[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1987130 [NCBI, ExPASy, EBI, Israel, Japan] Kovacevic S., Miller J.R.; "Cloning and sequencing of the beta-lactam hydroxylase gene (cefF) from Streptomyces clavuligerus: gene duplication may have led to separate hydroxylase and expandase activities in the actinomycetes."; J. Bacteriol. 173:398-400(1991).
[2]	PROTEIN SEQUENCE OF 2-29 AND 92-100, AND CHARACTERIZATION. PubMed=2002049 [NCBI, ExPASy, EBI, Israel, Japan] Baker B.J., Dotzlaf J.E., Yeh W.K.; "Deacetoxycephalosporin C hydroxylase of Streptomyces clavuligerus. Purification, characterization, bifunctionality, and evolutionary implication."; J. Biol. Chem. 266:5087-5093(1991).

Comments

FUNCTION: Hydroxylation of desacetoxicephalosporin C in 3'position to form deacetylcephalosporin C.
CATALYTIC ACTIVITY: Deacetoxycephalosporin C + 2-oxoglutarate + O₂ = deacetylcephalosporin C + succinate + CO₂.
COFACTOR: Iron.
PATHWAY: Antibiotic biosynthesis; cephalosporin C biosynthesis .
SUBUNIT: Monomer.
SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase 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

M63809; AAA26716.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A39204; A39204.

3D structure databases

HSSP

P18548; 1RXF. [HSSP ENTRY / PDB]

ModBase

P42220.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13408; -.

Family and domain databases

InterPro

IPR005123; 2OG-FeII_Oase.
Graphical view of domain structure.

Pfam

PF03171; 2OG-FeII_Oxy; 1.
Pfam graphical view of domain structure.

Other

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

Keywords

Antibiotic biosynthesis; Direct protein sequencing; Iron; Oxidoreductase; Vitamin C.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 318`	`317`	`Deacetoxycephalosporin C hydroxylase.`	`PRO_0000219513`

Sequence information

Length: 318 AA [This is the length of the unprocessed precursor]

Molecular weight: 34585 Da [This is the MW of the unprocessed precursor]

CRC64: B17CC1CBC1E67178 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MADTPVPIFN LAALREGADQ EKFRECVTGM GVFYLTGYGA GDKDHRLATD TAMDFFANGT 

        70         80         90        100        110        120 
EAEKAAVTTD VPTMRRGYSA LEAESTAQVT RTGSYTDYSM SFSMGISGNV FPSPEFERVW 

       130        140        150        160        170        180 
TEYFDKLYAA AQETARLVLT ASGGYDAEIV GSLDELLDAD PVLRLRYFPE VPEHRSAEHE 

       190        200        210        220        230        240 
PRRMAPHYDL SIITFIHQTP CANGFVSLQA EIGGELVSLP VVEDAVVVMC GAMAPLATQG 

       250        260        270        280        290        300 
ALPAPRHHVR SPGAGMREGS DRTSSVFFLR PTTDFSFSVA KARSYGLAVD LDMETATFGD 

       310 
WIGTNYVTMH AKNEPQAG

P42220 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