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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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei94 – 941Substrate2 Publications
    Metal bindingi354 – 3541Iron (heme axial ligand)4 PublicationsImported

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi50 – 501D → A: Mildly reduces activity with YC-17 and narbomycin. 1 Publication
    Mutagenesisi50 – 501D → N: Increases affinity for narbomycin and YC-17. Mildly increases activity YC-17 and narbomycin. 2 Publications
    Mutagenesisi85 – 851E → 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 Publication
    Mutagenesisi85 – 851E → Q: Reduces affinity for narbomycin and YC-17. Strongly reduces activity with narbomycin and YC-17. 2 Publications
    Mutagenesisi94 – 941E → 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 Publication
    Mutagenesisi94 – 941E → Q: Strongly reduces affinity for narbomycin and YC-17. Strongly reduces activity with narbomycin and YC-17. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 416416Cytochrome P450 monooxygenase PikCPRO_0000430718Add
    BLAST

    Structurei

    Secondary structure

    1
    416
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 163Combined sources
    Helixi18 – 203Combined sources
    Helixi21 – 266Combined sources
    Helixi29 – 3810Combined sources
    Beta strandi40 – 456Combined sources
    Beta strandi47 – 493Combined sources
    Beta strandi51 – 555Combined sources
    Helixi58 – 658Combined sources
    Helixi74 – 763Combined sources
    Helixi83 – 886Combined sources
    Helixi92 – 943Combined sources
    Helixi99 – 1079Combined sources
    Helixi108 – 1114Combined sources
    Helixi113 – 1175Combined sources
    Helixi120 – 13516Combined sources
    Beta strandi137 – 1393Combined sources
    Beta strandi140 – 1434Combined sources
    Helixi144 – 1474Combined sources
    Turni148 – 1503Combined sources
    Helixi151 – 16111Combined sources
    Helixi165 – 1673Combined sources
    Helixi170 – 17910Combined sources
    Helixi184 – 20522Combined sources
    Helixi213 – 22311Combined sources
    Turni225 – 2273Combined sources
    Helixi230 – 24314Combined sources
    Helixi246 – 26116Combined sources
    Helixi263 – 2719Combined sources
    Helixi273 – 2753Combined sources
    Helixi276 – 28712Combined sources
    Beta strandi289 – 2924Combined sources
    Beta strandi296 – 3005Combined sources
    Beta strandi302 – 3043Combined sources
    Beta strandi307 – 3093Combined sources
    Beta strandi315 – 3173Combined sources
    Helixi319 – 3224Combined sources
    Turni326 – 3283Combined sources
    Beta strandi329 – 3313Combined sources
    Beta strandi350 – 3534Combined sources
    Helixi357 – 37418Combined sources
    Beta strandi379 – 3824Combined sources
    Helixi384 – 3863Combined sources
    Beta strandi393 – 3953Combined sources
    Beta strandi402 – 4043Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 11-406.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO87605.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni187 – 1915Substrate binding2 Publications
    Regioni238 – 2469Substrate binding2 Publications

    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
    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. Positions 11-406.
    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: March 16, 2016
    This is version 93 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.