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Protein

Arginase

Gene

rocF

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

Functioni

Controls arginine catabolism.

Catalytic activityi

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

Cofactori

Mn2+PROSITE-ProRule annotation1 PublicationNote: Binds 2 manganese ions per subunit.PROSITE-ProRule annotation1 Publication

Pathwayi: urea cycle

This protein is involved in step 1 of the subpathway that synthesizes L-ornithine and urea from L-arginine.By similarity
Proteins known to be involved in this subpathway in this organism are:
  1. Arginase (rocF)
This subpathway is part of the pathway urea cycle, which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-ornithine and urea from L-arginine, the pathway urea cycle and in Nitrogen metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi99Manganese 1Combined sources1 Publication1
Metal bindingi122Manganese 1Combined sources1 Publication1
Metal bindingi122Manganese 2Combined sources1 Publication1
Metal bindingi124Manganese 2Combined sources1 Publication1
Metal bindingi126Manganese 1Combined sources1 Publication1
Binding sitei178SubstrateCombined sources1 Publication1
Metal bindingi226Manganese 1Combined sources1 Publication1
Metal bindingi226Manganese 2Combined sources1 Publication1
Metal bindingi228Manganese 2Combined sources1 Publication1
Binding sitei240SubstrateCombined sources1 Publication1
Binding sitei271SubstrateCombined sources1 Publication1

GO - Molecular functioni

GO - Biological processi

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:3.5.3.1By similarity)
Gene namesi
Name:rocF
OrganismiBacillus caldovelox
Taxonomic identifieri33931 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillusGeobacillus thermoleovorans group

Pathology & Biotechi

Chemistry databases

DrugBankiDB00536. Guanidine.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001737141 – 299ArginaseAdd BLAST299

Interactioni

Subunit structurei

Homohexamer.1 Publication

Structurei

Secondary structure

1299
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Beta strandi14 – 16Combined sources3
Helixi20 – 22Combined sources3
Helixi23 – 29Combined sources7
Helixi32 – 38Combined sources7
Beta strandi43 – 48Combined sources6
Turni57 – 59Combined sources3
Beta strandi60 – 62Combined sources3
Beta strandi63 – 65Combined sources3
Helixi68 – 87Combined sources20
Beta strandi91 – 98Combined sources8
Helixi99 – 101Combined sources3
Helixi102 – 110Combined sources9
Beta strandi114 – 124Combined sources11
Turni130 – 132Combined sources3
Helixi138 – 140Combined sources3
Helixi142 – 146Combined sources5
Helixi152 – 155Combined sources4
Helixi157 – 159Combined sources3
Helixi166 – 168Combined sources3
Beta strandi169 – 174Combined sources6
Helixi179 – 188Combined sources10
Beta strandi191 – 194Combined sources4
Helixi195 – 201Combined sources7
Helixi203 – 215Combined sources13
Beta strandi219 – 226Combined sources8
Helixi227 – 229Combined sources3
Turni232 – 234Combined sources3
Beta strandi238 – 240Combined sources3
Helixi248 – 261Combined sources14
Beta strandi264 – 270Combined sources7
Helixi274 – 276Combined sources3
Helixi281 – 293Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53608.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni124 – 128Substrate bindingCombined sources1 Publication5
Regioni135 – 137Substrate bindingCombined sources1 Publication3

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.
PIRiS68863.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB00536. Guanidine.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00158; UER00270.
SABIO-RKP53608.

Miscellaneous databases

EvolutionaryTraceiP53608.

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]
ProtoNetiSearch...

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 2, 2016
This is version 92 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.