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D8MEX2 (D8MEX2_LEUGT) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 23. 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:LEGAS_0742
OrganismLeuconostoc gasicomitatum (strain DSM 15947 / CECT 5767 / JCM 12535 / LMG 18811 / TB1-10) [Complete proteome] [HAMAP] EMBL CBL91390.1
Taxonomic identifier762550 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Leuconostoc ›

Protein attributes

Sequence length431 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

Region282 – 2854Pyridoxal phosphate binding By similarity HAMAP-Rule MF_02120

Sites

Binding site2401Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_02120
Binding site2851Substrate By similarity HAMAP-Rule MF_02120
Binding site3221Substrate By similarity HAMAP-Rule MF_02120
Binding site3261Substrate By similarity HAMAP-Rule MF_02120
Binding site3541Substrate By similarity HAMAP-Rule MF_02120
Binding site3821Pyridoxal phosphate By similarity HAMAP-Rule MF_02120
Binding site3821Substrate By similarity HAMAP-Rule MF_02120

Amino acid modifications

Modified residue621N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_02120

Sequences

Sequence LengthMass (Da)Tools
D8MEX2 [UniParc].

Last modified October 5, 2010. Version 1.
Checksum: 89E244ECBAB4CD14

FASTA43147,424
        10         20         30         40         50         60 
MSYPINTAQH LTIGEVDAID LAKTYGTPLY VYDVTKIRQT MRDFKAIFEK EDVPYVVSYA 

        70         80         90        100        110        120 
SKAFASKAIY QVAQQEGIHA DIVSGGELYT ALAAGFDPKH LSFNGNNKSW DELTMAVTEG 

       130        140        150        160        170        180 
VGTIIVDNFL ELQLLSEITT QNGVKQDILL RISPGISAHT HEFISTGQQD SKFGFDLLTG 

       190        200        210        220        230        240 
QAKTAYDIAR QNENFNLRGL HAHIGSQIFD VTGFEKNAAL LAETAKSWGF QPEVINVGGG 

       250        260        270        280        290        300 
FGIRYTSEDE PLPESEYADA IIRTLKSKAA EYDWKMPEIW IEPGRSIVGP AGQTLYTIGS 

       310        320        330        340        350        360 
RKDIPDLRHY LAVDGGMGDN IRPALYQANY DAILANNPNA STQEVVRVAG KYCESGDVLV 

       370        380        390        400        410        420 
WQQALPKTKP GDILSVLATG AYGYAMASNY NRNPRPAVVF VENGKHQVVI ARESYAHLIA 

       430 
LDHDYMLKNG K

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References

[1]"Genome sequence and comparative genomics of a food spoilage lactic acid bacterium Leuconostoc gasicomitatum 18811T."
Johansson P., Paulin L., Vihavainen E.J., Salovuori N., Alatalo E.R., Bjoerkroth J.K., Auvinen P.
Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 15947 / CECT 5767 / JCM 12535 / LMG 18811 / TB1-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FN822744 Genomic DNA. Translation: CBL91390.1.
RefSeqYP_003772209.1. NC_014319.1.

3D structure databases

ProteinModelPortalD8MEX2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCBL91390; CBL91390; LEGAS_0742.
GeneID9398407.
KEGGlgs:LEGAS_0742.
PATRIC42383148. VBILeuGas160647_0754.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000045071.
KOK01586.
OMAHPKISTG.

Enzyme and pathway databases

BioCycLGAS762550:GHH1-1439-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.
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.
PROSITEPS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD8MEX2_LEUGT
AccessionPrimary (citable) accession number: D8MEX2
Entry history
Integrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: May 1, 2013
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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