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B8DWQ9 (B8DWQ9_BIFA0) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 29. 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 EMBL ACL28910.1
Ordered Locus Names:BLA_0617
OrganismBifidobacterium animalis subsp. lactis (strain AD011) [Complete proteome] [HAMAP] EMBL ACL28910.1
Taxonomic identifier442563 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium ›

Protein attributes

Sequence length529 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. HAMAP-Rule MF_02120

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_02120

Pathway

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

Region372 – 3754Pyridoxal phosphate binding By similarity HAMAP-Rule MF_02120

Sites

Binding site3301Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_02120
Binding site3751Substrate By similarity HAMAP-Rule MF_02120
Binding site4251Substrate By similarity HAMAP-Rule MF_02120
Binding site4291Substrate By similarity HAMAP-Rule MF_02120
Binding site4571Substrate By similarity HAMAP-Rule MF_02120
Binding site4861Pyridoxal phosphate By similarity HAMAP-Rule MF_02120
Binding site4861Substrate By similarity HAMAP-Rule MF_02120

Amino acid modifications

Modified residue721N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_02120

Sequences

Sequence LengthMass (Da)Tools
B8DWQ9 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: DF015C5601DA58D9

FASTA52957,114
        10         20         30         40         50         60 
MAISPIWPAD TARNSNGELT FHGITASTLL DEFGSPLYVL DLDEVRARAS HFVKAAAHAF 

        70         80         90        100        110        120 
TNNTTHVSYA AKAFLSKEMA RIVTEEGMFV DTCTLGEMKI ALAAGVPGRR LVLHGNNKSD 

       130        140        150        160        170        180 
EEIELAIAEG FSKIVIDSPD EPARIAAIAE RLGKRARVML RVTSGIHAGG HEYVSTAHED 

       190        200        210        220        230        240 
QKFGVALLPA GADTEIVDNI DQLQDVSPAA TNALVHETEL ERGGETKQQA DRQLRYDVRY 

       250        260        270        280        290        300 
PYDLNAADVT EGDRLLAAAM ELVANGPAIA VLREIAKYGN LELVGVHSHI GSNIHDAEAF 

       310        320        330        340        350        360 
IQAAKRMMLL RKTFYATNAY TLPEVDLGGG YSVAYTDDED RMDVDRELGR LADAVSKTNR 

       370        380        390        400        410        420 
LLGMPAPIIS FEPGRWIVAP AGVTLYRVGT VKTVQLGDGF TNNAGERIRE RAYISVDGGM 

       430        440        450        460        470        480 
SDNIRPALYD AKYTAILANR ESAEPAKLSR VVGIHCESGD IVVNEANLPA DVHRGDILAV 

       490        500        510        520 
PVTGAYGRSM ASNYNMALIP AVVGIDGHGA HVMMRRQTID DLLALDVSE

« Hide

References

[1]"Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp. lactis AD011."
Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., Yoon S.H., Kim D.-W., Ji G.E., Park H.-S., Oh T.K.
J. Bacteriol. 191:678-679(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AD011.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001213 Genomic DNA. Translation: ACL28910.1.
RefSeqYP_002469486.1. NC_011835.1.

3D structure databases

ProteinModelPortalB8DWQ9.
ModBaseSearch...

Protein-protein interaction databases

STRING442563.BLA_0617.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL28910; ACL28910; BLA_0617.
GeneID7264024.
KEGGbla:BLA_0617.
PATRIC21104119. VBIBifAni98964_0648.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0019.
HOGENOMHOG000045071.
KOK01586.
OMAHPKISTG.
ProtClustDBCLSK572987.

Enzyme and pathway databases

BioCycBANI442563:GHG0-612-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.
[Graphical view]
PfamPF02784. Orn_Arg_deC_N. 2 hits.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
SUPFAMSSF50621. Racem_decarbox_C. 1 hit.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB8DWQ9_BIFA0
AccessionPrimary (citable) accession number: B8DWQ9
Entry history
Integrated into UniProtKB/TrEMBL: March 3, 2009
Last sequence update: March 3, 2009
Last modified: May 1, 2013
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info