Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P27744

- IPNS_AMYLA

UniProt

P27744 - IPNS_AMYLA

Protein

Isopenicillin N synthase

Gene

pcbC

Organism
Amycolatopsis lactamdurans (Nocardia lactamdurans)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 bindingi210 – 2101IronPROSITE-ProRule annotation
    Metal bindingi212 – 2121IronPROSITE-ProRule annotation
    Metal bindingi266 – 2661IronPROSITE-ProRule annotation

    GO - Molecular functioni

    1. iron ion binding Source: InterPro
    2. isopenicillin-N synthase activity Source: UniProtKB-EC
    3. L-ascorbic acid binding Source: UniProtKB-KW
    4. 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. antibiotic biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Antibiotic biosynthesis

    Keywords - Ligandi

    Iron, Metal-binding, Vitamin C

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13365.
    UniPathwayiUPA00149; UER00240.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isopenicillin N synthase (EC:1.21.3.1)
    Short name:
    IPNS
    Gene namesi
    Name:pcbC
    OrganismiAmycolatopsis lactamdurans (Nocardia lactamdurans)
    Taxonomic identifieri1913 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeAmycolatopsis

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 328328Isopenicillin N synthasePRO_0000219502Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP27744.
    SMRiP27744. Positions 6-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini178 – 284107Fe2OG dioxygenasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation

    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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P27744-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKMPSAEVPT IDVSPLFGDD AQEKVRVGQE INKACRGSGF FYAANHGVDV    50
    QRLQDVVNEF HRTMSPQEKY DLAIHAYNKN NSHVRNGYYM AIEGKKAVES 100
    FCYLNPSFSE DHPEIKAGTP MHEVNSWPDE EKHPSFRPFC EEYYWTMHRL 150
    SKVLMRGFAL ALGKDERFFE PELKEADTLS SVSLIRYPYL EDYPPVKTGP 200
    DGEKLSFEDH FDVSMITVLY QTQVQNLQVE TVDGWRDLPT SDTDFLVNAG 250
    TYLGHLTNDY FPSPLHRVKF VNAERLSLPF FFHAGQHTLI EPFFPDGAPE 300
    GKQGNEAVRY GDYLNHGLHS LIVKNGQT 328
    Length:328
    Mass (Da):37,466
    Last modified:August 1, 1992 - v1
    Checksum:iF0DE8B0727AC3855
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57310 Genomic DNA. Translation: CAA40562.1.
    PIRiS15284.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57310 Genomic DNA. Translation: CAA40562.1 .
    PIRi S15284.

    3D structure databases

    ProteinModelPortali P27744.
    SMRi P27744. Positions 6-328.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00149 ; UER00240 .
    BioCyci MetaCyc:MONOMER-13365.

    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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The cephamycin biosynthetic genes pcbAB, encoding a large multidomain peptide synthetase, and pcbC of Nocardia lactamdurans are clustered together in an organization different from the same genes in Acremonium chrysogenum and Penicillium chrysogenum."
      Coque J.J.R., Martin J.F., Calzada J.G., Liras P.
      Mol. Microbiol. 5:1125-1133(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: VAR LC 411.

    Entry informationi

    Entry nameiIPNS_AMYLA
    AccessioniPrimary (citable) accession number: P27744
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 74 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3