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C4L931 (PAND_TOLAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 28. 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:Tola_2304
OrganismTolumonas auensis (strain DSM 9187 / TA4) [Complete proteome] [HAMAP]
Taxonomic identifier595494 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeTolumonas

Protein attributes

Sequence length126 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-Rule MF_00446

Catalytic activity

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

Cofactor

Pyruvoyl group By similarity.

Pathway

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

Subunit structure

Heterooctamer of four alpha and four beta subunits By similarity.

Subcellular location

Cytoplasm By similarity.

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-Rule 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: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaspartate 1-decarboxylase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2424Aspartate 1-decarboxylase beta chain By similarity
PRO_1000206196
Chain25 – 126102Aspartate 1-decarboxylase alpha chain By similarity
PRO_1000206197

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
C4L931 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: AD90287D1E5C0B19

FASTA12613,954
        10         20         30         40         50         60 
MQRIMLRGKL HQARVTHAVL NYEGSCGIDQ DFLDAAGIVE YEAIDIYNIE NGERFSTYAI 

        70         80         90        100        110        120 
SGERGSRMIS LNGAAARKAA VGDRIIICAY GPMTEDEVAQ HKPRLVYLDA QNNIVRTSKD 


IPLQLA 

« Hide

References

[1]"Complete sequence of Tolumonas auensis DSM 9187."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S., Beller H.
Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 9187 / TA4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001616 Genomic DNA. Translation: ACQ93901.1.
RefSeqYP_002893487.1. NC_012691.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING595494.Tola_2304.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACQ93901; ACQ93901; Tola_2304.
GeneID7886071.
KEGGtau:Tola_2304.
PATRIC23981251. VBITolAue42623_2285.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0853.
HOGENOMHOG000221007.
KOK01579.
ProtClustDBCLSK2504861.

Enzyme and pathway databases

UniPathwayUPA00028; UER00002.

Family and domain databases

Gene3D2.40.40.20. 1 hit.
HAMAPMF_00446. PanD.
InterProIPR009010. Asp_de-COase-like_dom.
IPR003190. Asp_decarbox.
[Graphical view]
PANTHERPTHR21012. PTHR21012. 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_TOLAT
AccessionPrimary (citable) accession number: C4L931
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 7, 2009
Last modified: May 1, 2013
This is version 28 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