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Protein

Biflaviolin synthase CYP158A2

Gene

cyp158a2

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

Functioni

Catalyzes 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

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

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)DescriptionActionsGraphical viewLength
    Sitei87Involved in determining product regiospecificity1 Publication1
    Binding sitei288Flaviolin 1Combined sources2 Publications1
    Binding sitei288Flaviolin 2Combined sources2 Publications1
    Binding sitei293Flaviolin 1; via amide nitrogenCombined sources2 Publications1
    Metal bindingi353Iron (heme axial ligand)Combined sources3 Publications1

    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

    Keywordsi

    Molecular functionMonooxygenase, Oxidoreductase
    LigandHeme, 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)DescriptionActionsGraphical viewLength
    Mutagenesisi87I → K: Catalyzes the formation of two isomers of biflaviolin instead of three. Reduced affinity for flaviolin. 1 Publication1

    Chemistry databases

    DrugBankiDB03814 2-(N-Morpholino)-Ethanesulfonic Acid
    DB03254 4-Phenyl-1h-Imidazole
    DB02175 Malonic acid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004307931 – 404Biflaviolin synthase CYP158A2Add BLAST404

    Interactioni

    Protein-protein interaction databases

    STRINGi100226.SCO1207

    Structurei

    Secondary structure

    1404
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi13 – 15Combined sources3
    Helixi28 – 36Combined sources9
    Beta strandi38 – 43Combined sources6
    Beta strandi45 – 49Combined sources5
    Beta strandi51 – 54Combined sources4
    Helixi57 – 64Combined sources8
    Beta strandi69 – 71Combined sources3
    Turni72 – 78Combined sources7
    Beta strandi81 – 85Combined sources5
    Beta strandi90 – 92Combined sources3
    Helixi93 – 95Combined sources3
    Helixi100 – 112Combined sources13
    Helixi114 – 138Combined sources25
    Beta strandi140 – 143Combined sources4
    Helixi144 – 147Combined sources4
    Turni148 – 150Combined sources3
    Helixi151 – 161Combined sources11
    Helixi165 – 167Combined sources3
    Helixi168 – 182Combined sources15
    Beta strandi183 – 186Combined sources4
    Helixi189 – 192Combined sources4
    Helixi194 – 204Combined sources11
    Turni206 – 208Combined sources3
    Helixi214 – 223Combined sources10
    Helixi229 – 242Combined sources14
    Helixi245 – 259Combined sources15
    Helixi261 – 269Combined sources9
    Helixi271 – 273Combined sources3
    Helixi274 – 284Combined sources11
    Beta strandi288 – 290Combined sources3
    Beta strandi295 – 299Combined sources5
    Beta strandi301 – 303Combined sources3
    Beta strandi306 – 308Combined sources3
    Beta strandi313 – 316Combined sources4
    Helixi318 – 321Combined sources4
    Turni325 – 327Combined sources3
    Beta strandi328 – 330Combined sources3
    Helixi356 – 373Combined sources18
    Beta strandi378 – 381Combined sources4
    Helixi383 – 385Combined sources3
    Beta strandi401 – 403Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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
    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
    OrthoDBiPOG091H0API
    PhylomeDBiQ9FCA6

    Family and domain databases

    Gene3Di1.10.630.10, 1 hit
    InterProiView protein in InterPro
    IPR001128 Cyt_P450
    IPR002397 Cyt_P450_B
    IPR017972 Cyt_P450_CS
    IPR036396 Cyt_P450_sf
    PfamiView protein in Pfam
    PF00067 p450, 1 hit
    PRINTSiPR00359 BP450
    SUPFAMiSSF48264 SSF48264, 1 hit
    PROSITEiView protein in PROSITE
    PS00086 CYTOCHROME_P450, 1 hit

    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
    29664198
    KEGGisco:SCO1207
    PATRICifig|100226.15.peg.1206

    Similar proteinsi

    Entry informationi

    Entry nameiC1582_STRCO
    AccessioniPrimary (citable) accession number: Q9FCA6
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 29, 2014
    Last sequence update: March 1, 2001
    Last modified: March 28, 2018
    This is version 111 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health