Skip Header

Contribute Send feedback
Read comments (?) or add your own

O67262 (DCDA_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Diaminopimelate decarboxylase
Short name=DAP decarboxylase
Short name=DAPDC
EC=4.1.1.20
Gene names
Name:lysA
Ordered Locus Names:aq_1208
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteria › Aquificae › Aquificales › Aquificaceae › Aquifex ›

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. HAMAP-Rule MF_02120

Subunit structure

Homodimer Probable. Ref.2

Sequence similarities

Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420Diaminopimelate decarboxylase HAMAP-Rule MF_02120
PRO_0000149912

Regions

Region279 – 2824Pyridoxal phosphate binding By similarity

Sites

Active site3481Proton donor Potential
Binding site2441Pyridoxal phosphate; via amide nitrogen By similarity
Binding site2821Substrate By similarity
Binding site3181Substrate By similarity
Binding site3221Substrate By similarity
Binding site3491Substrate By similarity
Binding site3771Pyridoxal phosphate By similarity
Binding site3771Substrate By similarity

Amino acid modifications

Modified residue651N6-(pyridoxal phosphate)lysine By similarity

Secondary structure

1 ............................................................................... 420
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O67262 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 4B5E922DBE5338EB

FASTA42046,966
        10         20         30         40         50         60 
MELLKEYNPY LEYRDGELFI EGVSLKELAQ TFGTPLYVYS SNFIKERFEA YRKAFPDALI 

        70         80         90        100        110        120 
CYAVKANFNP HLVKLLGELG AGADIVSGGE LYLAKKAGIP PERIVYAGVG KTEKELTDAV 

       130        140        150        160        170        180 
DSEILMFNVE SRQELDVLNE IAGKLGKKAR IAIRVNPDVD PKTHPYIATG MQKSKFGVDI 

       190        200        210        220        230        240 
REAQKEYEYA SKLENLEIVG IHCHIGSQIL DISPYREAVE KVVSLYESLT QKGFDIKYLD 

       250        260        270        280        290        300 
IGGGLGIKYK PEDKEPAPQD LADLLKDLLE NVKAKIILEP GRSIMGNAGI LITQVQFLKD 

       310        320        330        340        350        360 
KGSKHFIIVD AGMNDLIRPS IYNAYHHIIP VETKERKKVV ADIVGPICET GDFLALDREI 

       370        380        390        400        410        420 
EEVQRGEYLA VLSAGAYGFA MSSHYNMRPR AAEVLVENGS VKLIRKRENY DYIVEPSLDI

« Hide

References

« Hide 'large scale' references
[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
[2]Southeast collaboratory for structural genomics (SECSG)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000657 Genomic DNA. Translation: AAC07209.1.
PIRC70404.
RefSeqNP_213826.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2P3EX-ray1.99A/B1-420[»]
ProteinModelPortalO67262.
SMRO67262. Positions 2-420.
ModBaseSearch...

Protein-protein interaction databases

STRING224324.aq_1208.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC07209; AAC07209; aq_1208.
GeneID1192608.
KEGGaae:aq_1208.
PATRIC20959642. VBIAquAeo85532_0940.

Phylogenomic databases

eggNOGCOG0019.
HOGENOMHOG000045070.
KOK01586.
OMAGPICETS.
ProtClustDBCLSK2299618.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-862-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.
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.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO67262.

Entry information

Entry nameDCDA_AQUAE
AccessionPrimary (citable) accession number: O67262
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents