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P0A2Y1 (ARGI_BRUAB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Arginase

EC=3.5.3.1
Gene names
Name:arcB
Synonyms:rocF
Ordered Locus Names:BruAb2_0333
OrganismBrucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]
Taxonomic identifier262698 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length306 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

L-arginine + H2O = L-ornithine + urea.

Cofactor

Binds 2 manganese ions per subunit By similarity.

Pathway

Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.

Sequence similarities

Belongs to the arginase family.

Ontologies

Keywords
   Biological processArginine metabolism
   LigandManganese
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processarginine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

urea cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionarginase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 306306Arginase
PRO_0000173716

Regions

Region125 – 1295Substrate binding By similarity
Region136 – 1383Substrate binding By similarity

Sites

Metal binding961Manganese 1 By similarity
Metal binding1231Manganese 1 By similarity
Metal binding1231Manganese 2 By similarity
Metal binding1251Manganese 2 By similarity
Metal binding1271Manganese 1 By similarity
Metal binding2261Manganese 1 By similarity
Metal binding2261Manganese 2 By similarity
Metal binding2281Manganese 2 By similarity
Binding site1781Substrate By similarity
Binding site2711Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A2Y1 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: A953867BC04570B3

FASTA30633,182
        10         20         30         40         50         60 
MHCKILGLPV QEGTGRKGCN MGPDSYRAAG IADAIRELGH ECTDLGNLAP AAQRPLQHPN 

        70         80         90        100        110        120 
HAIKALPYAV AWIEAISEAA YRESAEGFPI FLGGDHLLAA GTVPGIARRA AEKGRKQFVL 

       130        140        150        160        170        180 
WLDAHTDFHT LETTTSGNLH GTPVAYYTGQ KGFEGYFPKL AAPIDPHNVC MLGIRSVDPA 

       190        200        210        220        230        240 
EREAVKKTEV IVYDMRLIDE HGVAALLRRF LERVKAEDGL LHVSLDVDFL DPSIAPAVGT 

       250        260        270        280        290        300 
TVPGGATFRE AHLIMEMLHD SGLVTSLDLV ELNPFLDERG RTAAVMVDLM ASLLGRSVMD 


RPTISY 

« Hide

References

« Hide 'large scale' references
[1]"Brucella abortus arginase and ornithine cyclodeaminase genes are similar to Ti plasmid arginase and ornithine cyclodeaminase."
Kim J., Mayfield J.E.
Biochim. Biophys. Acta 1354:55-57(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 19.
[2]"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis."
Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.
J. Bacteriol. 187:2715-2726(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9-941.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U57319 Genomic DNA. Translation: AAC05588.1.
AE017224 Genomic DNA. Translation: AAX75764.1.
RefSeqYP_223125.1. NC_006933.1.

3D structure databases

ProteinModelPortalP0A2Y1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262698.BruAb2_0333.

Proteomic databases

PRIDEP0A2Y1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAX75764; AAX75764; BruAb2_0333.
GeneID3341875.
KEGGbmb:BruAb2_0333.
PATRIC17826904. VBIBruAbo15061_2635.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0010.
HOGENOMHOG000204319.
KOK01476.
OMAVMELNPA.
OrthoDBEOG6BKJ5H.

Enzyme and pathway databases

BioCycBABO262698:GJC2-2542-MONOMER.
UniPathwayUPA00158; UER00270.

Family and domain databases

Gene3D3.40.800.10. 1 hit.
InterProIPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERPTHR11358. PTHR11358. 1 hit.
PfamPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFPIRSF036979. Arginase. 1 hit.
PRINTSPR00116. ARGINASE.
TIGRFAMsTIGR01229. rocF_arginase. 1 hit.
PROSITEPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGI_BRUAB
AccessionPrimary (citable) accession number: P0A2Y1
Secondary accession number(s): Q579C0, Q59174
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: June 11, 2014
This is version 66 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Brucella abortus strain 9-941

Brucella abortus (strain 9-941): entries and gene names