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Q5NF56 (PAND_FRATT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 62. 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:FTT_1391
OrganismFrancisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4) [Reference proteome] [HAMAP]
Taxonomic identifier177416 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Thiotrichales › Francisellaceae › Francisella ›

Protein attributes

Sequence length111 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-Rule MF_00446

Catalytic activity

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

Cofactor

Pyruvoyl group By similarity. HAMAP-Rule MF_00446

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 HAMAP-Rule 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-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 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: 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_0000306981
Chain25 – 11187Aspartate 1-decarboxylase alpha chain By similarity
PRO_0000306982

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-Rule MF_00446

Secondary structure

1 .................... 111
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5NF56 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 22EAAAB806B751EF

FASTA11112,329
        10         20         30         40         50         60 
MLISVLKSKI SYATVTGKDL FYVGSITIDS EIMKQANIIE NEKVQVVNLN NGERLETYVI 

        70         80         90        100        110 
KGEPNSKTIA LNGPAARRCE IGDQLFIISY TQVDPTRENI KPKLVDLKTG D

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ749949 Genomic DNA. Translation: CAG46024.1.
RefSeqYP_170336.1. NC_006570.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3OUGX-ray1.55A/B/C/E/F/G/H/I1-111[»]
ProteinModelPortalQ5NF56.
ModBaseSearch...

Protein-protein interaction databases

STRING177416.FTT_1391.

Protocols and materials databases

DNASU3191388.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG46024; CAG46024; FTT_1391.
GeneID3191388.
KEGGftu:FTT_1391.

Phylogenomic databases

eggNOGCOG0853.
HOGENOMHOG000221007.
KOK01579.
OMALYSKIHR.
ProtClustDBPRK05449.

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...

Other

EvolutionaryTraceQ5NF56.

Entry information

Entry namePAND_FRATT
AccessionPrimary (citable) accession number: Q5NF56
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: February 1, 2005
Last modified: May 1, 2013
This is version 62 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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