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P53608

- ARGI_BACCD

UniProt

P53608 - ARGI_BACCD

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Protein
Arginase
Gene
rocF
Organism
Bacillus caldovelox
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Controls arginine catabolism.

Catalytic activityi

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

Cofactori

Binds 2 manganese ions per subunit.1 Publication

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
Complete GO annotation...

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 – 299299Arginase
PRO_0000173714Add
BLAST

Interactioni

Subunit structurei

Homohexamer.1 Publication

Structurei

Secondary structure

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.

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.

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: September 3, 2014
This is version 84 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

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