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Q9PIK3 (PAND_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Aspartate 1-decarboxylase
EC=4.1.1.11
Alternative name(s):
Aspartate alpha-decarboxylase

Cleaved into the following 2 chains:

  1. Aspartate 1-decarboxylase beta chain
  2. Aspartate 1-decarboxylase alpha chain
Gene names
Name:panD
Ordered Locus Names:Cj0296c
OrganismCampylobacter jejuni
Taxonomic identifier197 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length126 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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 term3D-structure
Complete proteome
Reference 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_0000023053
Chain25 – 126102Aspartate 1-decarboxylase alpha chain By similarity
PRO_0000023054

Regions

Region72 – 743Substrate 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

Secondary structure

1 ... 126
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9PIK3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: ADC5871912B2C074

FASTA12613,974
        10         20         30         40         50         60 
MNITLLKSKI HRASVTEARL DYIGSISIDE KLLQASGILE YEKVQVVNVN NGARFETYTI 

        70         80         90        100        110        120 
ATQEEGVVCL NGAAARLAEV GDKVIIMSYA DFNEEEAKTF KPKVVFVDEN NTATKITNYE 


KHGAIF

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL111168 Genomic DNA. Translation: CAL34447.1.
PIRD81448.
RefSeqYP_002343734.1. NC_002163.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3PLXX-ray1.75A1-24[»]
B26-126[»]
ProteinModelPortalQ9PIK3.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9PIK3. 82 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID904620.
GenomeReviewsGene locus Cj0296c in contig AL111168_GR.
KEGGcje:Cj0296c.
PATRIC20057509. VBICamJej33762_0288.

Phylogenomic databases

HOGENOMHBG302821.
OMALYSKIHR.
ProtClustDBPRK05449.

Enzyme and pathway databases

BioCycCJEJ192222:CJ0296C-MONOMER.

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_CAMJE
AccessionPrimary (citable) accession number: Q9PIK3
Secondary accession number(s): Q0PBL3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 76 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

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