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Protein

Cytochrome P450 monooxygenase PikC

Gene

pikC

Organism
Streptomyces venezuelae
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydroxylation of narbomycin to give rise to pikromycin, and of 10-deoxymethymycin (YC-17) to give rise to methymycin and neomethymycin during macrolide antibiotic biosynthesis. In addition, produces low amounts of neopicromycin, novapikromycin and novamethymycin. Requires the participation of a ferredoxin and a ferredoxin reductase for the transfer of electrons from NADPH to the monooxygenase.6 Publications

Catalytic activityi

Narbomycin + NADPH + O2 = pikromycin + NADP+ + H2O.6 Publications
Narbomycin + NADPH + O2 = neopikromycin + NADP+ + H2O.1 Publication
Narbomycin + 2 NADPH + 2 O2 = novapikromyin + 2 NADP+ + 2 H2O.1 Publication
10-deoxymethymycin + NADPH + O2 = methymycin + NADP+ + H2O.5 Publications
10-deoxymethymycin + NADPH + O2 = neomethymycin + NADP+ + H2O.4 Publications
10-deoxymethymycin + 2 NADPH + 2 O2 = novamethymycin + 2 NADP+ + 2 H2O.1 Publication

Cofactori

heme6 Publications

Kineticsi

  1. KM=120 µM for narbomycin1 Publication
  2. KM=20.4 µM for 10-deoxymethymycin1 Publication
  3. KM=44 µM for narbomycin1 Publication

    Pathwayi: Antibiotic biosynthesis

    This protein is involved in Antibiotic biosynthesis.7 Publications
    View all proteins of this organism that are known to be involved in Antibiotic biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei94Substrate2 Publications1
    Metal bindingi354Iron (heme axial ligand)4 PublicationsImported1

    GO - Molecular functioni

    • heme binding Source: UniProtKB
    • iron ion binding Source: UniProtKB
    • monooxygenase activity Source: UniProtKB
    • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Source: InterPro

    GO - Biological processi

    • macrolide biosynthetic process Source: UniProtKB
    • oxidation-reduction process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Antibiotic biosynthesis

    Keywords - Ligandi

    Heme, Iron, Metal-binding, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-18405.
    BRENDAi1.14.13.185. 6106.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytochrome P450 monooxygenase PikC1 Publication (EC:1.14.13.1856 Publications)
    Alternative name(s):
    Cytochrome P450 monooxygenase PicK1 Publication
    Narbomycin C-12 hydroxylase1 Publication
    Pikromycin synthase CYP107L1
    Gene namesi
    Name:pikC2 Publications
    Synonyms:picK1 Publication
    OrganismiStreptomyces venezuelaeImported
    Taxonomic identifieri54571 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

    Pathology & Biotechi

    Disruption phenotypei

    Abolishes the production of methymycin, neomethymycin and pikromycin and leads to the accumulation of their precursors.2 Publications

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi50D → A: Mildly reduces activity with YC-17 and narbomycin. 1 Publication1
    Mutagenesisi50D → N: Increases affinity for narbomycin and YC-17. Mildly increases activity YC-17 and narbomycin. 2 Publications1
    Mutagenesisi85E → A: Strongly reduces activity with narbomycin, but has only minor effect on activity with YC-17. Loss of activity with YC-17 and narbomycin; when associated with A-94. 1 Publication1
    Mutagenesisi85E → Q: Reduces affinity for narbomycin and YC-17. Strongly reduces activity with narbomycin and YC-17. 2 Publications1
    Mutagenesisi94E → A: Strongly reduces activity with YC-17, but has only minor effect on activity with narbomycin. Loss of activity with YC-17 and narbomycin; when associated with A-85. 1 Publication1
    Mutagenesisi94E → Q: Strongly reduces affinity for narbomycin and YC-17. Strongly reduces activity with narbomycin and YC-17. 2 Publications1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004307181 – 416Cytochrome P450 monooxygenase PikCAdd BLAST416

    Structurei

    Secondary structure

    1416
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi14 – 16Combined sources3
    Helixi18 – 20Combined sources3
    Helixi21 – 26Combined sources6
    Helixi29 – 38Combined sources10
    Beta strandi40 – 45Combined sources6
    Beta strandi47 – 49Combined sources3
    Beta strandi51 – 55Combined sources5
    Helixi58 – 65Combined sources8
    Helixi74 – 76Combined sources3
    Helixi83 – 88Combined sources6
    Helixi92 – 94Combined sources3
    Helixi99 – 107Combined sources9
    Helixi108 – 111Combined sources4
    Helixi113 – 117Combined sources5
    Helixi120 – 135Combined sources16
    Beta strandi137 – 139Combined sources3
    Beta strandi140 – 143Combined sources4
    Helixi144 – 147Combined sources4
    Turni148 – 150Combined sources3
    Helixi151 – 161Combined sources11
    Helixi165 – 167Combined sources3
    Helixi170 – 179Combined sources10
    Helixi184 – 205Combined sources22
    Helixi213 – 223Combined sources11
    Turni225 – 227Combined sources3
    Helixi230 – 243Combined sources14
    Helixi246 – 261Combined sources16
    Helixi263 – 271Combined sources9
    Helixi273 – 275Combined sources3
    Helixi276 – 287Combined sources12
    Beta strandi289 – 292Combined sources4
    Beta strandi296 – 300Combined sources5
    Beta strandi302 – 304Combined sources3
    Beta strandi307 – 309Combined sources3
    Beta strandi315 – 317Combined sources3
    Helixi319 – 322Combined sources4
    Turni326 – 328Combined sources3
    Beta strandi329 – 331Combined sources3
    Beta strandi350 – 353Combined sources4
    Helixi357 – 374Combined sources18
    Beta strandi379 – 382Combined sources4
    Helixi384 – 386Combined sources3
    Beta strandi393 – 395Combined sources3
    Beta strandi402 – 404Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2BVJX-ray2.10A/B1-416[»]
    2C6HX-ray2.35A/B1-416[»]
    2C7XX-ray1.75A1-416[»]
    2CA0X-ray2.85A/B1-416[»]
    2CD8X-ray1.70A/B1-416[»]
    2VZ7X-ray3.20A/B1-416[»]
    2VZMX-ray1.85A/B1-416[»]
    2WHWX-ray2.20A/B1-416[»]
    2WI9X-ray2.00A/B1-416[»]
    3ZK5X-ray1.89A/B1-416[»]
    3ZPIX-ray1.63A/B1-416[»]
    4B7DX-ray1.89A/B1-416[»]
    4B7SX-ray1.84A/B1-416[»]
    4BF4X-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-416[»]
    4UMZX-ray2.32A/B1-416[»]
    ProteinModelPortaliO87605.
    SMRiO87605.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO87605.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni187 – 191Substrate binding2 Publications5
    Regioni238 – 246Substrate binding2 Publications9

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.2 PublicationsUniRule annotationCurated

    Phylogenomic databases

    KOiK16006.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR002397. Cyt_P450_B.
    IPR017972. Cyt_P450_CS.
    [Graphical view]
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PRINTSiPR00359. BP450.
    PR00385. P450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O87605-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRRTQQGTTA SPPVLDLGAL GQDFAADPYP TYARLRAEGP AHRVRTPEGD
    60 70 80 90 100
    EVWLVVGYDR ARAVLADPRF SKDWRNSTTP LTEAEAALNH NMLESDPPRH
    110 120 130 140 150
    TRLRKLVARE FTMRRVELLR PRVQEIVDGL VDAMLAAPDG RADLMESLAW
    160 170 180 190 200
    PLPITVISEL LGVPEPDRAA FRVWTDAFVF PDDPAQAQTA MAEMSGYLSR
    210 220 230 240 250
    LIDSKRGQDG EDLLSALVRT SDEDGSRLTS EELLGMAHIL LVAGHETTVN
    260 270 280 290 300
    LIANGMYALL SHPDQLAALR ADMTLLDGAV EEMLRYEGPV ESATYRFPVE
    310 320 330 340 350
    PVDLDGTVIP AGDTVLVVLA DAHRTPERFP DPHRFDIRRD TAGHLAFGHG
    360 370 380 390 400
    IHFCIGAPLA RLEARIAVRA LLERCPDLAL DVSPGELVWY PNPMIRGLKA
    410
    LPIRWRRGRE AGRRTG
    Length:416
    Mass (Da):46,038
    Last modified:November 1, 1998 - v1
    Checksum:iB7392C742045F06B
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF087022 Genomic DNA. Translation: AAC64105.1.
    AF079139 Genomic DNA. Translation: AAC68886.1.
    RefSeqiWP_055641638.1. NZ_LN881739.1.

    Genome annotation databases

    KEGGiag:AAC68886.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF087022 Genomic DNA. Translation: AAC64105.1.
    AF079139 Genomic DNA. Translation: AAC68886.1.
    RefSeqiWP_055641638.1. NZ_LN881739.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2BVJX-ray2.10A/B1-416[»]
    2C6HX-ray2.35A/B1-416[»]
    2C7XX-ray1.75A1-416[»]
    2CA0X-ray2.85A/B1-416[»]
    2CD8X-ray1.70A/B1-416[»]
    2VZ7X-ray3.20A/B1-416[»]
    2VZMX-ray1.85A/B1-416[»]
    2WHWX-ray2.20A/B1-416[»]
    2WI9X-ray2.00A/B1-416[»]
    3ZK5X-ray1.89A/B1-416[»]
    3ZPIX-ray1.63A/B1-416[»]
    4B7DX-ray1.89A/B1-416[»]
    4B7SX-ray1.84A/B1-416[»]
    4BF4X-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-416[»]
    4UMZX-ray2.32A/B1-416[»]
    ProteinModelPortaliO87605.
    SMRiO87605.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAC68886.

    Phylogenomic databases

    KOiK16006.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-18405.
    BRENDAi1.14.13.185. 6106.

    Miscellaneous databases

    EvolutionaryTraceiO87605.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR002397. Cyt_P450_B.
    IPR017972. Cyt_P450_CS.
    [Graphical view]
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PRINTSiPR00359. BP450.
    PR00385. P450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPIKC_STRVZ
    AccessioniPrimary (citable) accession number: O87605
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 29, 2014
    Last sequence update: November 1, 1998
    Last modified: November 2, 2016
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    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.