ID DGDA_BURCE STANDARD; PRT; 432 AA. AC P16932; DT 01-AUG-1990 (Rel. 15, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 01-FEB-2005 (Rel. 46, Last annotation update) DE 2,2-dialkylglycine decarboxylase (EC 4.1.1.64) (DGD). GN Name=dgdA; OS Burkholderia cepacia (Pseudomonas cepacia). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=292; RN [1] RP NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 1-19 AND 260-275. RX MEDLINE=90202788; PubMed=2180928; RA Keller J.W., Baurick K.B., Rutt G.C., O'Malley M.V., Sonafrank N.L., RA Reynolds R.A., Ebbesson L.O.E., Vajdos F.F.; RT "Pseudomonas cepacia 2,2-dialkylglycine decarboxylase. Sequence and RT expression in Escherichia coli of structural and repressor genes."; RL J. Biol. Chem. 265:5531-5539(1990). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RX MEDLINE=93342511; PubMed=8342040; RA Toney M.D., Hohenester E., Cowan S.W., Jansonius J.N.; RT "Dialkylglycine decarboxylase structure: bifunctional active site and RT alkali metal sites."; RL Science 261:756-759(1993). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND SEQUENCE REVISION TO 51; RP 81-82 AND 307-311. RX MEDLINE=95034792; PubMed=7947767; RA Hohenester E., Keller J.W., Jansonius J.N.; RT "An alkali metal ion size-dependent switch in the active site RT structure of dialkylglycine decarboxylase."; RL Biochemistry 33:13561-13570(1994). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX MEDLINE=95097385; PubMed=7799433; RA Toney M.D., Hohenester E., Keller J.W., Jansonius J.N.; RT "Structural and mechanistic analysis of two refined crystal structures RT of the pyridoxal phosphate-dependent enzyme dialkylglycine RT decarboxylase."; RL J. Mol. Biol. 245:151-179(1995). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX MEDLINE=20027099; PubMed=10556038; DOI=10.1006/jmbi.1999.3254; RA Malashkevich V.N., Strop P., Keller J.W., Jansonius J.N., Toney M.D.; RT "Crystal structures of dialkylglycine decarboxylase inhibitor RT complexes."; RL J. Mol. Biol. 294:193-200(1999). CC -!- FUNCTION: The dialkylglycine decarboxylase is of interest because CC it normally catalyzes both decarboxylation and amino transfer. It CC may be more properly described as a decarboxylating CC aminotransferase rather than an aminotransferring decarboxylase. CC -!- CATALYTIC ACTIVITY: 2,2-dialkylglycine + pyruvate = dialkyl ketone CC + CO(2) + L-alanine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- SUBUNIT: Homotetramer. CC -!- MISCELLANEOUS: The enzyme may have evolved to use the rare CC dialkylglycines of cosmic origin, or it may be part of a metabolic CC pathway for breaking down cytotoxic peptides and the constituent CC amino acids. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase 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; J05282; AAA50844.1; -. DR PIR; A35173; A35173. DR PDB; 1D7R; X-ray; A=1-432. DR PDB; 1D7S; X-ray; A=1-432. DR PDB; 1D7U; X-ray; A=1-432. DR PDB; 1D7V; X-ray; A=1-432. DR PDB; 1DGD; X-ray; @=1-432. DR PDB; 1DGE; X-ray; @=1-432. DR PDB; 1DKA; X-ray; @=1-432. DR PDB; 1M0N; X-ray; A=1-432. DR PDB; 1M0O; X-ray; A=1-432. DR PDB; 1M0P; X-ray; A=1-432. DR PDB; 1M0Q; X-ray; A=1-432. DR PDB; 2DKB; X-ray; @=1-432. DR InterPro; IPR005814; Aminotrans_3. DR Pfam; PF00202; Aminotran_3; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. KW 3D-structure; Decarboxylase; Direct protein sequencing; Lyase; KW Pyridoxal phosphate. FT INIT_MET 0 0 FT BINDING 271 271 Pyridoxal phosphate (covalent). FT HELIX 6 15 FT STRAND 28 33 FT TURN 34 34 FT STRAND 35 38 FT TURN 39 40 FT STRAND 43 46 FT TURN 47 48 FT HELIX 49 52 FT TURN 53 53 FT TURN 55 56 FT STRAND 58 58 FT TURN 59 59 FT HELIX 61 73 FT TURN 79 80 FT HELIX 84 96 FT TURN 99 100 FT STRAND 103 107 FT HELIX 110 125 FT STRAND 129 133 FT TURN 134 135 FT HELIX 142 146 FT TURN 147 147 FT TURN 161 162 FT STRAND 163 166 FT TURN 171 172 FT STRAND 177 178 FT TURN 179 180 FT STRAND 181 182 FT HELIX 184 198 FT STRAND 203 208 FT STRAND 211 212 FT TURN 213 216 FT STRAND 218 219 FT TURN 222 223 FT HELIX 224 234 FT TURN 235 236 FT STRAND 238 242 FT TURN 244 251 FT HELIX 256 260 FT TURN 261 261 FT STRAND 266 269 FT TURN 275 276 FT STRAND 280 284 FT HELIX 286 295 FT TURN 296 296 FT TURN 302 305 FT HELIX 307 322 FT TURN 323 324 FT HELIX 325 346 FT TURN 348 349 FT STRAND 350 356 FT TURN 357 358 FT STRAND 359 365 FT TURN 368 371 FT STRAND 373 373 FT HELIX 377 388 FT TURN 389 389 FT STRAND 390 391 FT STRAND 394 395 FT TURN 398 399 FT STRAND 403 406 FT TURN 410 411 FT HELIX 414 432 SQ SEQUENCE 432 AA; 46313 MW; 90A4A5C7FB6127E1 CRC64; SLNDDATFWR NARQHLVRYG GTFEPMIIER AKGSFVYDAD GRAILDFTSG QMSAVLGHCH PEIVSVIGEY AGKLDHLFSG MLSRPVVDLA TRLANITPPG LDRALLLSTG AESNEAAIRM AKLVTGKYEI VGFAQSWHGM TGAAASATYS AGRKGVGPAA VGSFAIPAPF TYRPRFERNG AYDYLAELDY AFDLIDRQSS GNLAAFIAEP ILSSGGIIEL PDGYMAALKR KCEARGMLLI LDEAQTGVGR TGTMFACQRD GVTPDILTLS KTLGAGLPLA AIVTSAAIEE RAHELGYLFY TTHVSDPLPA AVGLRVLDVV QRDGLVARAN VMGDRLRRGL LDLMERFDCI GDVRGRGLLL GVEIVKDRRT KEPADGLGAK ITRECMNLGL SMNIVQLPGM GGVFRIAPPL TVSEDEIDLG LSLLGQAIER AL //