Skip Header

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

B4S6J7 (PDAD_PROA2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable pyruvoyl-dependent arginine decarboxylase
Short name=PvlArgDC
EC=4.1.1.19

Cleaved into the following 2 chains:

  1. Pyruvoyl-dependent arginine decarboxylase subunit beta
  2. Pyruvoyl-dependent arginine decarboxylase subunit alpha
Gene names
Name:pdaD
Ordered Locus Names:Paes_0705
OrganismProsthecochloris aestuarii (strain DSM 271 / SK 413) [Complete proteome] [HAMAP]
Taxonomic identifier290512 [NCBI]
Taxonomic lineageBacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Prosthecochloris

Protein attributes

Sequence length181 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

L-arginine = agmatine + CO2. HAMAP MF_01404

Cofactor

Pyruvoyl group By similarity. HAMAP MF_01404

Sequence similarities

Belongs to the pdaD family.

Ontologies

Keywords
   LigandPyruvate
   Molecular functionDecarboxylase
Lyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginine catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionarginine decarboxylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4242Pyruvoyl-dependent arginine decarboxylase subunit beta By similarity
PRO_1000145474
Chain43 – 181139Pyruvoyl-dependent arginine decarboxylase subunit alpha By similarity
PRO_1000145475

Sites

Site42 – 432Cleavage (non-hydrolytic) By similarity

Amino acid modifications

Modified residue431Pyruvic acid (Ser) By similarity

Sequences

Sequence LengthMass (Da)Tools
B4S6J7 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 968B05A7649D11F7

FASTA18119,898
        10         20         30         40         50         60 
MSFVPTKVFF TKGVGRHKEY LSSFELALRE AKIEKCNLVT VSSIFPPQCE RISVEEGLKS 

        70         80         90        100        110        120 
LSPGEITFAV MARNSTNEHG RLIASSIGVA LPADESVYGY LSEHHPYGQT EEQSGEYAED 

       130        140        150        160        170        180 
LAATMLATTL GIEFDPNKDW DEREGIYKMS GKIINSFNIT QSAEGQNGLW TTVIACAVLL 


P

« Hide

References

[1]"Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 271 / SK 413.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001108 Genomic DNA. Translation: ACF45752.1.
RefSeqYP_002015399.1. NC_011059.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB4S6J7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6458504.
GenomeReviewsGene locus Paes_0705 in contig CP001108_GR.
KEGGpaa:Paes_0705.
PATRIC23041096. VBIProAes37017_0736.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG539680.
OMAYKMSGKI.
ProtClustDBPRK01285.

Family and domain databases

HAMAPMF_01404. PvlArgDC.
[Tree]
InterProIPR016104. Pyr-dep_his/arg-deCO2ase.
IPR016105. Pyr-dep_his/arg-deCO2ase_sand.
IPR002724. Pyruvoyl-dep_arg_deCO2ase.
[Graphical view]
Gene3DG3DSA:3.50.20.10. Pyr-dep_his/arg-deCO2ase_sand. 1 hit.
KOK02626.
PfamPF01862. PvlArgDC. 1 hit.
[Graphical view]
PIRSFPIRSF005216. Pyruvoyl-dep_arg_deCO2ase. 1 hit.
ProDomPD010449. Pyruvoyl-dep_arg_deCO2ase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF56271. His_carbxylase. 1 hit.
TIGRFAMsTIGR00286. TIGR00286. 1 hit.
ProtoNetSearch...

Entry information

Entry namePDAD_PROA2
AccessionPrimary (citable) accession number: B4S6J7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: January 25, 2012
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents