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Reviewed, UniProtKB/Swiss-Prot P11935 (EXPA_CEPAC)

Last modified June 16, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cephalosporin biosynthesis expandase/hydroxylase
Including the following 2 domains:
    1- Recommended name:
            Deacetoxycephalosporin C synthetase
                Short name=DAOCS
              EC=1.14.20.1
        Alternative name(s):
            Expandase
    2- 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: CEFEF
OrganismCephalosporium acremonium (Acremonium chrysogenum)
Taxonomic identifier5044 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesmitosporic HypocrealesAcremonium

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 332332Cephalosporin biosynthesis expandase/hydroxylase
PRO_0000219509

Sites

Metal binding1841Iron By similarity
Metal binding1861Iron By similarity
Metal binding2441Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
P11935-1 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: E0BD8CE68AA28B79

FASTA33236,479
        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 

« Hide

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.

Cross-references

Sequence databases

PIRA29711.

3D structure databases

HSSPHSSP built from PDB template 1RXG based on UniProtKB P18548.
ModBaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MON-13406.
BRENDA1.14.11.26. 66776.
1.14.20.1. 66776.

Family and domain databases

InterProIPR002057. Isopenicillin-N_synth_CS.
IPR005123. Oxoglutarate/Fe-dep_Oase.
[Graphical view]
PfamPF03171. 2OG-FeII_Oxy. 1 hit.
[Graphical view]
PROSITEPS00185. IPNS_1. 1 hit.
PS00186. IPNS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEXPA_CEPAC
AccessionPrimary (citable) accession number: P11935
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: June 16, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents