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P53608

- ARGI_BACCD

UniProt

P53608 - ARGI_BACCD

Protein

Arginase

Gene

rocF

Organism
Bacillus caldovelox
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Controls arginine catabolism.

    Catalytic activityi

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

    Cofactori

    Binds 2 manganese ions per subunit.1 PublicationPROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi99 – 991Manganese 1
    Metal bindingi122 – 1221Manganese 1
    Metal bindingi122 – 1221Manganese 2
    Metal bindingi124 – 1241Manganese 2
    Metal bindingi126 – 1261Manganese 1
    Binding sitei178 – 1781Substrate
    Metal bindingi226 – 2261Manganese 1
    Metal bindingi226 – 2261Manganese 2
    Metal bindingi228 – 2281Manganese 2
    Binding sitei240 – 2401Substrate
    Binding sitei271 – 2711Substrate

    GO - Molecular functioni

    1. arginase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. arginine metabolic process Source: UniProtKB-KW
    2. urea cycle Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Arginine metabolism

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    SABIO-RKP53608.
    UniPathwayiUPA00158; UER00270.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arginase (EC:3.5.3.1)
    Gene namesi
    Name:rocF
    OrganismiBacillus caldovelox
    Taxonomic identifieri33931 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillusGeobacillus thermoleovorans group

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 299299ArginasePRO_0000173714Add
    BLAST

    Interactioni

    Subunit structurei

    Homohexamer.1 Publication

    Structurei

    Secondary structure

    1
    299
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 96
    Beta strandi14 – 163
    Helixi20 – 223
    Helixi23 – 297
    Helixi32 – 387
    Beta strandi43 – 486
    Turni57 – 593
    Beta strandi60 – 623
    Beta strandi63 – 653
    Helixi68 – 8720
    Beta strandi91 – 988
    Helixi99 – 1013
    Helixi102 – 1109
    Beta strandi114 – 12411
    Turni130 – 1323
    Helixi138 – 1403
    Helixi142 – 1465
    Helixi152 – 1554
    Helixi157 – 1593
    Helixi166 – 1683
    Beta strandi169 – 1746
    Helixi179 – 18810
    Beta strandi191 – 1944
    Helixi195 – 2017
    Helixi203 – 21513
    Beta strandi219 – 2268
    Helixi227 – 2293
    Turni232 – 2343
    Beta strandi238 – 2403
    Helixi248 – 26114
    Beta strandi264 – 2707
    Helixi274 – 2763
    Helixi281 – 29313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP53608.
    SMRiP53608. Positions 1-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53608.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni124 – 1285Substrate binding
    Regioni135 – 1373Substrate binding

    Sequence similaritiesi

    Belongs to the arginase family.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di3.40.800.10. 1 hit.
    InterProiIPR014033. Arginase.
    IPR006035. Ureohydrolase.
    IPR023696. Ureohydrolase_domain.
    IPR020855. Ureohydrolase_Mn_BS.
    [Graphical view]
    PANTHERiPTHR11358. PTHR11358. 1 hit.
    PfamiPF00491. Arginase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036979. Arginase. 1 hit.
    PRINTSiPR00116. ARGINASE.
    TIGRFAMsiTIGR01229. rocF_arginase. 1 hit.
    PROSITEiPS01053. ARGINASE_1. 1 hit.
    PS51409. ARGINASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P53608-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKPISIIGVP MDLGQTRRGV DMGPSAMRYA GVIERLERLH YDIEDLGDIP    50
    IGKAERLHEQ GDSRLRNLKA VAEANEKLAA AVDQVVQRGR FPLVLGGDHS 100
    IAIGTLAGVA KHYERLGVIW YDAHGDVNTA ETSPSGNIHG MPLAASLGFG 150
    HPALTQIGGY SPKIKPEHVV LIGVRSLDEG EKKFIREKGI KIYTMHEVDR 200
    LGMTRVMEET IAYLKERTDG VHLSLDLDGL DPSDAPGVGT PVIGGLTYRE 250
    SHLAMEMLAE AQIITSAEFV EVNPILDERN KTASVAVALM GSLFGEKLM 299
    Length:299
    Mass (Da):32,433
    Last modified:October 1, 1996 - v1
    Checksum:i32D522AFE7F059D1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U48226 Genomic DNA. Translation: AAB06939.1.
    PIRiS68863.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U48226 Genomic DNA. Translation: AAB06939.1 .
    PIRi S68863.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CEV X-ray 2.40 A/B/C/D/E/F 1-299 [» ]
    2CEV X-ray 2.15 A/B/C/D/E/F 1-299 [» ]
    3CEV X-ray 2.40 A/B/C/D/E/F 1-299 [» ]
    4CEV X-ray 2.70 A/B/C/D/E/F 1-299 [» ]
    5CEV X-ray 2.50 A/B/C/D/E/F 1-299 [» ]
    ProteinModelPortali P53608.
    SMRi P53608. Positions 1-299.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    DrugBanki DB00536. Guanidine.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00158 ; UER00270 .
    SABIO-RK P53608.

    Miscellaneous databases

    EvolutionaryTracei P53608.

    Family and domain databases

    Gene3Di 3.40.800.10. 1 hit.
    InterProi IPR014033. Arginase.
    IPR006035. Ureohydrolase.
    IPR023696. Ureohydrolase_domain.
    IPR020855. Ureohydrolase_Mn_BS.
    [Graphical view ]
    PANTHERi PTHR11358. PTHR11358. 1 hit.
    Pfami PF00491. Arginase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036979. Arginase. 1 hit.
    PRINTSi PR00116. ARGINASE.
    TIGRFAMsi TIGR01229. rocF_arginase. 1 hit.
    PROSITEi PS01053. ARGINASE_1. 1 hit.
    PS51409. ARGINASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiARGI_BACCD
    AccessioniPrimary (citable) accession number: P53608
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3