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E3E822 (E3E822_PAEPS) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 20. 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:PPSC2_c3176 EMBL ADO57135.1
OrganismPaenibacillus polymyxa (strain SC2) (Bacillus polymyxa) [Complete proteome] [HAMAP]
Taxonomic identifier886882 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Paenibacillaceae › Paenibacillus ›

Protein attributes

Sequence length455 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 SAAS022644

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

Region290 – 2934Pyridoxal phosphate binding By similarity HAMAP-Rule MF_02120

Sites

Binding site2481Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_02120
Binding site2931Substrate By similarity HAMAP-Rule MF_02120
Binding site3301Substrate By similarity HAMAP-Rule MF_02120
Binding site3341Substrate By similarity HAMAP-Rule MF_02120
Binding site3621Substrate By similarity HAMAP-Rule MF_02120
Binding site3901Pyridoxal phosphate By similarity HAMAP-Rule MF_02120
Binding site3901Substrate By similarity HAMAP-Rule MF_02120

Amino acid modifications

Modified residue661N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_02120

Sequences

Sequence LengthMass (Da)Tools
E3E822 [UniParc].

Last modified January 11, 2011. Version 1.
Checksum: 838B6375806EED0C

FASTA45550,264
        10         20         30         40         50         60 
MYLHGSSKIN SNGHLEIGGC DTTLLKERFG TPLYIVDEQL VRRRCREFIE AFRETGLKFQ 

        70         80         90        100        110        120 
VAYASKAFCV MAMCALAAEE GMSLDVVSSG ELFTALQAGF PAERIHFHGN NKTPEEIEMA 

       130        140        150        160        170        180 
LEAQIGCFVV DSKMELHLLQ ALASEKGQQV NILLRVTPGV EAHTHEYMAT GQEDSKFGFD 

       190        200        210        220        230        240 
IANGTARQAV EQAIKLDHLN LLGVHSHIGS QIFEVNGFQM AAERVAVFCR EIKEQLQYSF 

       250        260        270        280        290        300 
KVINLGGGFG IRYTEEDTPL KLSTYVQAIG EAVKTHFSGL YDELPEIWIE PGRSIVGDSG 

       310        320        330        340        350        360 
TTLYTVGSIK DIPQVRKYVS VDGGMTDNPR PALYQAKYEA MLANRAQDAN EETVSIAGKC 

       370        380        390        400        410        420 
CESGDMLIWD VELPRPNSGD LLAVASTGAY NYSMASNYNR IRRPAVVFVN NGEAELVVRR 

       430        440        450 
ETYEDIVRND VLPQRLVRDQ ASSVVQPNAK ITVSS

« Hide

References

[1]"Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant growth-promoting Rhizobacterium with broad-spectrum antimicrobial activity."
Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F., Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.
J. Bacteriol. 193:311-312(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002213 Genomic DNA. Translation: ADO57135.1.
RefSeqYP_003947376.1. NC_014622.1.

3D structure databases

ProteinModelPortalE3E822.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADO57135; ADO57135; PPSC2_c3176.
GeneID9851474.
KEGGppm:PPSC2_c3176.
PATRIC42509522. VBIPaePol172748_3037.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000045071.
KOK01586.
OMAQGIDCHI.

Enzyme and pathway databases

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.
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.
ProtoNetSearch...

Entry information

Entry nameE3E822_PAEPS
AccessionPrimary (citable) accession number: E3E822
Entry history
Integrated into UniProtKB/TrEMBL: January 11, 2011
Last sequence update: January 11, 2011
Last modified: May 1, 2013
This is version 20 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