[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 27064 / DSM 738 / IFO 13307 / JCM 4710 / NRRL 3585; DOI=10.1016/0378-1119(94)90036-1; PubMed=8088547 [NCBI, ExPASy, EBI, Israel, Japan] Aidoo K.A., Wong A., Alexander D.C., Rittammer R.A.R., Jensen S.E.; "Cloning, sequencing and disruption of a gene from Streptomyces clavuligerus involved in clavulanic acid biosynthesis."; Gene 147:41-46(1994).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0378-1119(95)00560-9; PubMed=8529893 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Clavulanic acid biosynthesis in Streptomyces clavuligerus: gene cloning and characterization."; Gene 166:49-55(1995).
[3]	X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 9-309, AND PROTEIN SEQUENCE OF 1-6. DOI=10.1042/BJ20020125; PubMed=12020346 [NCBI, ExPASy, EBI, Israel, Japan] Elkins J.M., Clifton I.J., Hernandez H., Doan L.X., Robinson C.V., Schofield C.J., Hewitson K.S.; "Oligomeric structure of proclavaminic acid amidino hydrolase: evolution of a hydrolytic enzyme in clavulanic acid biosynthesis."; Biochem. J. 366:423-434(2002).

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: Homohexamer.
SIMILARITY: Belongs to the arginase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U87786; AAA62451.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X84101; CAA58904.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S57669; S57669.

3D structure databases

PDB

1GQ6; X-ray; 1.75 A; A/B/C=1-313.	[ExPASy / RCSB / EBI]
1GQ7; X-ray; 2.45 A; A/B/C/D/E/F=1-313.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1GQ6; -.
1GQ7; -.

ModBase

P37819.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13488; -.

Ontologies

GO:0008783;	Molecular function: agmatinase activity (inferred from electronic annotation from InterPro).
GO:0030145;	Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0033972;	Molecular function: proclavaminate amidinohydrolase activity (inferred from electronic annotation from EC).
GO:0006596;	Biological process: polyamine biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR005925; Agmatinase.
IPR005924; Arginase.
IPR006035; Ureohydrolase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.800.10; Ureohydrolase; 1.

PANTHER

PTHR11358; Ureohydrolase; 1.

Pfam

PF00491; Arginase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00116; ARGINASE.

TIGRFAMs

TIGR01230; agmatinase; 1.

PROSITE

PS00147; ARGINASE_1; 1.
PS00148; ARGINASE_2; 1.
PS01053; ARGINASE_3; 1.

ProtoNet

P37819.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Hydrolase; Manganese; Metal-binding.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 313`	`313`	`Proclavaminate amidinohydrolase.`	`PRO_0000173746`
`METAL`	`121 121`		`Manganese 1.`
`METAL`	`144 144`		`Manganese 1.`
`METAL`	`144 144`		`Manganese 2.`
`METAL`	`146 146`		`Manganese 2.`
`METAL`	`148 148`		`Manganese 1.`
`METAL`	`235 235`		`Manganese 1.`
`METAL`	`235 235`		`Manganese 2.`
`METAL`	`237 237`		`Manganese 2.`
`HELIX`	`18 20`	`3`
`STRAND`	`31 37`	`7`
`HELIX`	`49 51`	`3`
`HELIX`	`52 60`	`9`
`HELIX`	`74 77`	`4`
`STRAND`	`80 85`	`6`
`HELIX`	`93 110`	`18`
`STRAND`	`111 119`	`9`
`HELIX`	`121 123`	`3`
`HELIX`	`124 135`	`12`
`STRAND`	`136 143`	`8`
`HELIX`	`163 169`	`7`
`STRAND`	`172 183`	`12`
`HELIX`	`194 198`	`5`
`STRAND`	`202 205`	`4`
`HELIX`	`206 225`	`20`
`STRAND`	`228 235`	`8`
`HELIX`	`236 238`	`3`
`TURN`	`241 243`	`3`
`STRAND`	`246 249`	`4`
`HELIX`	`257 263`	`7`
`HELIX`	`264 269`	`6`
`STRAND`	`270 278`	`9`
`HELIX`	`282 284`	`3`
`HELIX`	`289 308`	`20`

Sequence information

Length: 313 AA [This is the length of the unprocessed precursor]

Molecular weight: 33401 Da [This is the MW of the unprocessed precursor]

CRC64: 759E9B5644B88D5E [This is a checksum on the sequence]

        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

P37819 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools