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B3PEI9 (B3PEI9_CELJU) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. 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:CJA_3291
OrganismCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa) [Complete proteome] [HAMAP] EMBL ACE84391.1
Taxonomic identifier498211 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Cellvibrio ›

Protein attributes

Sequence length415 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 RuleBase RU003738

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_02120 RuleBase RU003738 SAAS SAAS000183

Pathway

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

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

Region273 – 2764Pyridoxal phosphate binding By similarity HAMAP-Rule MF_02120

Sites

Binding site2391Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_02120
Binding site2761Substrate By similarity HAMAP-Rule MF_02120
Binding site3121Substrate By similarity HAMAP-Rule MF_02120
Binding site3161Substrate By similarity HAMAP-Rule MF_02120
Binding site3431Substrate By similarity HAMAP-Rule MF_02120
Binding site3701Pyridoxal phosphate By similarity HAMAP-Rule MF_02120
Binding site3701Substrate By similarity HAMAP-Rule MF_02120

Amino acid modifications

Modified residue601N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_02120

Sequences

Sequence LengthMass (Da)Tools
B3PEI9 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 20F19B23F0C8E0F3

FASTA41545,035
        10         20         30         40         50         60 
MQYFTERNGE LYAEDLPLRD VAERFGTPCY VYSRAAFTQQ YLSYAQALGS HPGMICYAIK 

        70         80         90        100        110        120 
ANSNLAILNM LAKLGAGFDI VSGGELERVL YAGGNPSRIV FSGVGKSVQE MARALDVGIF 

       130        140        150        160        170        180 
CFNVESEAEL ELLAQVAADK GKVANVSLRV NPDVDANTHP YISTGLKENK FGIAIERAPA 

       190        200        210        220        230        240 
VYARAAQLPS LAIKGLDCHI GSQLTQLTPF LDALERLLLL IDELAAKGIH ISHLDLGGGL 

       250        260        270        280        290        300 
GVTYRDETPP PVAEYMAAIK AKLGDRPLAL MFEPGRSISA NAGVLLTQVM FLKPTEHKNF 

       310        320        330        340        350        360 
AVIDAAMNDN IRPSLYQAWQ DIRPLQQRGQ APKTWDLVGP ICETGDFLGK GRELAIEPGD 

       370        380        390        400        410 
LLAVMSAGAY GFSMSSNYNT RGRAAEVVVD GDQMHLVRAR ETFEDLIRGE ALLPE

« Hide

References

[1]"Insights into plant cell wall degradation from the genome sequence of the soil bacterium Cellvibrio japonicus."
DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., Nelson K.E.
J. Bacteriol. 190:5455-5463(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ueda107.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000934 Genomic DNA. Translation: ACE84391.1.
RefSeqYP_001983745.1. NC_010995.1.

3D structure databases

ProteinModelPortalB3PEI9.
ModBaseSearch...

Protein-protein interaction databases

STRING498211.CJA_3291.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACE84391; ACE84391; CJA_3291.
GeneID6413501.
KEGGcja:CJA_3291.
PATRIC21329971. VBICelJap122165_3250.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0019.
HOGENOMHOG000045070.
KOK01586.
OMAGPICETS.
ProtClustDBCLSK2312795.

Enzyme and pathway databases

BioCycCJAP498211:GHIT-3280-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.
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. Racem_decarbox_C. 1 hit.
TIGRFAMsTIGR01048. lysA. 1 hit.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB3PEI9_CELJU
AccessionPrimary (citable) accession number: B3PEI9
Entry history
Integrated into UniProtKB/TrEMBL: September 2, 2008
Last sequence update: September 2, 2008
Last modified: May 29, 2013
This is version 39 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