ID DGDA_BURCE STANDARD; PRT; 432 AA. AC P16932; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 2. DT 07-MAR-2006, entry version 56. 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; Burkholderia cepacia complex. OX NCBI_TaxID=292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-19 AND RP 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 Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J05282; AAA50844.1; -; Genomic_DNA. 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; 1Z3Z; X-ray; A=2-432. DR PDB; 1ZC9; X-ray; A=1-432. DR PDB; 2DKB; X-ray; @=1-432. DR LinkHub; P16932; -. DR InterPro; IPR005814; Aminotrans_3. DR PANTHER; PTHR11986; Aminotrans_3; 1. 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 CHAIN 1 432 2,2-dialkylglycine decarboxylase. FT /FTId=PRO_0000120509. FT BINDING 271 271 Pyridoxal phosphate (covalent). FT TURN 3 4 FT HELIX 6 15 FT STRAND 16 16 FT STRAND 20 21 FT STRAND 25 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 71 FT TURN 72 73 FT TURN 79 80 FT STRAND 82 82 FT HELIX 84 96 FT STRAND 97 97 FT TURN 99 100 FT STRAND 103 108 FT HELIX 110 125 FT TURN 126 126 FT STRAND 129 133 FT TURN 134 135 FT STRAND 140 141 FT HELIX 142 146 FT TURN 147 147 FT STRAND 150 151 FT STRAND 154 156 FT TURN 161 162 FT STRAND 163 166 FT STRAND 171 173 FT STRAND 177 182 FT HELIX 184 198 FT STRAND 201 201 FT STRAND 203 208 FT STRAND 210 212 FT TURN 213 216 FT STRAND 217 219 FT TURN 222 223 FT HELIX 224 234 FT TURN 235 236 FT STRAND 238 242 FT TURN 244 251 FT STRAND 252 255 FT HELIX 256 260 FT TURN 261 261 FT STRAND 265 269 FT TURN 271 271 FT HELIX 272 274 FT TURN 275 276 FT STRAND 277 278 FT STRAND 280 284 FT HELIX 286 294 FT TURN 295 296 FT STRAND 302 303 FT TURN 304 305 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 359 366 FT TURN 368 370 FT STRAND 373 373 FT TURN 375 376 FT HELIX 377 387 FT TURN 388 389 FT STRAND 390 391 FT STRAND 394 395 FT TURN 398 399 FT STRAND 400 400 FT STRAND 403 406 FT TURN 410 411 FT HELIX 414 431 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 //