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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

Mn2+1 PublicationPROSITE-ProRule annotationNote: 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
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 – 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 – 96Combined sources
Beta strandi14 – 163Combined sources
Helixi20 – 223Combined sources
Helixi23 – 297Combined sources
Helixi32 – 387Combined sources
Beta strandi43 – 486Combined sources
Turni57 – 593Combined sources
Beta strandi60 – 623Combined sources
Beta strandi63 – 653Combined sources
Helixi68 – 8720Combined sources
Beta strandi91 – 988Combined sources
Helixi99 – 1013Combined sources
Helixi102 – 1109Combined sources
Beta strandi114 – 12411Combined sources
Turni130 – 1323Combined sources
Helixi138 – 1403Combined sources
Helixi142 – 1465Combined sources
Helixi152 – 1554Combined sources
Helixi157 – 1593Combined sources
Helixi166 – 1683Combined sources
Beta strandi169 – 1746Combined sources
Helixi179 – 18810Combined sources
Beta strandi191 – 1944Combined sources
Helixi195 – 2017Combined sources
Helixi203 – 21513Combined sources
Beta strandi219 – 2268Combined sources
Helixi227 – 2293Combined sources
Turni232 – 2343Combined sources
Beta strandi238 – 2403Combined sources
Helixi248 – 26114Combined sources
Beta strandi264 – 2707Combined sources
Helixi274 – 2763Combined sources
Helixi281 – 29313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MKPISIIGVP MDLGQTRRGV DMGPSAMRYA GVIERLERLH YDIEDLGDIP
60 70 80 90 100
IGKAERLHEQ GDSRLRNLKA VAEANEKLAA AVDQVVQRGR FPLVLGGDHS
110 120 130 140 150
IAIGTLAGVA KHYERLGVIW YDAHGDVNTA ETSPSGNIHG MPLAASLGFG
160 170 180 190 200
HPALTQIGGY SPKIKPEHVV LIGVRSLDEG EKKFIREKGI KIYTMHEVDR
210 220 230 240 250
LGMTRVMEET IAYLKERTDG VHLSLDLDGL DPSDAPGVGT PVIGGLTYRE
260 270 280 290
SHLAMEMLAE AQIITSAEFV EVNPILDERN KTASVAVALM GSLFGEKLM
Length:299
Mass (Da):32,433
Last modified:October 1, 1996 - v1
Checksum:i32D522AFE7F059D1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48226 Genomic DNA. Translation: AAB06939.1.
PIRiS68863.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48226 Genomic DNA. Translation: AAB06939.1 .
PIRi S68863.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 87 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