ID DGDA_BURCE Reviewed; 433 AA. AC P16932; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 129. DE RecName: Full=2,2-dialkylglycine decarboxylase; DE Short=DGD; DE EC=4.1.1.64; GN Name=dgdA; OS Burkholderia cepacia (Pseudomonas cepacia). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-20 AND RP 261-276. RX PubMed=2180928; DOI=10.1016/s0021-9258(19)39393-7; 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 PubMed=8342040; DOI=10.1126/science.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 52; 82-83 RP AND 308-312. RX PubMed=7947767; DOI=10.1021/bi00250a008; RA Hohenester E., Keller J.W., Jansonius J.N.; RT "An alkali metal ion size-dependent switch in the active site structure of RT dialkylglycine decarboxylase."; RL Biochemistry 33:13561-13570(1994). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=7799433; DOI=10.1006/jmbi.1994.0014; RA Toney M.D., Hohenester E., Keller J.W., Jansonius J.N.; RT "Structural and mechanistic analysis of two refined crystal structures of RT the pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase."; RL J. Mol. Biol. 245:151-179(1995). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX 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 complexes."; RL J. Mol. Biol. 294:193-200(1999). CC -!- FUNCTION: The dialkylglycine decarboxylase is of interest because it CC normally catalyzes both decarboxylation and amino transfer. It may be CC more properly described as a decarboxylating aminotransferase rather CC than an aminotransferring decarboxylase. CC -!- CATALYTIC ACTIVITY: CC Reaction=2,2-dialkylglycine + H(+) + pyruvate = CO2 + dialkyl ketone + CC L-alanine; Xref=Rhea:RHEA:16073, ChEBI:CHEBI:15361, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:18044, CC ChEBI:CHEBI:57689, ChEBI:CHEBI:57972; EC=4.1.1.64; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; 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 amino CC acids. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J05282; AAA50844.1; -; Genomic_DNA. DR PIR; A35173; A35173. DR PDB; 1D7R; X-ray; 2.00 A; A=1-433. DR PDB; 1D7S; X-ray; 2.05 A; A=1-433. DR PDB; 1D7U; X-ray; 1.95 A; A=1-433. DR PDB; 1D7V; X-ray; 2.80 A; A=1-433. DR PDB; 1DGD; X-ray; 2.80 A; A=2-433. DR PDB; 1DGE; X-ray; 2.80 A; A=2-433. DR PDB; 1DKA; X-ray; 2.60 A; A=1-433. DR PDB; 1M0N; X-ray; 2.20 A; A=1-433. DR PDB; 1M0O; X-ray; 2.40 A; A=1-433. DR PDB; 1M0P; X-ray; 2.60 A; A=1-433. DR PDB; 1M0Q; X-ray; 2.00 A; A=1-433. DR PDB; 1Z3Z; X-ray; 2.90 A; A=3-433. DR PDB; 1ZC9; X-ray; 2.00 A; A=1-433. DR PDB; 1ZOB; X-ray; 2.75 A; A=1-433. DR PDB; 1ZOD; X-ray; 1.80 A; A=1-433. DR PDB; 2DKB; X-ray; 2.10 A; A=1-433. DR PDBsum; 1D7R; -. DR PDBsum; 1D7S; -. DR PDBsum; 1D7U; -. DR PDBsum; 1D7V; -. DR PDBsum; 1DGD; -. DR PDBsum; 1DGE; -. DR PDBsum; 1DKA; -. DR PDBsum; 1M0N; -. DR PDBsum; 1M0O; -. DR PDBsum; 1M0P; -. DR PDBsum; 1M0Q; -. DR PDBsum; 1Z3Z; -. DR PDBsum; 1ZC9; -. DR PDBsum; 1ZOB; -. DR PDBsum; 1ZOD; -. DR PDBsum; 2DKB; -. DR AlphaFoldDB; P16932; -. DR SMR; P16932; -. DR STRING; 292.WI67_29060; -. DR DrugBank; DB03787; (5-Hydroxy-6-methyl-4-{[(E)-(3-oxo-1,2-oxazolidin-4-ylidene)amino]methyl}-3-pyridinyl)methyl dihydrogen phosphate. DR DrugBank; DB02038; D-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-N,O-cycloserylamide. DR DrugBank; DB02849; N-Pyridoxyl-1-Amino-Cyclopropanecarboxylic Acid-5-Monophosphate. DR DrugBank; DB04241; N-Pyridoxyl-2-Methylalanine-5-Phosphate. DR KEGG; ag:AAA50844; -. DR eggNOG; COG0160; Bacteria. DR BRENDA; 4.1.1.64; 1028. DR SABIO-RK; P16932; -. DR EvolutionaryTrace; P16932; -. DR GO; GO:0047432; F:2,2-dialkylglycine decarboxylase (pyruvate) activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:InterPro. DR CDD; cd00610; OAT_like; 1. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR049704; Aminotrans_3_PPA_site. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1. DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1. DR Pfam; PF00202; Aminotran_3; 1. DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Decarboxylase; Direct protein sequencing; Lyase; KW Pyridoxal phosphate. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2180928" FT CHAIN 2..433 FT /note="2,2-dialkylglycine decarboxylase" FT /id="PRO_0000120509" FT MOD_RES 272 FT /note="N6-(pyridoxal phosphate)lysine" FT HELIX 7..16 FT /evidence="ECO:0007829|PDB:1ZOD" FT STRAND 31..34 FT /evidence="ECO:0007829|PDB:1ZOD" FT STRAND 36..38 FT /evidence="ECO:0007829|PDB:1ZOD" FT STRAND 44..47 FT /evidence="ECO:0007829|PDB:1ZOD" FT HELIX 50..53 FT /evidence="ECO:0007829|PDB:1ZOD" FT HELIX 62..74 FT /evidence="ECO:0007829|PDB:1ZOD" FT HELIX 85..97 FT /evidence="ECO:0007829|PDB:1ZOD" FT STRAND 104..109 FT /evidence="ECO:0007829|PDB:1ZOD" FT HELIX 111..126 FT /evidence="ECO:0007829|PDB:1ZOD" FT STRAND 130..134 FT /evidence="ECO:0007829|PDB:1ZOD" FT HELIX 143..147 FT /evidence="ECO:0007829|PDB:1ZOD" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:1ZOB" FT STRAND 155..157 FT /evidence="ECO:0007829|PDB:1ZOD" FT STRAND 164..167 FT /evidence="ECO:0007829|PDB:1ZOD" FT STRAND 172..174 FT /evidence="ECO:0007829|PDB:1D7U" FT STRAND 178..183 FT /evidence="ECO:0007829|PDB:1D7U" FT HELIX 185..199 FT /evidence="ECO:0007829|PDB:1ZOD" FT STRAND 204..209 FT /evidence="ECO:0007829|PDB:1ZOD" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:1ZOD" FT TURN 214..217 FT /evidence="ECO:0007829|PDB:1ZOD" FT STRAND 218..220 FT /evidence="ECO:0007829|PDB:1D7U" FT HELIX 225..235 FT /evidence="ECO:0007829|PDB:1ZOD" FT STRAND 239..243 FT /evidence="ECO:0007829|PDB:1ZOD" FT TURN 245..252 FT /evidence="ECO:0007829|PDB:1ZOD" FT STRAND 253..256 FT /evidence="ECO:0007829|PDB:1ZOD" FT HELIX 258..261 FT /evidence="ECO:0007829|PDB:1ZOD" FT STRAND 266..270 FT /evidence="ECO:0007829|PDB:1ZOD" FT HELIX 272..275 FT /evidence="ECO:0007829|PDB:1ZOD" FT STRAND 281..285 FT /evidence="ECO:0007829|PDB:1ZOD" FT HELIX 287..295 FT /evidence="ECO:0007829|PDB:1ZOD" FT TURN 303..306 FT /evidence="ECO:0007829|PDB:1ZOD" FT HELIX 308..323 FT /evidence="ECO:0007829|PDB:1ZOD" FT HELIX 326..347 FT /evidence="ECO:0007829|PDB:1ZOD" FT STRAND 351..357 FT /evidence="ECO:0007829|PDB:1ZOD" FT STRAND 360..368 FT /evidence="ECO:0007829|PDB:1ZOD" FT TURN 369..372 FT /evidence="ECO:0007829|PDB:1ZOD" FT HELIX 378..388 FT /evidence="ECO:0007829|PDB:1ZOD" FT STRAND 395..397 FT /evidence="ECO:0007829|PDB:1M0O" FT STRAND 404..407 FT /evidence="ECO:0007829|PDB:1ZOD" FT HELIX 415..432 FT /evidence="ECO:0007829|PDB:1ZOD" SQ SEQUENCE 433 AA; 46444 MW; EF441EC8DF8C37FE CRC64; MSLNDDATFW RNARQHLVRY GGTFEPMIIE RAKGSFVYDA DGRAILDFTS GQMSAVLGHC HPEIVSVIGE YAGKLDHLFS GMLSRPVVDL ATRLANITPP GLDRALLLST GAESNEAAIR MAKLVTGKYE IVGFAQSWHG MTGAAASATY SAGRKGVGPA AVGSFAIPAP FTYRPRFERN GAYDYLAELD YAFDLIDRQS SGNLAAFIAE PILSSGGIIE LPDGYMAALK RKCEARGMLL ILDEAQTGVG RTGTMFACQR DGVTPDILTL SKTLGAGLPL AAIVTSAAIE ERAHELGYLF YTTHVSDPLP AAVGLRVLDV VQRDGLVARA NVMGDRLRRG LLDLMERFDC IGDVRGRGLL LGVEIVKDRR TKEPADGLGA KITRECMNLG LSMNIVQLPG MGGVFRIAPP LTVSEDEIDL GLSLLGQAIE RAL //