P11935 (EXPA_CEPAC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cephalosporin biosynthesis expandase/hydroxylase

Including the following 2 domains:

1. Deacetoxycephalosporin C synthase
   Short name=DAOCS
   EC=1.14.20.1
   Alternative name(s):
   Expandase
2. Deacetoxycephalosporin C hydroxylase
   EC=1.14.11.26
   Alternative name(s):
   Beta-lactam hydroxylase
   Deacetylcephalosporin C synthase
   Short name=DACS

Gene names

Name:

CEFEF

Organism

Cephalosporium acremonium (Acremonium chrysogenum)

Taxonomic identifier

5044 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › mitosporic Hypocreales › Acremonium

Protein attributes

Sequence length	332 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	DAOCS catalyzes the step from penicillin N to deacetoxy-cephalosporin C, which is used as a substrate by DACS to form deacetylcephalosporin C.
Catalytic activity	Penicillin N + 2-oxoglutarate + O2 = deacetoxycephalosporin C + succinate + CO2 + H2O. Deacetoxycephalosporin C + 2-oxoglutarate + O2 = deacetylcephalosporin C + succinate + CO2.
Cofactor	Iron. Ascorbate.
Pathway	Antibiotic biosynthesis; cephalosporin C biosynthesis.
Sequence similarities	Belongs to the iron/ascorbate-dependent oxidoreductase family. Contains 1 Fe2OG dioxygenase domain.

Ontologies

Keywords
Biological process	Antibiotic biosynthesis
Ligand	Iron Metal-binding Vitamin C
Molecular function	Oxidoreductase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	antibiotic biosynthetic process 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 deacetoxycephalosporin-C synthase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 332	332	Cephalosporin biosynthesis expandase/hydroxylase		PRO_0000219509
Regions
	Domain	155 – 268	114	Fe2OG dioxygenase
Sites
	Metal binding	184	1	Iron By similarity
	Metal binding	186	1	Iron By similarity
	Metal binding	244	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	P11935 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: E0BD8CE68AA28B79	FASTA	332	36,479
	10 20 30 40 50 60 MTSKVPVFRL DDLKSGKVLT ELAEAVTTKG IFYLTESGLV DDDHTSARET CVDFFKNGSE 70 80 90 100 110 120 EEKRAVTLAD RNARRGFSAL EWESTAVVTE TGKYSDYSTC YSMGIGGNLF PNRGFEDVWQ 130 140 150 160 170 180 DYFDRMYGAA KDVARAVLNS VGAPLAGEDI DDFVECDPLL RLRYFPEVPE DRVAEEEPLR 190 200 210 220 230 240 MGPHYDLSTI TLVHQTACAN GFVSLQCEVD GEFVDLPTLP GAMVVFCGAV GTLATGGKVK 250 260 270 280 290 300 APKHRVKSPG RDQRVGSSRT SSVFFLRPKP DFSFNVQQSR EWGFNVRIPS ERTTFREWLG 310 320 330 GNYVNMRRDK PAAAEAAVPA AAPVSTAAPI AT

References

[1]	"Cloning and expression of the fungal expandase/hydroxylase gene involved in cephalosporin biosynthesis." Samson S.M., Dotzlaf J.E., Slisz M.L., Becker G.W., van Frank R.M., Veal L.E., Yeh W.K., Miller J.R., Queener S.W., Ingolia T.D. Biotechnology (N.Y.) 5:1207-1214(1987) Cited for: NUCLEOTIDE SEQUENCE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
PIR	A29711.
3D structure databases
ProteinModelPortal	P11935.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13406.
BRENDA	1.14.20.1. 1246.
Family and domain databases
InterPro	IPR002057. Isopenicillin-N_synth_CS. IPR005123. Oxoglutarate/Fe-dep_oxygenase. [Graphical view]
Pfam	PF03171. 2OG-FeII_Oxy. 1 hit. [Graphical view]
PROSITE	PS51471. FE2OG_OXY. 1 hit. PS00185. IPNS_1. 1 hit. PS00186. IPNS_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

EXPA_CEPAC

Accession

Primary (citable) accession number: P11935

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	September 21, 2011
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program