Reviewed, UniProtKB/Swiss-Prot P53608 (ARGI_BACCD)

Names and origin

Protein names

Recommended name:
    Arginase
    EC=3.5.3.1

Gene names

Name:

rocF

Organism

Bacillus caldovelox

Taxonomic identifier

33931 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	299 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Arginine metabolism
Ligand	Manganese Metal-binding
Molecular function	Hydrolase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	arginine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	arginase activity Inferred from electronic annotation. Source: EC manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 299

299

Arginase

PRO_0000173714

Regions

Region

124 – 128

5

Substrate binding

Region

135 – 137

3

Substrate binding

Sites

Metal binding

99

1

Manganese 1

Metal binding

122

1

Manganese 1

Metal binding

122

1

Manganese 2

Metal binding

124

1

Manganese 2

Metal binding

126

1

Manganese 1

Metal binding

226

1

Manganese 1

Metal binding

226

1

Manganese 2

Metal binding

228

1

Manganese 2

Binding site

178

1

Substrate

Binding site

240

1

Substrate

Binding site

271

1

Substrate

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

299

Helix Strand Turn

Details...

Beta strand

4 – 9

6

Beta strand

14 – 16

3

Helix

20 – 22

3

Helix

23 – 29

7

Helix

32 – 38

7

Beta strand

43 – 48

6

Beta strand

63 – 65

3

Helix

68 – 87

20

Beta strand

91 – 98

8

Helix

101 – 110

10

Beta strand

114 – 124

11

Turn

130 – 132

3

Helix

138 – 140

3

Helix

142 – 146

5

Helix

152 – 155

4

Helix

157 – 159

3

Helix

166 – 168

3

Beta strand

169 – 174

6

Helix

179 – 188

10

Beta strand

191 – 194

4

Helix

195 – 201

7

Helix

203 – 215

13

Beta strand

219 – 226

8

Helix

227 – 229

3

Turn

232 – 234

3

Beta strand

238 – 240

3

Helix

248 – 261

14

Beta strand

264 – 270

7

Helix

281 – 293

13

Sequences

	Sequence		Length	Mass (Da)
	P53608-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 32D522AFE7F059D1	FASTA	299	32,433
	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

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: 8647285] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 411 / IFO 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: 10196128] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEXES WITH MANGANESE AND ARGININE, COFACTOR, SUBUNIT. Strain: DSM 411 / IFO 15315.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U48226 Genomic DNA. Translation: AAB06939.1.

PIR

S68863.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

3.5.3.1. 119531.

Family and domain databases

InterPro

IPR005924. Arginase.
IPR014033. Arginase_sub.
IPR006035. Ureohydrolase.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]

Gene3D

G3DSA:3.40.800.10. Ureohydrolase. 1 hit.

PANTHER

PTHR11358:SF2. Arginase_sub. 1 hit.
PTHR11358. Ureohydrolase. 1 hit.

Pfam

PF00491. Arginase. 1 hit.
[Graphical view]

PRINTS

PR00116. ARGINASE.

TIGRFAMs

TIGR01229. rocF_arginase. 1 hit.

PROSITE

PS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00536. Guanidine.

Entry information

Entry name

ARGI_BACCD

Accession

Primary (citable) accession number: P53608

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	February 9, 2010
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)