Reviewed, UniProtKB/Swiss-Prot P37819 (PAH_STRCL)

Names and origin

Protein names

Recommended name:
    Proclavaminate amidinohydrolase
    EC=3.5.3.22
Alternative name(s):
    Proclavaminic acid amidino hydrolase

Gene names

Name:

pah

Organism

Streptomyces clavuligerus

Taxonomic identifier

1901 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	313 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Amidinoproclavaminate + H2O = proclavaminate + urea.
Cofactor	Binds 2 manganese ions per subunit.
Pathway	Antibiotic biosynthesis; clavulanic acid biosynthesis; clavulanic acid from D-glyceraldehyde 3-phosphate and L-arginine: step 4/8.
Subunit structure	Homohexamer.
Sequence similarities	Belongs to the arginase family.

Ontologies

Keywords
Ligand	Manganese Metal-binding
Molecular function	Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	polyamine biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	agmatinase activity Inferred from electronic annotation. Source: InterPro manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW proclavaminate amidinohydrolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 313

313

Proclavaminate amidinohydrolase

PRO_0000173746

Sites

Metal binding

121

1

Manganese 1

Metal binding

144

1

Manganese 1

Metal binding

144

1

Manganese 2

Metal binding

146

1

Manganese 2

Metal binding

148

1

Manganese 1

Metal binding

235

1

Manganese 1

Metal binding

235

1

Manganese 2

Metal binding

237

1

Manganese 2

Secondary structure

1

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313

Helix Strand Turn

Details...

Helix

18 – 20

3

Beta strand

31 – 37

7

Helix

49 – 51

3

Helix

52 – 60

9

Helix

74 – 77

4

Beta strand

80 – 85

6

Helix

93 – 110

18

Beta strand

111 – 119

9

Helix

121 – 123

3

Helix

124 – 135

12

Beta strand

136 – 143

8

Helix

163 – 169

7

Beta strand

172 – 183

12

Helix

194 – 198

5

Beta strand

202 – 205

4

Helix

206 – 225

20

Beta strand

228 – 235

8

Helix

236 – 238

3

Turn

241 – 243

3

Beta strand

246 – 249

4

Helix

257 – 263

7

Helix

264 – 269

6

Beta strand

270 – 278

9

Helix

282 – 284

3

Helix

289 – 308

20

Sequences

	Sequence		Length	Mass (Da)
	P37819-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 759E9B5644B88D5E	FASTA	313	33,401
	10 20 30 40 50 60 MERIDSHVSP RYAQIPTFMR LPHDPQPRGY DVVVIGAPYD GGTSYRPGAR FGPQAIRSES 70 80 90 100 110 120 GLIHGVGIDR GPGTFDLINC VDAGDINLTP FDMNIAIDTA QSHLSGLLKA NAAFLMIGGD 130 140 150 160 170 180 HSLTVAALRA VAEQHGPLAV VHLDAHSDTN PAFYGGRYHH GTPFRHGIDE KLIDPAAMVQ 190 200 210 220 230 240 IGIRGHNPKP DSLDYARGHG VRVVTADEFG ELGVGGTADL IREKVGQRPV YVSVDIDVVD 250 260 270 280 290 300 PAFAPGTGTP APGGLLSREV LALLRCVGDL KPVGFDVMEV SPLYDHGGIT SILATEIGAE 310 LLYQYARAHR TQL

References

[1]	"Cloning, sequencing and disruption of a gene from Streptomyces clavuligerus involved in clavulanic acid biosynthesis." Aidoo K.A., Wong A., Alexander D.C., Rittammer R.A.R., Jensen S.E. Gene 147:41-46(1994) [PubMed: 8088547] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 27064 / DSM 738 / IFO 13307 / JCM 4710 / NRRL 3585.
[2]	"Clavulanic acid biosynthesis in Streptomyces clavuligerus: gene cloning and characterization." Hodgson J.E., Fosberry A.P., Rawlinson N.S., Ross H.N.M., Neal R.J., Arnell J.C., Earl A.J., Lawlor E.J. Gene 166:49-55(1995) [PubMed: 8529893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Oligomeric structure of proclavaminic acid amidino hydrolase: evolution of a hydrolytic enzyme in clavulanic acid biosynthesis." Elkins J.M., Clifton I.J., Hernandez H., Doan L.X., Robinson C.V., Schofield C.J., Hewitson K.S. Biochem. J. 366:423-434(2002) [PubMed: 12020346] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 9-309, PROTEIN SEQUENCE OF 1-6.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U87786 Genomic DNA. Translation: AAA62451.1.
X84101 Genomic DNA. Translation: CAA58904.1.

PIR

S57669.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GQ6	X-ray	1.75	A/B/C	1-313	[»]
1GQ7	X-ray	2.45	A/B/C/D/E/F	1-313	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13488.

BRENDA

3.5.3.22. 229786.

Family and domain databases

InterPro

IPR005925. Agmatinase.
IPR005924. Arginase.
IPR006035. Ureohydrolase.
[Graphical view]

Gene3D

G3DSA:3.40.800.10. Ureohydrolase. 1 hit.

PANTHER

PTHR11358. Ureohydrolase. 1 hit.

Pfam

PF00491. Arginase. 1 hit.
[Graphical view]

PRINTS

PR00116. ARGINASE.

TIGRFAMs

TIGR01230. agmatinase. 1 hit.

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

PAH_STRCL

Accession

Primary (citable) accession number: P37819
Secondary accession number(s): P72400

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	January 20, 2009
This is version 66 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)