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B0UCU0 (B0UCU0_METS4) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 40. 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:M446_4848 EMBL ACA19177.1
OrganismMethylobacterium sp. (strain 4-46) [Complete proteome] [HAMAP] EMBL ACA19177.1
Taxonomic identifier426117 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Methylobacteriaceae › Methylobacterium

Protein attributes

Sequence length423 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

Region275 – 2784Pyridoxal phosphate binding By similarity HAMAP-Rule MF_02120

Sites

Binding site2391Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_02120
Binding site2781Substrate By similarity HAMAP-Rule MF_02120
Binding site3141Substrate By similarity HAMAP-Rule MF_02120
Binding site3181Substrate By similarity HAMAP-Rule MF_02120
Binding site3471Substrate By similarity HAMAP-Rule MF_02120
Binding site3751Pyridoxal phosphate By similarity HAMAP-Rule MF_02120
Binding site3751Substrate 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
B0UCU0 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 6812F7DFC193EFF2

FASTA42345,176
        10         20         30         40         50         60 
MHHFTYRDGT LHAEEVDLAR LAEAVGTPFY CYASATLERH FRVFAEAFAG DDPLVCFAVK 

        70         80         90        100        110        120 
ANSNQAVLAS LARLGAGMDI VSEGELRRAL AAGVPGERIV FSGVAKTRAE MAVALDAGIL 

       130        140        150        160        170        180 
CFNVESEPEL EALSEVARAR GQTAPVSIRV NPDVDARTHA KISTGKSENK FGIPISRARE 

       190        200        210        220        230        240 
VYARAAALPG LAVAGVDMHI GSQITDLAPY DNAASLLAEL ARDLMAAGHR LHHIDFGGGL 

       250        260        270        280        290        300 
GIPYRDDNAP PPDPAAFAAV IRPHFRPLGL RPVFEIGRMI AGNAGILVTR VVYVKEGEGR 

       310        320        330        340        350        360 
SFVIVDAGMN DLIRPTLYEA YHALRPVRQP DPEAPRLTAD VVGPVCESGD YLALGREMPA 

       370        380        390        400        410        420 
VAPGDLLAVM SAGAYGAVQA GTYNTRRLVP EVLVRGAAHA VVRPRQSYEE LIGLDRVPDW 


LAP

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References

[1]"Complete sequence of chromosome of Methylobacterium sp. 4-46."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Ivanova N., Marx C.J., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 4-46 EMBL ACA19177.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000943 Genomic DNA. Translation: ACA19177.1.
RefSeqYP_001771611.1. NC_010511.1.

3D structure databases

ProteinModelPortalB0UCU0.
ModBaseSearch...

Protein-protein interaction databases

STRING426117.M446_4848.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA19177; ACA19177; M446_4848.
GeneID6131665.
KEGGmet:M446_4848.
PATRIC22590882. VBIMetSp32184_4763.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0019.
HOGENOMHOG000045070.
KOK01586.
OMAGPICETS.
ProtClustDBCLSK2330848.

Enzyme and pathway databases

BioCycMSP426117:GI2I-4901-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 nameB0UCU0_METS4
AccessionPrimary (citable) accession number: B0UCU0
Entry history
Integrated into UniProtKB/TrEMBL: April 8, 2008
Last sequence update: April 8, 2008
Last modified: May 1, 2013
This is version 40 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