316 FT HELIX 318 320 FT HELIX 327 341 FT HELIX 350 352 FT STRAND 355 357 FT STRAND 362 367 FT HELIX 370 373 FT TURN 374 377 FT STRAND 380 386 FT HELIX 387 389 FT HELIX 391 395 FT TURN 396 397 FT STRAND 402 408 FT STRAND 413 421 FT TURN 422 423 FT HELIX 424 436 FT TURN 437 438 FT STRAND 440 440 FT HELIX 441 445 FT TURN 446 446 FT TURN 454 455 FT HELIX 456 465 FT TURN 466 467 SQ SEQUENCE 477 AA; 49567 MW; 4219A8EA4DAFCAD0 CRC64; MSQKFDVIVI GAGPGGYVAA IKSAQLGLKT ALIEKYKGKE GKTALGGTCL NVGCIPSKAL LDSSYKFHEA HESFKLHGIS TGEVAIDVPT MIARKDQIVR NLTGGVASLI KANGVTLFEG HGKLLAGKKV EVTAADGSSQ VLDTENVILA SGSKPVEIPP APVDQDVIVD STGALDFQNV PGKLGVIGAG VIGLELGSVW ARLGAEVTVL EAMDKFLPAV DEQVAKEAQK ILTKQGLKIL LGARVTGTEV KNKQVTVKFV DAEGEKSQAF DKLIVAVGRR PVTTDLLAAD SGVTLDERGF IYVDDYCATS VPGVYAIGDV VRGAMLAHKA SEEGVVVAER IAGHKAQMNY DLIPAVIYTH PEIAGVGKTE QALKAEGVAI NVGVFPFAAS GRAMAANDTA GFVKVIADAK TDRVLGVHVI GPSAAELVQQ GAIAMEFGTS AEDLGMMVFA HPALSEALHE AALAVSGHAI HVANRKK //