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Q5P5N4 (Q5P5N4_AROAE) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 63. 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 CAI07378.1
Ordered Locus Names:AZOSEA12530
ORF Names:ebA2271 EMBL CAI07378.1
OrganismAromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Aromatoleum ›

Protein attributes

Sequence length420 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

Region279 – 2824Pyridoxal phosphate binding By similarity HAMAP-Rule MF_02120

Sites

Binding site2451Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_02120
Binding site2821Substrate By similarity HAMAP-Rule MF_02120
Binding site3181Substrate By similarity HAMAP-Rule MF_02120
Binding site3221Substrate By similarity HAMAP-Rule MF_02120
Binding site3491Substrate By similarity HAMAP-Rule MF_02120
Binding site3761Pyridoxal phosphate By similarity HAMAP-Rule MF_02120
Binding site3761Substrate 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
Q5P5N4 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: C1A2AEE9599D5C1F

FASTA42044,496
        10         20         30         40         50         60 
MNSDFPIPTL RPGSAGLQIE DVPLAAIAER FGTPTYVYSR AALEQAFDAY RDALAGRRAL 

        70         80         90        100        110        120 
VCYAVKANSN LGVLAVFAKL GAGFDIVSGG ELSRVLAAGG DPGKVVFSGV GKSAGEMRQA 

       130        140        150        160        170        180 
LAAGIRCFNV ESEAELERLD MLAGELGTRA PIALRVNPDV DPKTHPYIST GLKNNKFGVA 

       190        200        210        220        230        240 
FDTALALYRR AAGMANVRIS GIACHIGSQL LDSGPIAEAA EKVLGLVDEL AAEGIHLDHI 

       250        260        270        280        290        300 
DLGGGLGIRY RDEAPPSVAA YLAPLLRLLD GRSEELCFEP GRSLIGNAGL LLTRIEYLKP 

       310        320        330        340        350        360 
GAERNFAIVD AAMNDLARPA LYDAYHEAVA VAPRDVPERN YEIVGPICES GDFLAHDRPL 

       370        380        390        400        410        420 
AVAAGDLVAL LSAGAYGMAM SSNYNTRPRA AEVIVDGSRM HLVRQRETVE SLYALESPLP

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References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EbN1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR555306 Genomic DNA. Translation: CAI07378.1.
RefSeqYP_158279.1. NC_006513.1.

3D structure databases

ProteinModelPortalQ5P5N4.
ModBaseSearch...

Protein-protein interaction databases

STRING76114.ebA2271.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI07378; CAI07378; ebA2271.
GeneID3182595.
KEGGeba:ebA2271.
PATRIC20968621. VBIAroAro98752_1271.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0019.
HOGENOMHOG000045070.
KOK01586.
OMAGPICETS.
ProtClustDBCLSK766520.

Enzyme and pathway databases

BioCycAARO76114:GJTA-1272-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 nameQ5P5N4_AROAE
AccessionPrimary (citable) accession number: Q5P5N4
Entry history
Integrated into UniProtKB/TrEMBL: January 4, 2005
Last sequence update: January 4, 2005
Last modified: May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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