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Reviewed, UniProtKB/Swiss-Prot Q57764 (PDAD_METJA)

Last modified February 9, 2010. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Pyruvoyl-dependent arginine decarboxylase
      Short name=PvlArgDC
    EC=4.1.1.19
Cleaved into the following 2 chains:
    1- Recommended name:
            Pyruvoyl-dependent arginine decarboxylase subunit beta
    2- Recommended name:
            Pyruvoyl-dependent arginine decarboxylase subunit alpha
Gene names
Name: pdaD
Ordered Locus Names: MJ0316
OrganismMethanocaldococcus jannaschii (Methanococcus jannaschii) [Complete proteome] [HAMAP]
Taxonomic identifier2190 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus

Protein attributes

Sequence length165 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

L-arginine = agmatine + CO2. HAMAP MF_01404

Cofactor

Pyruvoyl group. HAMAP MF_01404

Subunit structure

Trimer of an alpha-beta dimer. HAMAP MF_01404

Sequence similarities

Belongs to the pdaD family.

Biophysicochemical properties

Temperature dependence:

Thermostable. HAMAP MF_01404

Mass spectrometry

Molecular mass is 5436±11 Da from positions 1 - 52. Determined by MALDI. Ref.2

Molecular mass is 12356±57 Da from positions 53 - 165. Determined by MALDI. Ref.2

Ontologies

Keywords
   LigandPyruvate
   Molecular functionDecarboxylase
Lyase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processarginine catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionarginine decarboxylase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5252Pyruvoyl-dependent arginine decarboxylase subunit beta HAMAP MF_01404
PRO_0000023314
Chain53 – 165113Pyruvoyl-dependent arginine decarboxylase subunit alpha HAMAP MF_01404
PRO_0000023315

Sites

Site52 – 532Cleavage (non-hydrolytic) HAMAP MF_01404

Amino acid modifications

Modified residue531Pyruvic acid (Ser) HAMAP MF_01404

Secondary structure

................... 165
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q57764-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 04C7F8AB3AEC2342

FASTA16517,708
        10         20         30         40         50         60 
MNAEINPLHA YFKLPNTVSL VAGSSEGETP LNAFDGALLN AGIGNVNLIR ISSIMPPEAE 

        70         80         90        100        110        120 
IVPLPKLPMG ALVPTAYGYI ISDVPGETIS AAISVAIPKD KSLCGLIMEY EGKCSKKEAE 

       130        140        150        160 
KTVREMAKIG FEMRGWELDR IESIAVEHTV EKLGCAFAAA ALWYK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77117 Genomic DNA. Translation: AAB98302.1.
PIRE64339.
RefSeqNP_247289.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MT1X-ray2.20A/C/E/G/I/K1-52[»]
B/D/F/H/J/L54-165[»]
1N13X-ray1.40A/C/E/G/I/K1-52[»]
B/D/F/H/J/L54-165[»]
1N2MX-ray1.90A/B/C/D/E/F1-165[»]
2QQCX-ray2.00A/C/E/G/I/K1-52[»]
B/D/F/H/J/L54-165[»]
2QQDX-ray2.00A/D1-52[»]
B/E54-165[»]
C/F/G/H1-165[»]
ModBaseSearch...

Genome annotation databases

GeneID1451171.
GenomeReviewsGene locus MJ0316 in contig L77117_GR.
KEGGmja:MJ0316.
NMPDRfig|243232.1.peg.326.
TIGRMJ0316.

Phylogenomic databases

HOGENOMHBG539680.
OMALVPTAYG.

Enzyme and pathway databases

BRENDA4.1.1.19. 256362.

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.
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]
TIGRFAMsTIGR00286. PvlArgDC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePDAD_METJA
AccessionPrimary (citable) accession number: Q57764
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: February 9, 2010
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents