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A9A5S1 (PDAD_NITMS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. 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

Names and origin

Protein namesRecommended name:
Pyruvoyl-dependent arginine decarboxylase

Short name=PvlArgDC
EC=4.1.1.19
Gene names
Name:pdaD
Ordered Locus Names:Nmar_1180
OrganismNitrosopumilus maritimus (strain SCM1)
Taxonomic identifier436308 [NCBI]
Taxonomic lineageArchaeaThaumarchaeotamarine archaeal group 1NitrosopumilalesNitrosopumilaceaeNitrosopumilus

Protein attributes

Sequence length183 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
Reference 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 – 4343Pyruvoyl-dependent arginine decarboxylase subunit beta By similarity
PRO_1000145472
Chain44 – 183140Pyruvoyl-dependent arginine decarboxylase subunit alpha By similarity
PRO_1000145473

Sites

Site43 – 442Cleavage (non-hydrolytic) By similarity

Amino acid modifications

Modified residue441Pyruvic acid (Ser) By similarity

Sequences

Sequence LengthMass (Da)Tools
A9A5S1 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 0E5D71CB24A68451

FASTA18320,507
        10         20         30         40         50         60 
MLDLVAKKLF LTRGKGIHED RLTSFEYALR DAGIAGTNLV LISSIFPPKA KLISRKEGLQ 

        70         80         90        100        110        120 
QIKPGQILFT IYSKNQTNEP HRMCSASVGI AQPKDKDRYG YLSEYEAFGQ TETQAGDYAE 

       130        140        150        160        170        180 
DIAAQMLASS LGIPFDVDKN WDEKRQQWKI SGEIYKTQNI TQQTRGDKDG KWTTVFAAAV 


LLV 

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References

[1]"Complete sequence of Nitrosopumilus maritimus SCM1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Stahl D., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SCM1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000866 Genomic DNA. Translation: ABX13076.1.
RefSeqYP_001582514.1. NC_010085.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA9A5S1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5773086.
GenomeReviewsGene locus Nmar_1180 in contig CP000866_GR.
KEGGnmr:Nmar_1180.

Phylogenomic databases

HOGENOMHBG539680.
OMAYKMSGKI.

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_NITMS
AccessionPrimary (citable) accession number: A9A5S1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: January 15, 2008
Last modified: January 25, 2012
This is version 27 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