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P05326

- IPNS_EMENI

UniProt

P05326 - IPNS_EMENI

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Protein

Isopenicillin N synthase

Gene

ipnA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Iron.
Ascorbate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi214 – 2141Iron
Metal bindingi216 – 2161Iron
Metal bindingi270 – 2701Iron

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. isopenicillin-N synthase activity Source: ASPGD
  3. L-ascorbic acid binding Source: UniProtKB-KW
  4. manganese ion binding Source: ASPGD
  5. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors Source: InterPro

GO - Biological processi

  1. penicillin biosynthetic process Source: ASPGD
  2. secondary metabolic process Source: ASPGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

Iron, Metal-binding, Vitamin C

Enzyme and pathway databases

UniPathwayiUPA00149; UER00240.

Names & Taxonomyi

Protein namesi
Recommended name:
Isopenicillin N synthase (EC:1.21.3.1)
Short name:
IPNS
Gene namesi
Name:ipnA
Synonyms:ips
ORF Names:AN2622
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560: Chromosome VI

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 331331Isopenicillin N synthasePRO_0000219498Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00010504.

Structurei

Secondary structure

1
331
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 133
Helixi15 – 184
Helixi22 – 3716
Beta strandi40 – 467
Helixi51 – 6414
Helixi67 – 737
Turni76 – 783
Beta strandi86 – 916
Turni95 – 973
Beta strandi101 – 1055
Helixi115 – 1184
Turni132 – 1343
Helixi138 – 16326
Turni168 – 1714
Helixi172 – 1743
Turni177 – 1793
Beta strandi183 – 1897
Helixi197 – 1993
Beta strandi208 – 2147
Beta strandi217 – 2259
Beta strandi231 – 2355
Beta strandi238 – 2414
Beta strandi248 – 2536
Helixi255 – 2606
Turni261 – 2633
Beta strandi270 – 2734
Beta strandi279 – 2868
Beta strandi301 – 3033
Helixi313 – 32816

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP05326.
SMRiP05326. Positions 3-331.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05326.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini176 – 288113Fe2OG dioxygenasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG3491.
HOGENOMiHOG000089437.
InParanoidiP05326.
KOiK04126.
OMAiADDNAYL.
OrthoDBiEOG79W9FV.

Family and domain databases

Gene3Di2.60.120.330. 1 hit.
InterProiIPR026992. DIOX_N.
IPR027443. IPNS-like.
IPR002057. Isopenicillin-N_synth_CS.
IPR002283. Isopenicillin-N_synthase.
IPR005123. Oxoglu/Fe-dep_dioxygenase.
[Graphical view]
PfamiPF03171. 2OG-FeII_Oxy. 1 hit.
PF14226. DIOX_N. 1 hit.
[Graphical view]
PRINTSiPR00682. IPNSYNTHASE.
PROSITEiPS51471. FE2OG_OXY. 1 hit.
PS00185. IPNS_1. 1 hit.
PS00186. IPNS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P05326 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSVSKANVP KIDVSPLFGD DQAAKMRVAQ QIDAASRDTG FFYAVNHGIN
60 70 80 90 100
VQRLSQKTKE FHMSITPEEK WDLAIRAYNK EHQDQVRAGY YLSIPGKKAV
110 120 130 140 150
ESFCYLNPNF TPDHPRIQAK TPTHEVNVWP DETKHPGFQD FAEQYYWDVF
160 170 180 190 200
GLSSALLKGY ALALGKEENF FARHFKPDDT LASVVLIRYP YLDPYPEAAI
210 220 230 240 250
KTAADGTKLS FEWHEDVSLI TVLYQSNVQN LQVETAAGYQ DIEADDTGYL
260 270 280 290 300
INCGSYMAHL TNNYYKAPIH RVKWVNAERQ SLPFFVNLGY DSVIDPFDPR
310 320 330
EPNGKSDREP LSYGDYLQNG LVSLINKNGQ T
Length:331
Mass (Da):37,522
Last modified:November 1, 1988 - v1
Checksum:i5BA1A726E9EEFA25
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M18111 Genomic DNA. Translation: AAA33311.1.
M21882 Genomic DNA. Translation: AAA33310.1.
AACD01000045 Genomic DNA. Translation: EAA62969.1.
BN001306 Genomic DNA. Translation: CBF84347.1.
PIRiA27355.
RefSeqiXP_660226.1. XM_655134.1.

Genome annotation databases

EnsemblFungiiCADANIAT00010504; CADANIAP00010504; CADANIAG00010504.
GeneIDi2874542.
KEGGiani:AN2622.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M18111 Genomic DNA. Translation: AAA33311.1 .
M21882 Genomic DNA. Translation: AAA33310.1 .
AACD01000045 Genomic DNA. Translation: EAA62969.1 .
BN001306 Genomic DNA. Translation: CBF84347.1 .
PIRi A27355.
RefSeqi XP_660226.1. XM_655134.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BK0 X-ray 1.30 A 1-331 [» ]
1BLZ X-ray 1.45 A 1-331 [» ]
1HB1 X-ray 1.55 A 1-331 [» ]
1HB2 X-ray 1.30 A 1-331 [» ]
1HB3 X-ray 1.40 A 1-331 [» ]
1HB4 X-ray 1.50 A 1-331 [» ]
1IPS X-ray 2.50 A/B 1-331 [» ]
1OBN X-ray 1.30 A 1-331 [» ]
1OC1 X-ray 2.20 A 1-331 [» ]
1ODM X-ray 1.15 A 1-331 [» ]
1ODN X-ray 1.60 A 1-331 [» ]
1QIQ X-ray 1.50 A 1-331 [» ]
1QJE X-ray 1.35 A 1-331 [» ]
1QJF X-ray 1.40 A 1-331 [» ]
1UZW X-ray 1.30 A 1-331 [» ]
1W03 X-ray 2.10 A 1-331 [» ]
1W04 X-ray 1.28 A 1-331 [» ]
1W05 X-ray 2.46 A 1-331 [» ]
1W06 X-ray 1.65 A 1-331 [» ]
1W3V X-ray 1.40 A 1-331 [» ]
1W3X X-ray 1.46 A 1-331 [» ]
2BJS X-ray 1.30 A 1-325 [» ]
2BU9 X-ray 1.30 A 1-331 [» ]
2IVI X-ray 1.30 B 1-331 [» ]
2IVJ X-ray 1.46 A 1-331 [» ]
2JB4 X-ray 1.30 A 1-331 [» ]
2VAU X-ray 1.80 A 1-331 [» ]
2VBB X-ray 1.40 A 1-331 [» ]
2VBD X-ray 2.00 A 1-331 [» ]
2VBP X-ray 1.50 A 1-331 [» ]
2VCM X-ray 1.65 A 1-331 [» ]
2VE1 X-ray 2.20 A 1-331 [» ]
2WO7 X-ray 2.50 A 1-331 [» ]
2Y60 X-ray 1.40 A 1-331 [» ]
2Y6F X-ray 1.79 A 1-331 [» ]
3ZKU X-ray 1.40 A 1-331 [» ]
3ZKY X-ray 1.45 A 1-331 [» ]
3ZOI X-ray 1.82 A 1-331 [» ]
4BB3 X-ray 1.40 A 1-331 [» ]
ProteinModelPortali P05326.
SMRi P05326. Positions 3-331.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 162425.CADANIAP00010504.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANIAT00010504 ; CADANIAP00010504 ; CADANIAG00010504 .
GeneIDi 2874542.
KEGGi ani:AN2622.2.

Phylogenomic databases

eggNOGi COG3491.
HOGENOMi HOG000089437.
InParanoidi P05326.
KOi K04126.
OMAi ADDNAYL.
OrthoDBi EOG79W9FV.

Enzyme and pathway databases

UniPathwayi UPA00149 ; UER00240 .

Miscellaneous databases

EvolutionaryTracei P05326.

Family and domain databases

Gene3Di 2.60.120.330. 1 hit.
InterProi IPR026992. DIOX_N.
IPR027443. IPNS-like.
IPR002057. Isopenicillin-N_synth_CS.
IPR002283. Isopenicillin-N_synthase.
IPR005123. Oxoglu/Fe-dep_dioxygenase.
[Graphical view ]
Pfami PF03171. 2OG-FeII_Oxy. 1 hit.
PF14226. DIOX_N. 1 hit.
[Graphical view ]
PRINTSi PR00682. IPNSYNTHASE.
PROSITEi PS51471. FE2OG_OXY. 1 hit.
PS00185. IPNS_1. 1 hit.
PS00186. IPNS_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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).

Entry informationi

Entry nameiIPNS_EMENI
AccessioniPrimary (citable) accession number: P05326
Secondary accession number(s): C8VHS7, Q5BA08
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: October 29, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3