SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P16932

- DGDA_BURCE

UniProt

P16932 - DGDA_BURCE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
2,2-dialkylglycine decarboxylase
Gene
dgdA
Organism
Burkholderia cepacia (Pseudomonas cepacia)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Pyridoxal phosphate.

GO - Molecular functioni

  1. 2,2-dialkylglycine decarboxylase (pyruvate) activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro
  3. transaminase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

SABIO-RKP16932.

Names & Taxonomyi

Protein namesi
Recommended name:
2,2-dialkylglycine decarboxylase (EC:4.1.1.64)
Short name:
DGD
Gene namesi
Name:dgdA
OrganismiBurkholderia cepacia (Pseudomonas cepacia)
Taxonomic identifieri292 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 4334322,2-dialkylglycine decarboxylase
PRO_0000120509Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei272 – 2721N6-(pyridoxal phosphate)lysine

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 1610
Beta strandi31 – 344
Beta strandi36 – 383
Beta strandi44 – 474
Helixi50 – 534
Helixi62 – 7413
Helixi85 – 9713
Beta strandi104 – 1096
Helixi111 – 12616
Beta strandi130 – 1345
Helixi143 – 1475
Beta strandi151 – 1533
Beta strandi155 – 1573
Beta strandi164 – 1674
Beta strandi172 – 1743
Beta strandi178 – 1836
Helixi185 – 19915
Beta strandi204 – 2096
Beta strandi211 – 2133
Turni214 – 2174
Beta strandi218 – 2203
Helixi225 – 23511
Beta strandi239 – 2435
Turni245 – 2528
Beta strandi253 – 2564
Helixi258 – 2614
Beta strandi266 – 2705
Helixi272 – 2754
Beta strandi281 – 2855
Helixi287 – 2959
Turni303 – 3064
Helixi308 – 32316
Helixi326 – 34722
Beta strandi351 – 3577
Beta strandi360 – 3689
Turni369 – 3724
Helixi378 – 38811
Beta strandi395 – 3973
Beta strandi404 – 4074
Helixi415 – 43218

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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-ray2.90A3-433[»]
1ZC9X-ray2.00A1-433[»]
1ZOBX-ray2.75A1-433[»]
1ZODX-ray1.80A1-433[»]
2DKBX-ray2.10A1-433[»]
ProteinModelPortaliP16932.
SMRiP16932. Positions 3-433.

Miscellaneous databases

EvolutionaryTraceiP16932.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16932-1 [UniParc]FASTAAdd to Basket

« Hide

MSLNDDATFW RNARQHLVRY GGTFEPMIIE RAKGSFVYDA DGRAILDFTS    50
GQMSAVLGHC HPEIVSVIGE YAGKLDHLFS GMLSRPVVDL ATRLANITPP 100
GLDRALLLST GAESNEAAIR MAKLVTGKYE IVGFAQSWHG MTGAAASATY 150
SAGRKGVGPA AVGSFAIPAP FTYRPRFERN GAYDYLAELD YAFDLIDRQS 200
SGNLAAFIAE PILSSGGIIE LPDGYMAALK RKCEARGMLL ILDEAQTGVG 250
RTGTMFACQR DGVTPDILTL SKTLGAGLPL AAIVTSAAIE ERAHELGYLF 300
YTTHVSDPLP AAVGLRVLDV VQRDGLVARA NVMGDRLRRG LLDLMERFDC 350
IGDVRGRGLL LGVEIVKDRR TKEPADGLGA KITRECMNLG LSMNIVQLPG 400
MGGVFRIAPP LTVSEDEIDL GLSLLGQAIE RAL 433
Length:433
Mass (Da):46,444
Last modified:January 23, 2007 - v3
Checksum:iEF441EC8DF8C37FE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05282 Genomic DNA. Translation: AAA50844.1.
PIRiA35173.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05282 Genomic DNA. Translation: AAA50844.1 .
PIRi A35173.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D7R X-ray 2.00 A 1-433 [» ]
1D7S X-ray 2.05 A 1-433 [» ]
1D7U X-ray 1.95 A 1-433 [» ]
1D7V X-ray 2.80 A 1-433 [» ]
1DGD X-ray 2.80 A 2-433 [» ]
1DGE X-ray 2.80 A 2-433 [» ]
1DKA X-ray 2.60 A 1-433 [» ]
1M0N X-ray 2.20 A 1-433 [» ]
1M0O X-ray 2.40 A 1-433 [» ]
1M0P X-ray 2.60 A 1-433 [» ]
1M0Q X-ray 2.00 A 1-433 [» ]
1Z3Z X-ray 2.90 A 3-433 [» ]
1ZC9 X-ray 2.00 A 1-433 [» ]
1ZOB X-ray 2.75 A 1-433 [» ]
1ZOD X-ray 1.80 A 1-433 [» ]
2DKB X-ray 2.10 A 1-433 [» ]
ProteinModelPortali P16932.
SMRi P16932. Positions 3-433.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P16932.

Miscellaneous databases

EvolutionaryTracei P16932.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
PANTHERi PTHR11986. PTHR11986. 1 hit.
Pfami PF00202. Aminotran_3. 1 hit.
[Graphical view ]
PIRSFi PIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
PROSITEi PS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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).

Entry informationi

Entry nameiDGDA_BURCE
AccessioniPrimary (citable) accession number: P16932
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 93 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi