Skip Header

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

A1WBI2 (PAND_ACISJ) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 34. 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:Ajs_3494
OrganismAcidovorax sp. (strain JS42) [Complete proteome] [HAMAP]
Taxonomic identifier232721 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

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 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_0000306917
Chain25 – 126102Aspartate 1-decarboxylase alpha chain By similarity
PRO_0000306918

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) HAMAP MF_00446

Sequences

Sequence LengthMass (Da)Tools
A1WBI2 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 6C0BC7A82DF8F01D

FASTA12614,036
        10         20         30         40         50         60 
MYRTLLKSKI HRVKTTHCEL HYEGSCAIDE DLLEAANICE NEQVHIWNVD NGERFVTYAI 

        70         80         90        100        110        120 
KGQRGSGMIS VNGSAARRAC VGDLLIIAAF AQVAEADVAA HQPQLVFVND QNRQVELRHH 


VPTQAL 

« Hide

References

[1]"Complete sequence of chromosome 1 of Acidovorax sp. JS42."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JS42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000539 Genomic DNA. Translation: ABM43607.1.
RefSeqYP_987683.1. NC_008782.1.

3D structure databases

ProteinModelPortalA1WBI2.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1WBI2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4673274.
GenomeReviewsGene locus Ajs_3494 in contig CP000539_GR.
KEGGajs:Ajs_3494.
PATRIC20692369. VBIAciSp27161_3702.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0853.
HOGENOMHBG302821.
OMAGSREINL.
PhylomeDBA1WBI2.
ProtClustDBPRK05449.

Enzyme and pathway databases

BioCycASP232721:AJS_3494-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_ACISJ
AccessionPrimary (citable) accession number: A1WBI2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 34 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