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B1JWS9 (PAND_BURCC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
Aspartate 1-decarboxylase

EC=4.1.1.11
Alternative name(s):
Aspartate alpha-decarboxylase
Gene names
Name:panD
Ordered Locus Names:Bcenmc03_2448
OrganismBurkholderia cenocepacia (strain MC0-3) [Complete proteome] [HAMAP]
Taxonomic identifier406425 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length128 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine By similarity. HAMAP MF_00446

Catalytic activity

L-aspartate = beta-alanine + CO2. HAMAP MF_00446

Cofactor

Pyruvoyl group By similarity. HAMAP MF_00446

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. HAMAP MF_00446

Subunit structure

Heterooctamer of four alpha and four beta subunits By similarity.

Subcellular location

Cytoplasm By similarity HAMAP MF_00446.

Post-translational modification

Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus By similarity. HAMAP MF_00446

Sequence similarities

Belongs to the PanD family.

Ontologies

Keywords
   Biological processPantothenate biosynthesis
   Cellular componentCytoplasm
   LigandPyruvate
Schiff base
   Molecular functionDecarboxylase
Lyase
   PTMAutocatalytic cleavage
Zymogen
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processalanine biosynthetic process

Inferred from electronic annotation. Source: InterPro

pantothenate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaspartate 1-decarboxylase activity

Inferred from electronic annotation. Source: EC

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2424Aspartate 1-decarboxylase beta chain By similarity
PRO_1000191932
Chain25 – 128104Aspartate 1-decarboxylase alpha chain By similarity
PRO_1000191933

Regions

Region73 – 753Substrate binding By similarity

Sites

Active site251Schiff-base intermediate with substrate; via pyruvic acid By similarity
Active site581Proton donor By similarity
Binding site571Substrate By similarity

Amino acid modifications

Modified residue251Pyruvic acid (Ser) By similarity

Sequences

Sequence LengthMass (Da)Tools
B1JWS9 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 5615978329BE737E

FASTA12814,297
        10         20         30         40         50         60 
MQRHMLKSKI HRAAVTHCEL HYEGSCAIDE DLLEAAGLIE NERIDIWNIN NGERFSTYAI 

        70         80         90        100        110        120 
KGERGSGMIS LNGSAARRAQ LGDLVIIAAF AMVDEAELQA GWKPKLVFID DGNKIKGHRD 


HVPTQNWT 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0-3."
Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Tiedje J., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC0-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000958 Genomic DNA. Translation: ACA91609.1.
RefSeqYP_001765731.1. NC_010508.1.

3D structure databases

ProteinModelPortalB1JWS9.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1JWS9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6124112.
GenomeReviewsGene locus Bcenmc03_2448 in contig CP000958_GR.
KEGGbcm:Bcenmc03_2448.
PATRIC19092126. VBIBurCen61509_2548.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG302821.
OMALYSKIHR.
ProtClustDBPRK05449.

Family and domain databases

HAMAPMF_00446. PanD.
[Tree]
InterProIPR009010. Asp_de-COase-like_fold.
IPR003190. Asp_decarbox.
[Graphical view]
Gene3DG3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit.
KOK01579.
PANTHERPTHR21012. Asp_decarbox. 1 hit.
PfamPF02261. Asp_decarbox. 1 hit.
[Graphical view]
PIRSFPIRSF006246. Asp_decarbox. 1 hit.
ProDomPD009294. Asp_decarbox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF50692. Asp_decarb_fold. 1 hit.
TIGRFAMsTIGR00223. PanD. 1 hit.
ProtoNetSearch...

Entry information

Entry namePAND_BURCC
AccessionPrimary (citable) accession number: B1JWS9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: January 25, 2012
This is version 30 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

SIMILARITY comments

Index of protein domains and families