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P16932 (DGDA_BURCE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2,2-dialkylglycine decarboxylase
Short name=DGD
EC=4.1.1.64
Gene names
Name:dgdA
OrganismBurkholderia cepacia (Pseudomonas cepacia)
Taxonomic identifier292 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

Protein attributes

Sequence length433 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The dialkylglycine decarboxylase is of interest because it normally catalyzes both decarboxylation and amino transfer. It may be more properly described as a decarboxylating aminotransferase rather than an aminotransferring decarboxylase.

Catalytic activity

2,2-dialkylglycine + pyruvate = dialkyl ketone + CO2 + L-alanine.

Cofactor

Pyridoxal phosphate.

Subunit structure

Homotetramer.

Miscellaneous

The enzyme may have evolved to use the rare dialkylglycines of cosmic origin, or it may be part of a metabolic pathway for breaking down cytotoxic peptides and the constituent amino acids.

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 4334322,2-dialkylglycine decarboxylase
PRO_0000120509

Amino acid modifications

Modified residue2721N6-(pyridoxal phosphate)lysine

Secondary structure

1 ............................................................................. 433
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16932 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: EF441EC8DF8C37FE

FASTA43346,444
        10         20         30         40         50         60 
MSLNDDATFW RNARQHLVRY GGTFEPMIIE RAKGSFVYDA DGRAILDFTS GQMSAVLGHC 

        70         80         90        100        110        120 
HPEIVSVIGE YAGKLDHLFS GMLSRPVVDL ATRLANITPP GLDRALLLST GAESNEAAIR 

       130        140        150        160        170        180 
MAKLVTGKYE IVGFAQSWHG MTGAAASATY SAGRKGVGPA AVGSFAIPAP FTYRPRFERN 

       190        200        210        220        230        240 
GAYDYLAELD YAFDLIDRQS SGNLAAFIAE PILSSGGIIE LPDGYMAALK RKCEARGMLL 

       250        260        270        280        290        300 
ILDEAQTGVG RTGTMFACQR DGVTPDILTL SKTLGAGLPL AAIVTSAAIE ERAHELGYLF 

       310        320        330        340        350        360 
YTTHVSDPLP AAVGLRVLDV VQRDGLVARA NVMGDRLRRG LLDLMERFDC IGDVRGRGLL 

       370        380        390        400        410        420 
LGVEIVKDRR TKEPADGLGA KITRECMNLG LSMNIVQLPG MGGVFRIAPP LTVSEDEIDL 

       430 
GLSLLGQAIE RAL

« Hide

References

[1]"Pseudomonas cepacia 2,2-dialkylglycine decarboxylase. Sequence and expression in Escherichia coli of structural and repressor genes."
Keller J.W., Baurick K.B., Rutt G.C., O'Malley M.V., Sonafrank N.L., Reynolds R.A., Ebbesson L.O.E., Vajdos F.F.
J. Biol. Chem. 265:5531-5539(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20 AND 261-276.
[2]"Dialkylglycine decarboxylase structure: bifunctional active site and alkali metal sites."
Toney M.D., Hohenester E., Cowan S.W., Jansonius J.N.
Science 261:756-759(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[3]"An alkali metal ion size-dependent switch in the active site structure of dialkylglycine decarboxylase."
Hohenester E., Keller J.W., Jansonius J.N.
Biochemistry 33:13561-13570(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SEQUENCE REVISION TO 52; 82-83 AND 308-312.
[4]"Structural and mechanistic analysis of two refined crystal structures of the pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase."
Toney M.D., Hohenester E., Keller J.W., Jansonius J.N.
J. Mol. Biol. 245:151-179(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[5]"Crystal structures of dialkylglycine decarboxylase inhibitor complexes."
Malashkevich V.N., Strop P., Keller J.W., Jansonius J.N., Toney M.D.
J. Mol. Biol. 294:193-200(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J05282 Genomic DNA. Translation: AAA50844.1.
PIRA35173.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D7RX-ray2.00A1-433[»]
1D7SX-ray2.05A1-433[»]
1D7UX-ray1.95A1-433[»]
1D7VX-ray2.80A1-433[»]
1DGDX-ray2.80A2-433[»]
1DGEX-ray2.80A2-433[»]
1DKAX-ray2.60A1-433[»]
1M0NX-ray2.20A1-433[»]
1M0OX-ray2.40A1-433[»]
1M0PX-ray2.60A1-433[»]
1M0QX-ray2.00A1-433[»]
1Z3ZX-ray2.90A3-432[»]
1ZC9X-ray2.00A1-432[»]
1ZOBX-ray2.75A1-432[»]
1ZODX-ray1.80A1-432[»]
2DKBX-ray2.10A1-433[»]
ProteinModelPortalP16932.
SMRP16932. Positions 3-433.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP16932.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16932.

Entry information

Entry nameDGDA_BURCE
AccessionPrimary (citable) accession number: P16932
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 90 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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