Skip Header

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

B3EGI2 (PDAD_CHLL2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 22. 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:Clim_0527
OrganismChlorobium limicola (strain DSM 245 / NBRC 103803) [Complete proteome] [HAMAP]
Taxonomic identifier290315 [NCBI]
Taxonomic lineageBacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobium/Pelodictyon group › Chlorobium

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_1000145460
Chain43 – 181139Pyruvoyl-dependent arginine decarboxylase subunit alpha By similarity
PRO_1000145461

Sites

Site42 – 432Cleavage (non-hydrolytic) By similarity

Amino acid modifications

Modified residue431Pyruvic acid (Ser) By similarity

Sequences

Sequence LengthMass (Da)Tools
B3EGI2 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: A1AA45394E641B7E

FASTA18120,014
        10         20         30         40         50         60 
MSFVPTKVFF TKGVGRHKEY LSSFELALRD AKIEKCNLVT VSSIFPPKCE RISVEEGLKL 

        70         80         90        100        110        120 
LSPGQITFAV MARNATNEYN RLISASVGVA IPADDTQYGY LSEHHPYGES DEQCGEYAED 

       130        140        150        160        170        180 
LAATMLATTL GIEFDPNKDW DEREGIYKMS GKIINSYNIT QSAEGENGLW TTVISCAVLL 


P

« Hide

References

[1]"Complete sequence of Chlorobium limicola DSM 245."
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., Ovchinnikova G., Zhao F., Li T., Liu Z. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 245 / NBRC 103803.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001097 Genomic DNA. Translation: ACD89619.1.
RefSeqYP_001942598.1. NC_010803.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB3EGI2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6354878.
GenomeReviewsGene locus Clim_0527 in contig CP001097_GR.
KEGGcli:Clim_0527.
PATRIC21373051. VBIChlLim118737_0568.

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_CHLL2
AccessionPrimary (citable) accession number: B3EGI2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 22, 2008
Last modified: January 25, 2012
This is version 22 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