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A4SFG2 (PDAD_PROVI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 42. 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

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-Rule MF_01404

Cofactor

Pyruvoyl group By similarity. HAMAP-Rule 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: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4242Pyruvoyl-dependent arginine decarboxylase subunit beta By similarity
PRO_1000087373
Chain43 – 181139Pyruvoyl-dependent arginine decarboxylase subunit alpha By similarity
PRO_1000087374

Sites

Site42 – 432Cleavage (non-hydrolytic) By similarity

Amino acid modifications

Modified residue431Pyruvic acid (Ser) By similarity

Sequences

Sequence LengthMass (Da)Tools
A4SFG2 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 6B2A4FB6EA6A6CD0

FASTA18120,070
        10         20         30         40         50         60 
MSFVPTKVFF TKGVGRHKEY LSSFELALRD AKIEKCNLVT VSSIFPPKCE RISVEEGIKL 

        70         80         90        100        110        120 
LTPGQITFAV MARNSTNEYN RLMAASIGVA IPADDTQYGY LSEHHPFGED EEQSGEYAED 

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


P 

« Hide

References

[1]"Complete sequence of Prosthecochloris vibrioformis DSM 265."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J., Schuster S.C., Bryant D.A., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 265.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000607 Genomic DNA. Translation: ABP37221.1.
RefSeqYP_001130723.1. NC_009337.1.

3D structure databases

ProteinModelPortalA4SFG2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290318.Cvib_1209.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP37221; ABP37221; Cvib_1209.
GeneID4970178.
KEGGpvi:Cvib_1209.
PATRIC21396890. VBIChlPha132153_1275.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1945.
HOGENOMHOG000012204.
KOK02626.
OMASEHHSFG.
OrthoDBEOG6JHRMR.
ProtClustDBPRK01285.

Enzyme and pathway databases

BioCycCPHA290318:GHNQ-1243-MONOMER.

Family and domain databases

Gene3D3.50.20.10. 1 hit.
HAMAPMF_01404. PvlArgDC.
InterProIPR016104. Pyr-dep_his/arg-deCO2ase.
IPR016105. Pyr-dep_his/arg-deCO2ase_sand.
IPR002724. Pyruvoyl-dep_arg_deCO2ase.
[Graphical view]
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. SSF56271. 1 hit.
TIGRFAMsTIGR00286. TIGR00286. 1 hit.
ProtoNetSearch...

Entry information

Entry namePDAD_PROVI
AccessionPrimary (citable) accession number: A4SFG2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 15, 2007
Last modified: February 19, 2014
This is version 42 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