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B2TA75 (B2TA75_BURPP) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Diaminopimelate decarboxylase HAMAP-Rule MF_02120

Short name=DAP decarboxylase HAMAP-Rule MF_02120
Short name=DAPDC HAMAP-Rule MF_02120
EC=4.1.1.20 HAMAP-Rule MF_02120
Gene names
Name:lysA HAMAP-Rule MF_02120
Ordered Locus Names:Bphyt_7089 EMBL ACD21377.1
OrganismBurkholderia phytofirmans (strain DSM 17436 / PsJN) [Complete proteome] [HAMAP] EMBL ACD21377.1
Taxonomic identifier398527 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine By similarity. HAMAP-Rule MF_02120

Catalytic activity

Meso-2,6-diaminoheptanedioate = L-lysine + CO2. RuleBase RU003738 HAMAP-Rule MF_02120

Cofactor

Pyridoxal phosphate By similarity. RuleBase RU003738 HAMAP-Rule MF_02120 SAAS SAAS009006

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. RuleBase RU003738 HAMAP-Rule MF_02120

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_02120

Sequence similarities

Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily. HAMAP-Rule MF_02120

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region260 – 2634Pyridoxal phosphate binding By similarity HAMAP-Rule MF_02120

Sites

Binding site2191Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_02120
Binding site2631Substrate By similarity HAMAP-Rule MF_02120
Binding site2991Substrate By similarity HAMAP-Rule MF_02120
Binding site3031Substrate By similarity HAMAP-Rule MF_02120
Binding site3341Substrate By similarity HAMAP-Rule MF_02120
Binding site3691Pyridoxal phosphate By similarity HAMAP-Rule MF_02120
Binding site3691Substrate By similarity HAMAP-Rule MF_02120

Amino acid modifications

Modified residue451N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_02120

Sequences

Sequence LengthMass (Da)Tools
B2TA75 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 9F021CE2A1EE4E53

FASTA41345,539
        10         20         30         40         50         60 
MPFNPQQLVE LAHEHGTPLW VYDADTIRRR IAELRSFDVI RYAQKACSNL HILKLMRDEG 

        70         80         90        100        110        120 
AMVDAVSLGE IKRSLAAGFK PDGDPEGVVF TADLIDHATL ATVIEHRITV NAGSLDMLEQ 

       130        140        150        160        170        180 
IGRHAPEGHR VWLRINPGFG HGHSNKTNTG GEHSKHGIWL DDVPRAVELV RRYRLKLVGL 

       190        200        210        220        230        240 
HMHIGSGVDY GHLSRVCEAM VEAVKGLGHD IEAISAGGGL SVPYREGEPD IDVAHYFRLW 

       250        260        270        280        290        300 
DAARRQIETH VGHRVRLEIE PGRFLVAQSG VLVAEVHALN RRPAQQFALL DAGFNDLVRP 

       310        320        330        340        350        360 
SFYGSHHEMT VLRRDGALSE APIDSFAVAG PLCEAGDVFT QAESGVITNR SIHTPEVGDF 

       370        380        390        400        410 
IVFHDAGAYG ASMSSNYNSR PLAPEVLLDH GKPRLIRRRQ TIDELLALEE TAA 

« Hide

References

[1]"Complete sequence of chromosome 2 of Burkholderia phytofirmans PsJN."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Nowak J., Sessitsch A., Lazarovits G., Compant S., Barka E., Tiedje J.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17436 / PsJN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001053 Genomic DNA. Translation: ACD21377.1.
RefSeqYP_001890748.1. NC_010676.1.

3D structure databases

ProteinModelPortalB2TA75.
SMRB2TA75. Positions 6-402.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING398527.Bphyt_7089.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD21377; ACD21377; Bphyt_7089.
GeneID6277930.
KEGGbpy:Bphyt_7089.
PATRIC19209169. VBIBurPhy117947_3379.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0019.
HOGENOMHOG000045070.
KOK01586.
OMAKQTYRTY.
OrthoDBEOG6Z9B18.
ProtClustDBPRK11165.

Enzyme and pathway databases

BioCycBPHY398527:GJEX-7166-MONOMER.
UniPathwayUPA00034; UER00027.

Family and domain databases

Gene3D2.40.37.10. 1 hit.
HAMAPMF_02120. LysA.
InterProIPR009006. Ala_racemase/Decarboxylase_C.
IPR002986. DAP_deCOOHase_LysA.
IPR022643. De-COase2_C.
IPR022657. De-COase2_CS.
IPR022644. De-COase2_N.
IPR022653. De-COase2_pyr-phos_BS.
IPR000183. Orn/DAP/Arg_de-COase.
[Graphical view]
PfamPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PRINTSPR01181. DAPDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMSSF50621. SSF50621. 1 hit.
TIGRFAMsTIGR01048. lysA. 1 hit.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB2TA75_BURPP
AccessionPrimary (citable) accession number: B2TA75
Entry history
Integrated into UniProtKB/TrEMBL: July 1, 2008
Last sequence update: July 1, 2008
Last modified: February 19, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)