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P23793 (ARCA_MYCAR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismMycoplasma arginini
Taxonomic identifier2094 [NCBI]
Taxonomic lineageBacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma

Protein attributes

Sequence length410 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 + H2O = L-citrulline + NH3. 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
   Technical term3D-structure
Direct protein sequencing
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

Initiator methionine11Removed Ref.4
Chain2 – 410409Arginine deiminase HAMAP-Rule MF_00242
PRO_0000182219

Sites

Active site3981Amidino-cysteine intermediate By similarity

Experimental info

Sequence conflict761I → T in CAA36693. Ref.3
Sequence conflict1201A → S in CAA36693. Ref.3
Sequence conflict1261E → K in CAA38210. Ref.2
Sequence conflict375 – 41036EAAGI…KDVKW → DKKDYLRPISI in CAA36693. Ref.3

Secondary structure

1 ...................................................................................... 410
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23793 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: E15C9A8AC90176FA

FASTA41046,507
        10         20         30         40         50         60 
MSVFDSKFKG IHVYSEIGEL ESVLVHEPGR EIDYITPARL DELLFSAILE SHDARKEHKQ 

        70         80         90        100        110        120 
FVAELKANDI NVVELIDLVA ETYDLASQEA KDKLIEEFLE DSEPVLSEEH KVVVRNFLKA 

       130        140        150        160        170        180 
KKTSRELVEI MMAGITKYDL GIEADHELIV DPMPNLYFTR DPFASVGNGV TIHYMRYKVR 

       190        200        210        220        230        240 
QRETLFSRFV FSNHPKLINT PWYYDPSLKL SIEGGDVFIY NNDTLVVGVS ERTDLQTVTL 

       250        260        270        280        290        300 
LAKNIVANKE CEFKRIVAIN VPKWTNLMHL DTWLTMLDKD KFLYSPIAND VFKFWDYDLV 

       310        320        330        340        350        360 
NGGAEPQPVE NGLPLEGLLQ SIINKKPVLI PIAGEGASQM EIERETHFDG TNYLAIRPGV 

       370        380        390        400        410 
VIGYSRNEKT NAALEAAGIK VLPFHGNQLS LGMGNARCMS MPLSRKDVKW

« Hide

References

[1]"High-level expression of Mycoplasma arginine deiminase in Escherichia coli and its efficient renaturation as an anti-tumor enzyme."
Misawa S., Aoshima M., Takaku H., Matsumoto M., Hayashi H.
J. Biotechnol. 36:145-155(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: ATCC 23838 / G230 / NBRC 14476 / NCTC 10129.
[2]"Cloning and nucleotide sequence of the gene encoding arginine deiminase of Mycoplasma arginini."
Ohno T., Ando O., Sugimura K., Taniai M., Suzuki M., Fukuda S., Nagase Y., Yamamoto K., Azuma I.
Infect. Immun. 58:3788-3795(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[3]"Cloning and sequence analysis of the arginine deiminase gene from Mycoplasma arginini."
Kondo K., Sone H., Yoshida H., Toida T., Kanatani K., Hong Y.-M., Nishino N., Tanaka J.
Mol. Gen. Genet. 221:81-86(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: KM101.
[4]"Potent growth inhibition of human tumor cells in culture by arginine deiminase purified from a culture medium of a Mycoplasma-infected cell line."
Miyazaki K., Takaku H., Umeda M., Fujita T., Huang W.D., Kimura T., Yamashita J., Horio T.
Cancer Res. 50:4522-4527(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-18.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X54141 Genomic DNA. Translation: CAA38080.1.
X54312 Genomic DNA. Translation: CAA38210.1.
X52459 Genomic DNA. Translation: CAA36693.2.
PIRA41465.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LXYX-ray2.00A/B2-409[»]
1S9RX-ray1.60A/B1-410[»]
ProteinModelPortalP23793.
SMRP23793. Positions 2-410.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP23793.
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...

Other

EvolutionaryTraceP23793.

Entry information

Entry nameARCA_MYCAR
AccessionPrimary (citable) accession number: P23793
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 87 of the entry and version 4 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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