Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Epi-isozizaene 5-monooxygenase/(E)-beta-farnesene synthase

Gene

SCO5223

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of the sesquiterpenoid antibiotic albaflavenone. Catalyzes the two-step allylic oxidation of epi-isozizaene to albaflavenone. First carries out a non-stereo-specific oxidation of epi-isozizaene to give a mixture of the albaflavenol epimers ((5R)-albaflavenol and (5S)-albaflavenol), each of which can serve as substrate for the second oxidation to yield albaflavenone. This is quite different from most other P450s which catalyze regio- and stereospecific oxidation. Displays also a farnesene synthase activity with farnesyl diphosphate (FPP) as substrate.2 Publications

Catalytic activityi

+-epi-isozizaene + 2 NADPH + 2 O2 = albaflavenone + 2 NADP+ + 3 H2O.1 Publication
(2E,6E)-farnesyl diphosphate = (E)-beta-farnesene + diphosphate.1 Publication

Cofactori

Mg2+1 Publication, Ca2+1 Publication, Mn2+1 PublicationNote: Divalent metal cations. Mg2+, Ca2+ or Mn2+ ions for farnesene synthase activity.1 Publication

Kineticsi

Kcat is 0.019 s(-1) with farnesyl diphosphate (FPP) as substrate (in the presence of magnesium ions at 30 degrees Celsius and at pH 5.5).

  1. KM=16.8 µM for FPP (in the presence of magnesium ions at 30 degrees Celsius and at pH 5.5)1 Publication

    pH dependencei

    Optimum pH is between 7 and 8.2 for monooxygenase activity and between 5.5 and 6.5 for farnesene synthase activity.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi410 – 4101Iron (heme axial ligand)

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase, Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    Heme, Iron, Magnesium, Metal-binding, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13905.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Epi-isozizaene 5-monooxygenase/(E)-beta-farnesene synthase (EC:1.14.13.106, EC:4.2.3.47)
    Alternative name(s):
    Cytochrome P450 170A1
    Short name:
    CYP170A1
    Gene namesi
    Ordered Locus Names:SCO5223
    OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
    Taxonomic identifieri100226 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
    Proteomesi
    • UP000001973 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Disruption phenotypei

    Disruption abolishes biosynthesis of both albaflavenone and the albaflavenols, but not epi-isozizaene.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi253 – 2531D → A: Loss of any farnesene synthase activity, whereas the P450 monooxygenase activity is retained. 1 Publication
    Mutagenesisi254 – 2541D → A: Loss of any farnesene synthase activity, whereas the P450 monooxygenase activity is retained. 1 Publication
    Mutagenesisi257 – 2571D → A: Loss of any farnesene synthase activity, whereas the P450 monooxygenase activity is retained. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 461461Epi-isozizaene 5-monooxygenase/(E)-beta-farnesene synthasePRO_0000418620Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi100226.SCO5223.

    Structurei

    Secondary structure

    1
    461
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi35 – 428Combined sources
    Helixi44 – 518Combined sources
    Helixi52 – 543Combined sources
    Beta strandi56 – 627Combined sources
    Beta strandi65 – 706Combined sources
    Helixi73 – 819Combined sources
    Beta strandi85 – 873Combined sources
    Turni89 – 924Combined sources
    Helixi93 – 964Combined sources
    Turni97 – 1015Combined sources
    Beta strandi102 – 1043Combined sources
    Helixi117 – 1193Combined sources
    Helixi120 – 1234Combined sources
    Turni125 – 1273Combined sources
    Turni129 – 1313Combined sources
    Helixi132 – 14514Combined sources
    Helixi154 – 17017Combined sources
    Helixi177 – 19216Combined sources
    Helixi220 – 23415Combined sources
    Helixi244 – 2485Combined sources
    Helixi261 – 29232Combined sources
    Helixi294 – 30815Combined sources
    Helixi315 – 3184Combined sources
    Helixi322 – 33413Combined sources
    Beta strandi341 – 3444Combined sources
    Beta strandi349 – 3513Combined sources
    Beta strandi354 – 3563Combined sources
    Beta strandi361 – 3644Combined sources
    Helixi366 – 3705Combined sources
    Turni373 – 3753Combined sources
    Turni377 – 3804Combined sources
    Helixi384 – 3874Combined sources
    Helixi389 – 3924Combined sources
    Beta strandi405 – 4095Combined sources
    Helixi413 – 43018Combined sources
    Beta strandi431 – 4355Combined sources
    Beta strandi440 – 45314Combined sources
    Beta strandi455 – 4606Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3DBGX-ray2.60A/B1-461[»]
    3EL3X-ray3.30A/B1-461[»]
    ProteinModelPortaliQ9K498.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9K498.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Phylogenomic databases

    eggNOGiENOG41068W2. Bacteria.
    COG2124. LUCA.
    HOGENOMiHOG000043114.
    InParanoidiQ9K498.
    KOiK12645.
    OMAiEMSEWAS.
    OrthoDBiPOG091H09CE.
    PhylomeDBiQ9K498.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR002401. Cyt_P450_E_grp-I.
    [Graphical view]
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PRINTSiPR00463. EP450I.
    PR00385. P450.
    SUPFAMiSSF48264. SSF48264. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9K498-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTVESVNPET RAPAAPGAPE LREPPVAGGG VPLLGHGWRL ARDPLAFMSQ
    60 70 80 90 100
    LRDHGDVVRI KLGPKTVYAV TNPELTGALA LNPDYHIAGP LWESLEGLLG
    110 120 130 140 150
    KEGVATANGP LHRRQRRTIQ PAFRLDAIPA YGPIMEEEAH ALTERWQPGK
    160 170 180 190 200
    TVDATSESFR VAVRVAARCL LRGQYMDERA ERLCVALATV FRGMYRRMVV
    210 220 230 240 250
    PLGPLYRLPL PANRRFNDAL ADLHLLVDEI IAERRASGQK PDDLLTALLE
    260 270 280 290 300
    AKDDNGDPIG EQEIHDQVVA ILTPGSETIA STIMWLLQAL ADHPEHADRI
    310 320 330 340 350
    RDEVEAVTGG RPVAFEDVRK LRHTGNVIVE AMRLRPAVWV LTRRAVAESE
    360 370 380 390 400
    LGGYRIPAGA DIIYSPYAIQ RDPKSYDDNL EFDPDRWLPE RAANVPKYAM
    410 420 430 440 450
    KPFSAGKRKC PSDHFSMAQL TLITAALATK YRFEQVAGSN DAVRVGITLR
    460
    PHDLLVRPVA R
    Length:461
    Mass (Da):50,938
    Last modified:October 1, 2000 - v1
    Checksum:i10282E36A405B57E
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL939123 Genomic DNA. Translation: CAB94608.1.
    RefSeqiNP_629370.1. NC_003888.3.
    WP_011030120.1. NC_003888.3.

    Genome annotation databases

    EnsemblBacteriaiCAB94608; CAB94608; CAB94608.
    GeneIDi1100664.
    KEGGisco:SCO5223.
    PATRICi23740298. VBIStrCoe124346_5307.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL939123 Genomic DNA. Translation: CAB94608.1.
    RefSeqiNP_629370.1. NC_003888.3.
    WP_011030120.1. NC_003888.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3DBGX-ray2.60A/B1-461[»]
    3EL3X-ray3.30A/B1-461[»]
    ProteinModelPortaliQ9K498.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi100226.SCO5223.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB94608; CAB94608; CAB94608.
    GeneIDi1100664.
    KEGGisco:SCO5223.
    PATRICi23740298. VBIStrCoe124346_5307.

    Phylogenomic databases

    eggNOGiENOG41068W2. Bacteria.
    COG2124. LUCA.
    HOGENOMiHOG000043114.
    InParanoidiQ9K498.
    KOiK12645.
    OMAiEMSEWAS.
    OrthoDBiPOG091H09CE.
    PhylomeDBiQ9K498.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13905.

    Miscellaneous databases

    EvolutionaryTraceiQ9K498.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR002401. Cyt_P450_E_grp-I.
    [Graphical view]
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PRINTSiPR00463. EP450I.
    PR00385. P450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiEIZFM_STRCO
    AccessioniPrimary (citable) accession number: Q9K498
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: October 1, 2000
    Last modified: September 7, 2016
    This is version 94 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, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.