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P53608 (ARGI_BACCD) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 80. 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
OrganismBacillus caldovelox
Taxonomic identifier33931 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Controls arginine catabolism.

Catalytic activity

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

Cofactor

Binds 2 manganese ions per subunit. Ref.2

Pathway

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

Subunit structure

Homohexamer. Ref.2

Sequence similarities

Belongs to the arginase family.

Ontologies

Keywords
   Biological processArginine metabolism
   LigandManganese
Metal-binding
   Molecular functionHydrolase
   Technical term3D-structure
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: 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 – 299299Arginase
PRO_0000173714

Regions

Region124 – 1285Substrate binding
Region135 – 1373Substrate binding

Sites

Metal binding991Manganese 1
Metal binding1221Manganese 1
Metal binding1221Manganese 2
Metal binding1241Manganese 2
Metal binding1261Manganese 1
Metal binding2261Manganese 1
Metal binding2261Manganese 2
Metal binding2281Manganese 2
Binding site1781Substrate
Binding site2401Substrate
Binding site2711Substrate

Secondary structure

1 ........................................................... 299
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53608 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 32D522AFE7F059D1

FASTA29932,433
        10         20         30         40         50         60 
MKPISIIGVP MDLGQTRRGV DMGPSAMRYA GVIERLERLH YDIEDLGDIP IGKAERLHEQ 

        70         80         90        100        110        120 
GDSRLRNLKA VAEANEKLAA AVDQVVQRGR FPLVLGGDHS IAIGTLAGVA KHYERLGVIW 

       130        140        150        160        170        180 
YDAHGDVNTA ETSPSGNIHG MPLAASLGFG HPALTQIGGY SPKIKPEHVV LIGVRSLDEG 

       190        200        210        220        230        240 
EKKFIREKGI KIYTMHEVDR LGMTRVMEET IAYLKERTDG VHLSLDLDGL DPSDAPGVGT 

       250        260        270        280        290 
PVIGGLTYRE SHLAMEMLAE AQIITSAEFV EVNPILDERN KTASVAVALM GSLFGEKLM

« Hide

References

[1]"The cloning, expression and crystallisation of a thermostable arginase."
Bewley M.C., Lott J.S., Baker E.N., Patchett M.L.
FEBS Lett. 386:215-218(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 411 / NBRC 15315.
[2]"Crystal structures of Bacillus caldovelox arginase in complex with substrate and inhibitors reveal new insights into activation, inhibition and catalysis in the arginase superfamily."
Bewley M.C., Jeffrey P.D., Patchett M.L., Kanyo Z.F., Baker E.N.
Structure 7:435-448(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEXES WITH MANGANESE AND ARGININE, COFACTOR, SUBUNIT.
Strain: DSM 411 / NBRC 15315.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U48226 Genomic DNA. Translation: AAB06939.1.
PIRS68863.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CEVX-ray2.40A/B/C/D/E/F1-299[»]
2CEVX-ray2.15A/B/C/D/E/F1-299[»]
3CEVX-ray2.40A/B/C/D/E/F1-299[»]
4CEVX-ray2.70A/B/C/D/E/F1-299[»]
5CEVX-ray2.50A/B/C/D/E/F1-299[»]
ProteinModelPortalP53608.
SMRP53608. Positions 1-299.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP53608.
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.
PTHR11358:SF2. PTHR11358:SF2. 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...

Other

DrugBankDB00536. Guanidine.
EvolutionaryTraceP53608.

Entry information

Entry nameARGI_BACCD
AccessionPrimary (citable) accession number: P53608
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 3, 2013
This is version 80 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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