Reviewed, UniProtKB/Swiss-Prot P42220 (CEFF_STRCL)

Names and origin

Protein names

Recommended name:
    Deacetoxycephalosporin C hydroxylase
    EC=1.14.11.26
Alternative name(s):
    Deacetylcephalosporin C synthetase
      Short name=DACS
    Beta-lactam hydroxylase

Gene names

Name:

cefF

Organism

Streptomyces clavuligerus

Taxonomic identifier

1901 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	318 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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 structure	Monomer.
Sequence similarities	Belongs to the iron/ascorbate-dependent oxidoreductase family. Contains 1 Fe2OG dioxygenase domain.

Ontologies

Keywords
Biological process	Antibiotic biosynthesis
Ligand	Iron Vitamin C
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	antibiotic biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW deacetoxycephalosporin-C hydroxylase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 318	317	Deacetoxycephalosporin C hydroxylase		PRO_0000219513
Regions
	Domain	158 – 271	114	Fe2OG dioxygenase

Sequences

	Sequence		Length	Mass (Da)
	P42220-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: B17CC1CBC1E67178	FASTA	318	34,585
	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

References

[1]	"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." Kovacevic S., Miller J.R. J. Bacteriol. 173:398-400(1991) [PubMed: 1987130] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Deacetoxycephalosporin C hydroxylase of Streptomyces clavuligerus. Purification, characterization, bifunctionality, and evolutionary implication." Baker B.J., Dotzlaf J.E., Yeh W.K. J. Biol. Chem. 266:5087-5093(1991) [PubMed: 2002049] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-29 AND 92-100, CHARACTERIZATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M63809 Genomic DNA. Translation: AAA26716.1.
PIR	A39204.
3D structure databases
SMR	P42220. Positions 3-314.
ModBase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13408.
BRENDA	1.14.11.26. 229786.
Family and domain databases
InterPro	IPR005123. Oxoglutarate/Fe-dep_oxygenase. [Graphical view]
Pfam	PF03171. 2OG-FeII_Oxy. 1 hit. [Graphical view]
PROSITE	PS51471. FE2OG_OXY. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CEFF_STRCL

Accession

Primary (citable) accession number: P42220

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 48 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)