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D9QRQ2 (D9QRQ2_ACEAZ) 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:Acear_1688
OrganismAcetohalobium arabaticum (strain ATCC 49924 / DSM 5501 / Z-7288) [Complete proteome] [HAMAP] EMBL ADL13193.1
Taxonomic identifier574087 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Halanaerobiales › Halobacteroidaceae › Acetohalobium ›

Protein attributes

Sequence length437 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
D9QRQ2 [UniParc].

Last modified October 5, 2010. Version 1.
Checksum: 6A28CD7D7745FD3A

FASTA43748,309
        10         20         30         40         50         60 
MVLHGTMEVN EKGNLEVGGC DVTNIATEYG TPLYILDEEE LRDNCRAYRQ AFEEWYPNSE 

        70         80         90        100        110        120 
TIYASKAFMS LTICKIVEEE GLGLDVVSGG ELYTALEADF PTDKIYFHGN NKTPEELEMV 

       130        140        150        160        170        180 
LNEEIGRIVV DNNYELELLN ELADQQGKRA DILIRVTPGV EAHTHSYIQT GQTDSKFGVG 

       190        200        210        220        230        240 
IQNGLALETV KKAVELENID VKGIHCHIGS QIFNLESFEV AVDVMLDFVE EVKIETGLVM 

       250        260        270        280        290        300 
EELNIGGGIG IKYTDKDQSV SIDQYAELVA KAIKQKCEEI NIPLPKIINE PGRSIIGTAG 

       310        320        330        340        350        360 
STIYTVGSIK NIPDVRKYVA VDGGMPDNIR PALYEAEYEA IVANKANRKP EEVVSITGKC 

       370        380        390        400        410        420 
CESGDMLIWD IELPEMEPGD VLLTPCTGAY GYAMANNYNS LPKPGVVLIN NGQVEEIIRG 

       430 
ERYEDLVAKE EIPARLK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002105 Genomic DNA. Translation: ADL13193.1.
RefSeqYP_003828258.1. NC_014378.1.

3D structure databases

ProteinModelPortalD9QRQ2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADL13193; ADL13193; Acear_1688.
GeneID9513745.
KEGGaar:Acear_1688.
PATRIC42137625. VBIAceAra30843_1724.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000045071.
KOK01586.

Enzyme and pathway databases

BioCycAARA574087:GHPK-1769-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 nameD9QRQ2_ACEAZ
AccessionPrimary (citable) accession number: D9QRQ2
Entry history
Integrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
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