NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-24.
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).

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 (By similarity).
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

L06214; AAA26723.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q05581; 1DRY. [HSSP ENTRY / PDB]

SMR

Q05582; 6-324.

ModBase

Q05582.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13487; -.

Ontologies

GO:0033758;	Molecular function: clavaminate synthase activity (inferred from electronic annotation from EC).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0017000;	Biological process: antibiotic biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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.

ProtoNet

Q05582.

Other

UniRef

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

Keywords

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`	`2 325`	`324`	`Clavaminate synthase 2.`	`PRO_0000089323`
`METAL`	`145 145`		`Iron (By similarity).`
`METAL`	`147 147`		`Iron (By similarity).`
`METAL`	`280 280`		`Iron (By similarity).`
`BINDING`	`294 294`		`2-oxoglutarate (By similarity).`

Sequence information

Length: 325 AA [This is the length of the unprocessed precursor]

Molecular weight: 35840 Da [This is the MW of the unprocessed precursor]

CRC64: 98C03A901B371B0E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASPIVDCTP YRDELLALAS ELPEVPRADL HGFLDEAKTL AARLPEGLAA ALDTFNAVGS 

        70         80         90        100        110        120 
EDGYLLLRGL PVDDSELPET PTSTPAPLDR KRLVMEAMRA LAGRRLGLHT GYQELRSGTV 

       130        140        150        160        170        180 
YHDVYPSPGA HYLSSETSET LLEFHTEMAY HILQPNYVML ACSRADHENR AETLVGSVRK 

       190        200        210        220        230        240 
ALPLLDEKTR ARLFDRKVPC CVDVAFRGGV DDPGAIANVK PLYGDANDPF LGYDRELLAP 

       250        260        270        280        290        300 
EDPADKEAVA HLSQALDDVT VGVKLVPGDV LIIDNFRTTH ARTPFSPRWD GKDRWLHRVY 

       310        320 
IRTDRNGELS GGERAGDTIS FSPRR

Q05582 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