[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21. STRAIN=ATCC 27064 / DSM 738 / IFO 13307 / JCM 4710 / NRRL 3585; DOI=10.1021/bi00165a015; PubMed=1472501 [NCBI, ExPASy, EBI, Israel, Japan] Marsh E.N., Chang M.D.-T., Townsend C.A.; "Two isozymes of clavaminate synthase central to clavulanic acid formation: cloning and sequencing of both genes from Streptomyces clavuligerus."; Biochemistry 31:12648-12657(1992).
[2]	CHARACTERIZATION. STRAIN=ATCC 27064 / DSM 738 / IFO 13307 / JCM 4710 / NRRL 3585; DOI=10.1074/jbc.270.9.4262; PubMed=7876185 [NCBI, ExPASy, EBI, Israel, Japan] Busby R.W., Chang M.D.-T., Busby R.C., Wimp J., Townsend C.A.; "Expression and purification of two isozymes of clavaminate synthase and initial characterization of the iron binding site. General error analysis in polymerase chain reaction amplification."; J. Biol. Chem. 270:4262-4269(1995).
[3]	X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS). STRAIN=ATCC 27064 / DSM 738 / IFO 13307 / JCM 4710 / NRRL 3585; DOI=10.1038/72398; PubMed=10655615 [NCBI, ExPASy, EBI, Israel, Japan] Zhang Z., Ren J.-S., Stammers D.K., Baldwin J.E., Harlos K., Schofield C.J.; "Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase."; Nat. Struct. Biol. 7:127-133(2000).
[4]	X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS). STRAIN=ATCC 27064 / DSM 738 / IFO 13307 / JCM 4710 / NRRL 3585; DOI=10.1016/S0014-5793(02)02520-6; PubMed=12062399 [NCBI, ExPASy, EBI, Israel, Japan] Zhang Z., Ren J.-S., Harlos K., McKinnon C.H., Clifton I.J., Schofield C.J.; "Crystal structure of a clavaminate synthase-Fe(II)-2-oxoglutarate-substrate-NO complex: evidence for metal centered rearrangements."; FEBS Lett. 517:7-12(2002).

Comments

CATALYTIC ACTIVITY: Deoxyamidinoproclavaminate + 2-oxoglutarate + O₂ = amidinoproclavaminate + succinate + CO₂.
CATALYTIC ACTIVITY: Proclavaminate + 2-oxoglutarate + O₂ = dihydroclavaminate + succinate + CO₂ + H₂O.
CATALYTIC ACTIVITY: Dihydroclavaminate + 2-oxoglutarate + O₂ = clavaminate + succinate + CO₂ + H₂O.
COFACTOR: Binds 1 Fe(2+) ion per subunit.
PATHWAY: Antibiotic biosynthesis; clavulanic acid biosynthesis; clavulanic acid from D-glyceraldehyde 3-phosphate and L-arginine: step 3/8 .
PATHWAY: Antibiotic biosynthesis; clavulanic acid biosynthesis; clavulanic acid from D-glyceraldehyde 3-phosphate and L-arginine: step 5/8 .
PATHWAY: Antibiotic biosynthesis; clavulanic acid biosynthesis; clavulanic acid from D-glyceraldehyde 3-phosphate and L-arginine: step 6/8 .
SIMILARITY: Belongs to the clavaminate synthase 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

L06213; AAA26722.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A44241; A44241.

3D structure databases

PDB

1DRT; X-ray; 2.10 A; A=1-324.	[ExPASy / RCSB / EBI]
1DRY; X-ray; 1.40 A; A=1-324.	[ExPASy / RCSB / EBI]
1DS0; X-ray; 1.63 A; A=1-324.	[ExPASy / RCSB / EBI]
1DS1; X-ray; 1.08 A; A=1-324.	[ExPASy / RCSB / EBI]
1GVG; X-ray; 1.54 A; A=1-324.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1DRT; -.
1DRY; -.
1DS0; -.
1DS1; -.
1GVG; -.

ModBase

Q05581.

Family and domain databases

InterPro

IPR014503; Clavaminate_syn.
IPR003819; Taurine_dOase.
Graphical view of domain structure.

Pfam

PF02668; TauD; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF019543; Clavaminate_syn; 1.

Other

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

Keywords

3D-structure; Antibiotic biosynthesis; Direct protein sequencing; Iron; Metal-binding; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 324`	`323`	`Clavaminate synthase 1.`	`PRO_0000089322`
`METAL`	`144 144`		`Iron.`
`METAL`	`146 146`		`Iron.`
`METAL`	`279 279`		`Iron.`
`BINDING`	`293 293`		`2-oxoglutarate (By similarity).`
`STRAND`	`3 5`	`3`
`HELIX`	`7 9`	`3`
`HELIX`	`10 18`	`9`
`HELIX`	`24 27`	`4`
`HELIX`	`28 39`	`12`
`HELIX`	`44 56`	`13`
`STRAND`	`61 67`	`7`
`HELIX`	`73 75`	`3`
`STRAND`	`82 84`	`3`
`HELIX`	`93 105`	`13`
`HELIX`	`115 117`	`3`
`STRAND`	`119 123`	`5`
`STRAND`	`141 144`	`4`
`TURN`	`146 149`	`4`
`STRAND`	`155 163`	`9`
`STRAND`	`172 176`	`5`
`HELIX`	`177 180`	`4`
`HELIX`	`181 183`	`3`
`HELIX`	`186 192`	`7`
`STRAND`	`197 199`	`3`
`HELIX`	`203 205`	`3`
`STRAND`	`216 218`	`3`
`STRAND`	`220 223`	`4`
`TURN`	`234 236`	`3`
`HELIX`	`242 257`	`16`
`STRAND`	`260 262`	`3`
`STRAND`	`269 273`	`5`
`TURN`	`274 276`	`3`
`STRAND`	`277 281`	`5`
`STRAND`	`294 301`	`8`

Sequence information

Length: 324 AA [This is the length of the unprocessed precursor]

Molecular weight: 35370 Da [This is the MW of the unprocessed precursor]

CRC64: F5C251134CA4933E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTSVDCTAYG PELRALAARL PRTPRADLYA FLDAAHTAAA SLPGALATAL DTFNAEGSED 

        70         80         90        100        110        120 
GHLLLRGLPV EADADLPTTP SSTPAPEDRS LLTMEAMLGL VGRRLGLHTG YRELRSGTVY 

       130        140        150        160        170        180 
HDVYPSPGAH HLSSETSETL LEFHTEMAYH RLQPNYVMLA CSRADHERTA ATLVASVRKA 

       190        200        210        220        230        240 
LPLLDERTRA RLLDRRMPCC VDVAFRGGVD DPGAIAQVKP LYGDADDPFL GYDRELLAPE 

       250        260        270        280        290        300 
DPADKEAVAA LSKALDEVTE AVYLEPGDLL IVDNFRTTHA RTPFSPRWDG KDRWLHRVYI 

       310        320 
RTDRNGQLSG GERAGDVVAF TPRG

Q05581 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