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P39138 (ARGI_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Arginase
EC=3.5.3.1
Gene names
Name:rocF
Ordered Locus Names:BSU40320
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length296 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Controls arginine catabolism.

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.

Induction

Expression is sigma L dependent, induced by arginine, ornithine or proline.

Sequence similarities

Belongs to the arginase family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionarginase activity

Inferred from electronic annotation. Source: 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 – 296296Arginase
PRO_0000173715

Regions

Region122 – 1265Substrate binding By similarity
Region133 – 1353Substrate binding By similarity

Sites

Metal binding971Manganese 1 By similarity
Metal binding1201Manganese 1 By similarity
Metal binding1201Manganese 2 By similarity
Metal binding1221Manganese 2 By similarity
Metal binding1241Manganese 1 By similarity
Metal binding2231Manganese 1 By similarity
Metal binding2231Manganese 2 By similarity
Metal binding2251Manganese 2 By similarity
Binding site1761Substrate By similarity
Binding site2681Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P39138 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: A4074652A0B6C80D

FASTA29632,154
        10         20         30         40         50         60 
MDKTISVIGM PMDLGQARRG VDMGPSAIRY AHLIERLSDM GYTVEDLGDI PINREKIKND 

        70         80         90        100        110        120 
EELKNLNSVL AGNEKLAQKV NKVIEEKKFP LVLGGDHSIA IGTLAGTAKH YDNLGVIWYD 

       130        140        150        160        170        180 
AHGDLNTLET SPSGNIHGMP LAVSLGIGHE SLVNLEGYAP KIKPENVVII GARSLDEGER 

       190        200        210        220        230        240 
KYIKESGMKV YTMHEIDRLG MTKVIEETLD YLSACDGVHL SLDLDGLDPN DAPGVGTPVV 

       250        260        270        280        290 
GGISYRESHL AMEMLYDAGI ITSAEFVEVN PILDHKNKTG KTAVELVESL LGKKLL

« Hide

References

« Hide 'large scale' references
[1]"Expression of the rocDEF operon involved in arginine catabolism in Bacillus subtilis."
Gardan R., Rapoport G., Debarbouille M.
J. Mol. Biol. 249:843-856(1995) [PubMed: 7540694] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"Sequence analysis of the 36-kb region between gntZ and trnY genes of Bacillus subtilis genome."
Kasahara Y., Nakai S., Ogasawara N.
DNA Res. 4:155-159(1997) [PubMed: 9205843] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X81802 Genomic DNA. Translation: CAA57400.1.
D78193 Genomic DNA. Translation: BAA11291.1.
AL009126 Genomic DNA. Translation: CAB16069.1.
PIRS55795.
RefSeqNP_391912.1. NC_000964.3.

3D structure databases

ProteinModelPortalP39138.
SMRP39138. Positions 3-296.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000002520; EBBACP00000002520; EBBACG00000002515.
GeneID937760.
GenomeReviewsGene locus BSU40320 in contig AL009126_GR.
KEGGbsu:BSU40320.
NMPDRfig|224308.1.peg.4038.
PATRIC18980136. VBIBacSub10457_4230.

Organism-specific databases

GenoListBSU40320. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000001627.
HOGENOMHBG391953.
OMAIGAPTDI.
PhylomeDBP39138.
ProtClustDBCLSK873473.

Enzyme and pathway databases

BioCycBSUB:BSU40320-MONOMER.

Family and domain databases

InterProIPR014033. Arginase_subgr.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
Gene3DG3DSA:3.40.800.10. Ureohydrolase. 1 hit.
KOK01476.
PANTHERPTHR11358:SF2. Arginase_sub. 1 hit.
PTHR11358. Ureohydrolase. 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_BACSU
AccessionPrimary (citable) accession number: P39138
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 25, 2012
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents