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P41142 (ARCA_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Arginine deiminase
Short name=ADI
EC=3.5.3.6
Alternative name(s):
Arginine dihydrolase
Short name=AD
Gene names
Name:arcA
OrganismPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas ›

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-arginine + H2O = L-citrulline + NH3. HAMAP-Rule MF_00242

Enzyme regulation

Activated by Mg2+ or Mn2+ and strongly inhibited by Zn2+ By similarity. HAMAP-Rule MF_00242

Pathway

Amino-acid degradation; L-arginine degradation via ADI pathway; carbamoyl phosphate from L-arginine: step 1/2. HAMAP-Rule MF_00242

Subunit structure

Homodimer.

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00242.

Sequence similarities

Belongs to the arginine deiminase family.

Ontologies

Keywords
   Biological processArginine metabolism
   Cellular componentCytoplasm
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological_processarginine catabolic process to ornithine

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionarginine deiminase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420Arginine deiminase HAMAP-Rule MF_00242
PRO_0000182227

Sites

Active site4081Amidino-cysteine intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
P41142 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 4EE3BF5DD504AF2F

FASTA42046,620
        10         20         30         40         50         60 
MSAEKQKYGV HSEAGKLRKV MVCSPGLAHK RLTPSNCDEL LFDDVIWVDQ AKRDHFDFVT 

        70         80         90        100        110        120 
KMRERGVDVL EMHNLLTDIV QQPEALKWIL DRKITSDTVG VGLTNEVRSW LEGLEPRHLA 

       130        140        150        160        170        180 
EFLIGGVAGQ DLPVSEGAEV IKMYNKYLGH SSFILPPLPN TQFTRDTTCW IYGGVTLNPM 

       190        200        210        220        230        240 
YWPARRQETL LTTAIYKFHK EFTGADFQVW YGDPDKDHGN ATLEGGDVMP VGKGIVLIGM 

       250        260        270        280        290        300 
GERTSRHAIG QLAQNLFEKG AAEKIIVAGL PKSRAAMHLD TVFSFCDRDL VTVFPEVVKE 

       310        320        330        340        350        360 
IKPFIITPDS SKPYGMNIAP QDASFLEVVS EQLLGKKDKL RVVETGGNSF AAEREQWDDG 

       370        380        390        400        410        420 
NNVVALEPGV VIGYDRNTYT NTLLRKAGIE VITISAGELG RGRGGGHCMT CPIVRDPIDY

« Hide

References

[1]Wilson S.D., Wang M., Filpula D.
Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 4359 / IAM 1506 / JCM 20188.
[2]"Crystallization and properties of L-arginine deiminase of Pseudomonas putida."
Shibatani T., Kakimoto T., Chibat I.
J. Biol. Chem. 250:4580-4583(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, CRYSTALLIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U07185 Unassigned DNA. Translation: AAA16964.1.

3D structure databases

ProteinModelPortalP41142.
SMRP41142. Positions 7-420.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00254; UER00364.

Family and domain databases

HAMAPMF_00242. Arg_deiminase.
InterProIPR003198. Amidino_trans.
IPR003876. Arg_deiminase.
[Graphical view]
PANTHERPTHR12737:SF9. PTHR12737:SF9. 1 hit.
PfamPF02274. Amidinotransf. 1 hit.
[Graphical view]
PIRSFPIRSF006356. Arg_deiminase. 1 hit.
PRINTSPR01466. ARGDEIMINASE.
TIGRFAMsTIGR01078. arcA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARCA_PSEPU
AccessionPrimary (citable) accession number: P41142
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 3, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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