ID DLDH_AZOVI STANDARD; PRT; 477 AA. AC P18925; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 07-MAR-2006, entry version 61. 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 [GENOMIC DNA]. 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 [GENOMIC DNA] 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: 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M37307; AAA22139.1; -; Genomic_DNA. DR EMBL; X52432; CAA36679.1; -; Genomic_DNA. DR PIR; S00360; DEAVHL. DR PDB; 3LAD; X-ray; A/B=2-477. DR LinkHub; P18925; -. DR InterPro; IPR013027; 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; IPR012999; Pyr_redox_I_AS. DR InterPro; IPR001327; Pyr_redox_NAD_bd. DR InterPro; IPR003042; Rng_hydrolase. DR PANTHER; PTHR11493:SF98; 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 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 CHAIN 1 477 Dihydrolipoyl dehydrogenase. FT /FTId=PRO_0000068014. FT NP_BIND 34 49 FAD (ADP part) (By similarity). FT NP_BIND 188 190 Pyrophosphate (By similarity). FT ACT_SITE 451 451 Proton acceptor. FT DISULFID 49 54 Redox-active. FT STRAND 6 10 FT STRAND 13 13 FT HELIX 14 26 FT TURN 27 27 FT STRAND 30 34 FT STRAND 37 37 FT TURN 39 40 FT STRAND 41 43 FT STRAND 46 46 FT HELIX 47 52 FT STRAND 53 53 FT HELIX 54 71 FT TURN 72 73 FT STRAND 74 74 FT HELIX 75 77 FT TURN 78 78 FT STRAND 79 80 FT STRAND 82 82 FT STRAND 85 86 FT HELIX 88 113 FT TURN 114 114 FT STRAND 116 124 FT STRAND 126 126 FT TURN 127 128 FT STRAND 130 133 FT TURN 135 136 FT STRAND 137 137 FT STRAND 139 142 FT STRAND 145 145 FT STRAND 147 149 FT STRAND 153 155 FT TURN 159 160 FT STRAND 161 161 FT STRAND 165 170 FT HELIX 171 174 FT TURN 175 175 FT STRAND 176 176 FT STRAND 178 179 FT STRAND 182 187 FT STRAND 190 190 FT HELIX 191 202 FT TURN 203 204 FT STRAND 206 217 FT TURN 218 219 FT STRAND 220 220 FT HELIX 222 234 FT TURN 235 236 FT STRAND 237 241 FT TURN 242 242 FT STRAND 244 250 FT STRAND 252 253 FT STRAND 255 275 FT STRAND 277 277 FT STRAND 279 281 FT TURN 284 285 FT STRAND 288 289 FT STRAND 292 292 FT STRAND 295 295 FT TURN 297 298 FT STRAND 299 299 FT STRAND 301 301 FT TURN 305 306 FT STRAND 307 308 FT STRAND 310 311 FT TURN 312 313 FT STRAND 314 316 FT HELIX 318 320 FT STRAND 321 323 FT HELIX 327 343 FT TURN 350 351 FT STRAND 355 357 FT STRAND 359 367 FT HELIX 370 375 FT TURN 376 377 FT STRAND 380 386 FT HELIX 387 389 FT HELIX 391 396 FT TURN 397 397 FT STRAND 402 408 FT TURN 409 411 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 STRAND 447 447 FT STRAND 451 452 FT STRAND 454 454 FT HELIX 455 465 FT TURN 466 467 FT TURN 470 471 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 //