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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: 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

Protein has several cofactor binding sites:

Pathwayi: penicillin G biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes penicillin G from L-alpha-aminoadipate and L-cysteine and L-valine.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase (acvA)
  2. Isopenicillin N synthase (ipnA)
  3. Acyl-coenzyme A:6-aminopenicillanic-acid-acyltransferase 40 kDa form (penDE)
This subpathway is part of the pathway penicillin G biosynthesis, which is itself part of Antibiotic biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes penicillin G from L-alpha-aminoadipate and L-cysteine and L-valine, the pathway penicillin G biosynthesis and in Antibiotic biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi214Iron1
Metal bindingi216Iron1
Metal bindingi270Iron1

GO - Molecular functioni

GO - Biological processi

  • penicillin biosynthetic 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

BRENDAi1.21.3.1. 517.
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
Proteomesi
  • UP000000560 Componenti: Chromosome VI
  • UP000005890 Componenti: Partially assembled WGS sequence

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002194981 – 331Isopenicillin N synthaseAdd BLAST331

Structurei

Secondary structure

1331
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 13Combined sources3
Helixi15 – 18Combined sources4
Helixi22 – 37Combined sources16
Beta strandi40 – 46Combined sources7
Helixi51 – 64Combined sources14
Helixi67 – 73Combined sources7
Turni76 – 78Combined sources3
Beta strandi86 – 91Combined sources6
Turni95 – 97Combined sources3
Beta strandi101 – 105Combined sources5
Helixi115 – 118Combined sources4
Turni132 – 134Combined sources3
Helixi138 – 163Combined sources26
Turni168 – 171Combined sources4
Helixi172 – 174Combined sources3
Turni177 – 179Combined sources3
Beta strandi183 – 189Combined sources7
Helixi197 – 199Combined sources3
Beta strandi208 – 214Combined sources7
Beta strandi217 – 225Combined sources9
Beta strandi231 – 235Combined sources5
Beta strandi238 – 241Combined sources4
Beta strandi248 – 253Combined sources6
Helixi255 – 260Combined sources6
Turni261 – 263Combined sources3
Beta strandi270 – 273Combined sources4
Beta strandi279 – 286Combined sources8
Beta strandi301 – 303Combined sources3
Helixi313 – 328Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05326.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini176 – 288Fe2OG dioxygenasePROSITE-ProRule annotationAdd BLAST113

Sequence similaritiesi

Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000089437.
InParanoidiP05326.
KOiK04126.
OMAiEADDNAY.
OrthoDBiEOG092C2ZLC.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

P05326-1 [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:
EMBLi
GenBanki
DDBJi
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.
EAA62969; EAA62969; AN2622.2.
GeneIDi2874542.
KEGGiani:AN2622.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00010504; CADANIAP00010504; CADANIAG00010504.
EAA62969; EAA62969; AN2622.2.
GeneIDi2874542.
KEGGiani:AN2622.2.

Phylogenomic databases

HOGENOMiHOG000089437.
InParanoidiP05326.
KOiK04126.
OMAiEADDNAY.
OrthoDBiEOG092C2ZLC.

Enzyme and pathway databases

UniPathwayiUPA00149; UER00240.
BRENDAi1.21.3.1. 517.

Miscellaneous databases

EvolutionaryTraceiP05326.

Family and domain databases

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

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: November 30, 2016
This is version 140 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.