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P05326 (IPNS_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isopenicillin N synthase

Short name=IPNS
EC=1.21.3.1
Gene names
Name:ipnA
Synonyms:ips
ORF Names:AN2622
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length331 AA.
Sequence statusComplete.
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.

Contains 1 Fe2OG dioxygenase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 331331Isopenicillin N synthase
PRO_0000219498

Regions

Domain176 – 288113Fe2OG dioxygenase

Sites

Metal binding2141Iron
Metal binding2161Iron
Metal binding2701Iron

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P05326 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[4]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[5]"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] [Europe PMC] [Abstract]
Cited for: CRYSTALLIZATION.
[6]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[7]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
[8]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
[9]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M18111 Genomic DNA. Translation: AAA33311.1.
M21882 Genomic DNA. Translation: AAA33310.1.
AACD01000045 Genomic DNA. Translation: EAA62969.1.
BN001306 Genomic DNA. Translation: CBF84347.1.
PIRA27355.
RefSeqXP_660226.1. XM_655134.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
2WO7X-ray2.50A1-331[»]
2Y60X-ray1.40A1-331[»]
2Y6FX-ray1.79A1-331[»]
3ZKUX-ray1.40A1-331[»]
3ZKYX-ray1.45A1-331[»]
3ZOIX-ray1.82A1-331[»]
4BB3X-ray1.40A1-331[»]
ProteinModelPortalP05326.
SMRP05326. Positions 3-331.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00010504.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00010504; CADANIAP00010504; CADANIAG00010504.
GeneID2874542.
KEGGani:AN2622.2.

Phylogenomic databases

eggNOGCOG3491.
HOGENOMHOG000089437.
KOK04126.
OMAADDNAYL.
OrthoDBEOG79W9FV.

Enzyme and pathway databases

UniPathwayUPA00149; UER00240.

Family and domain databases

Gene3D2.60.120.330. 1 hit.
InterProIPR026992. DIOX_N.
IPR027443. IPNS-like.
IPR002057. Isopenicillin-N_synth_CS.
IPR002283. Isopenicillin-N_synthase.
IPR005123. Oxoglu/Fe-dep_dioxygenase.
[Graphical view]
PfamPF03171. 2OG-FeII_Oxy. 1 hit.
PF14226. DIOX_N. 1 hit.
[Graphical view]
PRINTSPR00682. IPNSYNTHASE.
PROSITEPS51471. FE2OG_OXY. 1 hit.
PS00185. IPNS_1. 1 hit.
PS00186. IPNS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP05326.

Entry information

Entry nameIPNS_EMENI
AccessionPrimary (citable) accession number: P05326
Secondary accession number(s): C8VHS7, Q5BA08
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: July 9, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways