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Protein

Biflaviolin synthase CYP158A2

Gene

cyp158a2

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

Catalyze oxidative C-C coupling reaction to polymerize flaviolin and form highly conjugated pigments which protect the soil bacterium from deleterious effects of UV irradiation (three isomers of biflaviolin and one triflaviolin).2 Publications

Catalytic activityi

2 flaviolin + NADPH + O2 = 3,3'-biflaviolin + NADP+ + 2 H2O.3 Publications
2 flaviolin + NADPH + O2 = 3,8'-biflaviolin + NADP+ + 2 H2O.3 Publications

Cofactori

heme3 Publications

Kineticsi

kcat is 1.4 min(-1) with flaviolin as substrate (at pH 7.5 and 37 degrees Celsius). kcat is 0.02 min(-1) with 2-hydroxy-1,4-naphthoquinone as substrate (at pH 7.5 and 25 degrees Celsius).2 Publications

  1. KM=7.3 µM for flaviolin (at pH 8.2 and 37 degrees Celsius)1 Publication

    Pathwayi: Pigment biosynthesis

    This protein is involved in Pigment biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in Pigment biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei87 – 871Involved in determining product regiospecificity1 Publication
    Binding sitei288 – 2881Flaviolin 1Combined sources2 Publications
    Binding sitei288 – 2881Flaviolin 2Combined sources2 Publications
    Binding sitei293 – 2931Flaviolin 1; via amide nitrogenCombined sources2 Publications
    Metal bindingi353 – 3531Iron (heme axial ligand)Combined sources3 Publications

    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: UniProtKB

    GO - Biological processi

    • oxidation-reduction process Source: UniProtKB
    • pigment metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    Heme, Iron, Metal-binding, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14458.
    BRENDAi1.14.21.7. 5998.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Biflaviolin synthase CYP158A2 (EC:1.14.21.73 Publications)
    Alternative name(s):
    Cytochrome P450 158A21 Publication
    Short name:
    CYP158A21 Publication
    Gene namesi
    Name:cyp158a21 Publication
    Ordered Locus Names:SCO1207Imported
    OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
    Taxonomic identifieri100226 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
    Proteomesi
    • UP000001973 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi87 – 871I → K: Catalyzes the formation of two isomers of biflaviolin instead of three. Reduced affinity for flaviolin. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 404404Biflaviolin synthase CYP158A2PRO_0000430793Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi100226.SCO1207.

    Structurei

    Secondary structure

    1
    404
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 153Combined sources
    Helixi28 – 369Combined sources
    Beta strandi38 – 436Combined sources
    Beta strandi45 – 495Combined sources
    Beta strandi51 – 544Combined sources
    Helixi57 – 648Combined sources
    Beta strandi69 – 713Combined sources
    Turni72 – 787Combined sources
    Beta strandi81 – 855Combined sources
    Beta strandi90 – 923Combined sources
    Helixi93 – 953Combined sources
    Helixi100 – 11213Combined sources
    Helixi114 – 13825Combined sources
    Beta strandi140 – 1434Combined sources
    Helixi144 – 1474Combined sources
    Turni148 – 1503Combined sources
    Helixi151 – 16111Combined sources
    Helixi165 – 1673Combined sources
    Helixi168 – 18215Combined sources
    Beta strandi183 – 1864Combined sources
    Helixi189 – 1924Combined sources
    Helixi194 – 20411Combined sources
    Turni206 – 2083Combined sources
    Helixi214 – 22310Combined sources
    Helixi229 – 24214Combined sources
    Helixi245 – 25915Combined sources
    Helixi261 – 2699Combined sources
    Helixi271 – 2733Combined sources
    Helixi274 – 28411Combined sources
    Beta strandi288 – 2903Combined sources
    Beta strandi295 – 2995Combined sources
    Beta strandi301 – 3033Combined sources
    Beta strandi306 – 3083Combined sources
    Beta strandi313 – 3164Combined sources
    Helixi318 – 3214Combined sources
    Turni325 – 3273Combined sources
    Beta strandi328 – 3303Combined sources
    Helixi356 – 37318Combined sources
    Beta strandi378 – 3814Combined sources
    Helixi383 – 3853Combined sources
    Beta strandi401 – 4033Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1S1FX-ray1.50A1-404[»]
    1SE6X-ray1.75A/B1-404[»]
    1T93X-ray1.62A1-404[»]
    2D09X-ray1.80A1-404[»]
    2D0EX-ray2.15A1-404[»]
    3TZOX-ray1.76A/B1-404[»]
    5DE9X-ray1.76A/B1-404[»]
    ProteinModelPortaliQ9FCA6.
    SMRiQ9FCA6. Positions 4-404.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9FCA6.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4106A3M. Bacteria.
    COG2124. LUCA.
    HOGENOMiHOG000243678.
    InParanoidiQ9FCA6.
    KOiK13074.
    OMAiIPHRNAV.
    OrthoDBiEOG6JB11P.
    PhylomeDBiQ9FCA6.

    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.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9FCA6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTEETISQAV PPVRDWPAVD LPGSDFDPVL TELMREGPVT RISLPNGEGW
    60 70 80 90 100
    AWLVTRHDDV RLVTNDPRFG REAVMDRQVT RLAPHFIPAR GAVGFLDPPD
    110 120 130 140 150
    HTRLRRSVAA AFTARGVERV RERSRGMLDE LVDAMLRAGP PADLTEAVLS
    160 170 180 190 200
    PFPIAVICEL MGVPATDRHS MHTWTQLILS SSHGAEVSER AKNEMNAYFS
    210 220 230 240 250
    DLIGLRSDSA GEDVTSLLGA AVGRDEITLS EAVGLAVLLQ IGGEAVTNNS
    260 270 280 290 300
    GQMFHLLLSR PELAERLRSE PEIRPRAIDE LLRWIPHRNA VGLSRIALED
    310 320 330 340 350
    VEIKGVRIRA GDAVYVSYLA ANRDPEVFPD PDRIDFERSP NPHVSFGFGP
    360 370 380 390 400
    HYCPGGMLAR LESELLVDAV LDRVPGLKLA VAPEDVPFKK GALIRGPEAL

    PVTW
    Length:404
    Mass (Da):44,355
    Last modified:March 1, 2001 - v1
    Checksum:iD195F5C42B0A8E2B
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL939108 Genomic DNA. Translation: CAC01489.1.
    RefSeqiNP_625496.1. NC_003888.3.
    WP_003977624.1. NC_003888.3.

    Genome annotation databases

    EnsemblBacteriaiCAC01489; CAC01489; CAC01489.
    GeneIDi1096630.
    KEGGisco:SCO1207.
    PATRICi23731966. VBIStrCoe124346_1206.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL939108 Genomic DNA. Translation: CAC01489.1.
    RefSeqiNP_625496.1. NC_003888.3.
    WP_003977624.1. NC_003888.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1S1FX-ray1.50A1-404[»]
    1SE6X-ray1.75A/B1-404[»]
    1T93X-ray1.62A1-404[»]
    2D09X-ray1.80A1-404[»]
    2D0EX-ray2.15A1-404[»]
    3TZOX-ray1.76A/B1-404[»]
    5DE9X-ray1.76A/B1-404[»]
    ProteinModelPortaliQ9FCA6.
    SMRiQ9FCA6. Positions 4-404.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi100226.SCO1207.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAC01489; CAC01489; CAC01489.
    GeneIDi1096630.
    KEGGisco:SCO1207.
    PATRICi23731966. VBIStrCoe124346_1206.

    Phylogenomic databases

    eggNOGiENOG4106A3M. Bacteria.
    COG2124. LUCA.
    HOGENOMiHOG000243678.
    InParanoidiQ9FCA6.
    KOiK13074.
    OMAiIPHRNAV.
    OrthoDBiEOG6JB11P.
    PhylomeDBiQ9FCA6.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14458.
    BRENDAi1.14.21.7. 5998.

    Miscellaneous databases

    EvolutionaryTraceiQ9FCA6.

    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.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-471 / A3(2) / M145Imported.
    2. "Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2."
      Zhao B., Guengerich F.P., Bellamine A., Lamb D.C., Izumikawa M., Lei L., Podust L.M., Sundaramoorthy M., Kalaitzis J.A., Reddy L.M., Kelly S.L., Moore B.S., Stec D., Voehler M., Falck J.R., Shimada T., Waterman M.R.
      J. Biol. Chem. 280:11599-11607(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH HEME AND SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    3. "Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer."
      Zhao B., Guengerich F.P., Voehler M., Waterman M.R.
      J. Biol. Chem. 280:42188-42197(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH HEME AND SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PROTON WIRE.
    4. "The role of Ile87 of CYP158A2 in oxidative coupling reaction."
      Zhao B., Bellamine A., Lei L., Waterman M.R.
      Arch. Biochem. Biophys. 518:127-132(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH HEME, MUTAGENESIS OF ILE-87, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, REGIOSPECIFICITY SITE.

    Entry informationi

    Entry nameiC1582_STRCO
    AccessioniPrimary (citable) accession number: Q9FCA6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 29, 2014
    Last sequence update: March 1, 2001
    Last modified: December 9, 2015
    This is version 100 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The structural studies suggest catalysis likely occurs through proton relay via a "proton wire" formed by water molecules in the active site.2 Publications

    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.