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

Biflaviolin synthase CYP158A1

Gene

cyp158a1

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 (two isomers of biflaviolin and one triflaviolin).1 Publication

Catalytic activityi

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

Cofactori

heme1 Publication

Kineticsi

kcat is 0.9 min(-1) with flaviolin as substrate (at pH 8.2 and 37 degrees Celsius).1 Publication

Manual assertion based on experiment ini

  1. KM=10.5 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
    Sitei90Involved in determining product regiospecificity1 Publication1
    Binding sitei92Flaviolin 1Combined sources1 Publication1
    Binding sitei199Flaviolin 1Combined sources1 Publication1
    Metal bindingi356Iron (heme axial ligand)Combined sources1 Publication1

    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-18705.
    BRENDAi1.14.21.7. 5998.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Biflaviolin synthase CYP158A1Curated (EC:1.14.21.72 Publications)
    Alternative name(s):
    Cytochrome P450 158A11 Publication
    Short name:
    CYP158A11 Publication
    Gene namesi
    Name:cyp158a11 Publication
    Ordered Locus Names:SCO6998Imported
    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
    Mutagenesisi90K → I: Normal activity. Reduced affinity for flaviolin. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004307921 – 407Biflaviolin synthase CYP158A1Add BLAST407

    Interactioni

    Protein-protein interaction databases

    STRINGi100226.SCO6998.

    Structurei

    Secondary structure

    1407
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi16 – 18Combined sources3
    Beta strandi25 – 27Combined sources3
    Helixi31 – 37Combined sources7
    Beta strandi41 – 46Combined sources6
    Beta strandi48 – 52Combined sources5
    Beta strandi54 – 57Combined sources4
    Helixi60 – 66Combined sources7
    Beta strandi72 – 74Combined sources3
    Helixi75 – 79Combined sources5
    Beta strandi84 – 87Combined sources4
    Helixi96 – 98Combined sources3
    Helixi103 – 111Combined sources9
    Helixi112 – 114Combined sources3
    Helixi117 – 141Combined sources25
    Helixi147 – 150Combined sources4
    Turni151 – 153Combined sources3
    Helixi154 – 164Combined sources11
    Helixi170 – 178Combined sources9
    Helixi179 – 181Combined sources3
    Helixi189 – 207Combined sources19
    Turni208 – 211Combined sources4
    Helixi217 – 226Combined sources10
    Beta strandi232 – 234Combined sources3
    Helixi235 – 244Combined sources10
    Helixi246 – 262Combined sources17
    Helixi264 – 272Combined sources9
    Helixi278 – 287Combined sources10
    Beta strandi291 – 293Combined sources3
    Beta strandi298 – 302Combined sources5
    Beta strandi304 – 306Combined sources3
    Beta strandi309 – 311Combined sources3
    Beta strandi316 – 319Combined sources4
    Helixi321 – 324Combined sources4
    Turni328 – 330Combined sources3
    Beta strandi331 – 333Combined sources3
    Helixi352 – 354Combined sources3
    Helixi359 – 376Combined sources18
    Beta strandi381 – 384Combined sources4
    Helixi386 – 388Combined sources3
    Beta strandi394 – 397Combined sources4
    Beta strandi404 – 406Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2DKKX-ray1.97A1-407[»]
    2NZ5X-ray2.35A/B1-407[»]
    2NZAX-ray2.90A/B1-407[»]
    ProteinModelPortaliQ9KZF5.
    SMRiQ9KZF5.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9KZF5.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni290 – 291Flaviolin 2 bindingCombined sources1 Publication2

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Phylogenomic databases

    eggNOGiENOG4106A3M. Bacteria.
    COG2124. LUCA.
    HOGENOMiHOG000243678.
    InParanoidiQ9KZF5.
    KOiK19628.
    OrthoDBiPOG091H0API.
    PhylomeDBiQ9KZF5.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR002397. Cyt_P450_B.
    [Graphical view]
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PRINTSiPR00359. BP450.
    SUPFAMiSSF48264. SSF48264. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9KZF5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTQETTTLTG QSPPPVRDWP ALDLDGPEFD PVLAELMREG PLTRVRLPHG
    60 70 80 90 100
    EGWAWLATRY DDVKAITNDP RFGRAEVTQR QITRLAPHFK PRPGSLAFAD
    110 120 130 140 150
    QPDHNRLRRA VAGAFTVGAT KRLRPRAQEI LDGLVDGILA EGPPADLVER
    160 170 180 190 200
    VLEPFPIAVV SEVMGVPAAD RERVHSWTRQ IISTSGGAEA AERAKRGLYG
    210 220 230 240 250
    WITETVRARA GSEGGDVYSM LGAAVGRGEV GETEAVGLAG PLQIGGEAVT
    260 270 280 290 300
    HNVGQMLYLL LTRRELMARM RERPGARGTA LDELLRWISH RTSVGLARIA
    310 320 330 340 350
    LEDVEVHGTR IAAGEPVYVS YLAANRDPDV FPDPDRIDLD RDPNPHLAYG
    360 370 380 390 400
    NGHHFCTGAV LARMQTELLV DTLLERLPGL RLAVPAEQVA WRRKTMIRGP

    RTLPCTW
    Length:407
    Mass (Da):44,701
    Last modified:October 1, 2000 - v1
    Checksum:i1FDD5A5496DB0DBE
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL939130 Genomic DNA. Translation: CAB88975.1.
    RefSeqiNP_631063.1. NC_003888.3.
    WP_011031367.1. NC_003888.3.

    Genome annotation databases

    EnsemblBacteriaiCAB88975; CAB88975; CAB88975.
    GeneIDi1102436.
    KEGGisco:SCO6998.
    PATRICi23743915. VBIStrCoe124346_7100.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL939130 Genomic DNA. Translation: CAB88975.1.
    RefSeqiNP_631063.1. NC_003888.3.
    WP_011031367.1. NC_003888.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2DKKX-ray1.97A1-407[»]
    2NZ5X-ray2.35A/B1-407[»]
    2NZAX-ray2.90A/B1-407[»]
    ProteinModelPortaliQ9KZF5.
    SMRiQ9KZF5.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi100226.SCO6998.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB88975; CAB88975; CAB88975.
    GeneIDi1102436.
    KEGGisco:SCO6998.
    PATRICi23743915. VBIStrCoe124346_7100.

    Phylogenomic databases

    eggNOGiENOG4106A3M. Bacteria.
    COG2124. LUCA.
    HOGENOMiHOG000243678.
    InParanoidiQ9KZF5.
    KOiK19628.
    OrthoDBiPOG091H0API.
    PhylomeDBiQ9KZF5.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-18705.
    BRENDAi1.14.21.7. 5998.

    Miscellaneous databases

    EvolutionaryTraceiQ9KZF5.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR002397. Cyt_P450_B.
    [Graphical view]
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PRINTSiPR00359. BP450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiC1581_STRCO
    AccessioniPrimary (citable) accession number: Q9KZF5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 29, 2014
    Last sequence update: October 1, 2000
    Last modified: November 2, 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

    Miscellaneous

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

    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.