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Reviewed, UniProtKB/Swiss-Prot P05326 (IPNS_EMENI)

Last modified September 22, 2009. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
    Isopenicillin N synthetase
    EC=1.21.3.1
Alternative name(s):
    Isopenicillin N synthase
      Short name=IPNS
Gene names
Name: ipnA
Synonyms: ips
ORF Names: AN2622
OrganismEmericella nidulans (Aspergillus nidulans) [Complete proteome]
Taxonomic identifier162425 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeEmericella

Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Removes, in the presence of oxygen, 4 hydrogen atoms from delta-L-(alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV) to form the azetidinone and thiazolidine rings of isopenicillin.

Catalytic activity

N-((5S)-5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + O2 = isopenicillin N + 2 H2O.

Cofactor

Iron.

Ascorbate.

Pathway

Antibiotic biosynthesis; penicillin G biosynthesis; penicillin G from L-alpha-aminoadipate and L-cysteine and L-valine: step 2/3.

Sequence similarities

Belongs to the iron/ascorbate-dependent oxidoreductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 331331Isopenicillin N synthetase
PRO_0000219498

Sites

Metal binding2141Iron
Metal binding2161Iron
Metal binding2701Iron

Secondary structure

....................................................... 331
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05326-1 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 5BA1A726E9EEFA25

FASTA33137,522
        10         20         30         40         50         60 
MGSVSKANVP KIDVSPLFGD DQAAKMRVAQ QIDAASRDTG FFYAVNHGIN VQRLSQKTKE 

        70         80         90        100        110        120 
FHMSITPEEK WDLAIRAYNK EHQDQVRAGY YLSIPGKKAV ESFCYLNPNF TPDHPRIQAK 

       130        140        150        160        170        180 
TPTHEVNVWP DETKHPGFQD FAEQYYWDVF GLSSALLKGY ALALGKEENF FARHFKPDDT 

       190        200        210        220        230        240 
LASVVLIRYP YLDPYPEAAI KTAADGTKLS FEWHEDVSLI TVLYQSNVQN LQVETAAGYQ 

       250        260        270        280        290        300 
DIEADDTGYL INCGSYMAHL TNNYYKAPIH RVKWVNAERQ SLPFFVNLGY DSVIDPFDPR 

       310        320        330 
EPNGKSDREP LSYGDYLQNG LVSLINKNGQ T 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the isopenicillin N synthetase gene mediating the formation of the beta-lactam ring in Aspergillus nidulans."
Ramon D., Carramolino L., Patino C., Sanchez F., Penalva M.A.
Gene 57:171-181(1987) [PubMed: 3319778] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cloning and expression in Escherichia coli of isopenicillin N synthetase genes from Streptomyces lipmanii and Aspergillus nidulans."
Weigel B.J., Burgett S.G., Chen V.J., Skatrud P.L., Frolik C.A., Queener S.W., Ingolia T.D.
J. Bacteriol. 170:3817-3826(1988) [PubMed: 3045077] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC 4.
[4]"Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans."
Roach P.L., Schofield C.J., Baldwin J.E., Clifton I.J., Hajdu J.
Protein Sci. 4:1007-1009(1995) [PubMed: 7663335] [Abstract]
Cited for: CRYSTALLIZATION.
[5]"Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes."
Roach P.L., Clifton I.J., Fueloep V., Harlos K., Barton G.J., Hajdu J., Andersson I., Schofield C.J., Baldwin J.E.
Nature 375:700-704(1995) [PubMed: 7791906] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[6]"Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation."
Roach P.L., Clifton I.J., Hensgens C.M., Shibata N., Schofield C.J., Hajdu J., Baldwin J.E.
Nature 387:827-830(1997) [PubMed: 9194566] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
[7]"The reaction cycle of isopenicillin N synthase observed by X-ray diffraction."
Burzlaff N.I., Rutledge P.J., Clifton I.J., Hensgens C.M.H., Pickford M., Adlington R.M., Roach P.L., Baldwin J.E.
Nature 401:721-724(1999) [PubMed: 10537113] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
[8]"Alternative oxidation by isopenicillin N synthase observed by X-ray diffraction."
Ogle J.M., Clifton I.J., Rutledge P.J., Elkins J.M., Burzlaff N.I., Adlington R.M., Roach P.L., Baldwin J.E.
Chem. Biol. 8:1231-1237(2001) [PubMed: 11755401] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

M18111 Genomic DNA. Translation: AAA33311.1.
M21882 Genomic DNA. Translation: AAA33310.1.
AACD01000045 Genomic DNA. Translation: EAA62969.1.
PIRA27355.
RefSeqXP_660226.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1BK0X-ray1.30A1-331[»]
1BLZX-ray1.45A1-331[»]
1HB1X-ray1.55A1-331[»]
1HB2X-ray1.30A1-331[»]
1HB3X-ray1.40A1-331[»]
1HB4X-ray1.50A1-331[»]
1IPSX-ray2.50A/B1-331[»]
1OBNX-ray1.30A1-331[»]
1OC1X-ray2.20A1-331[»]
1ODMX-ray1.15A1-331[»]
1ODNX-ray1.60A1-331[»]
1QIQX-ray1.50A1-331[»]
1QJEX-ray1.35A1-331[»]
1QJFX-ray1.40A1-331[»]
1UZWX-ray1.30A1-331[»]
1W03X-ray2.10A1-331[»]
1W04X-ray1.28A1-331[»]
1W05X-ray2.46A1-331[»]
1W06X-ray1.65A1-331[»]
1W3VX-ray1.40A1-331[»]
1W3XX-ray1.46A1-331[»]
2BJSX-ray1.30A1-325[»]
2BU9X-ray1.30A1-331[»]
2IVIX-ray1.30B1-331[»]
2IVJX-ray1.46A1-331[»]
2JB4X-ray1.30A1-331[»]
2VAUX-ray1.80A1-331[»]
2VBBX-ray1.40A1-331[»]
2VBDX-ray2.00A1-331[»]
2VBPX-ray1.50A1-331[»]
2VCMX-ray1.65A1-331[»]
2VE1X-ray2.20A1-331[»]
ModBaseSearch...

Genome annotation databases

GeneID2874542.
KEGGani:AN2622.2.

Family and domain databases

InterProIPR002057. Isopenicillin-N_synth_CS.
IPR002283. Isopenicillin-N_synthase.
IPR005123. Oxoglutarate/Fe-dep_oxygenase.
[Graphical view]
PfamPF03171. 2OG-FeII_Oxy. 1 hit.
[Graphical view]
PRINTSPR00682. IPNSYNTHASE.
PROSITEPS00185. IPNS_1. 1 hit.
PS00186. IPNS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIPNS_EMENI
AccessionPrimary (citable) accession number: P05326
Secondary accession number(s): Q5BA08
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: September 22, 2009
This is version 86 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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