C1581_STRCO
ID C1581_STRCO Reviewed; 407 AA.
AC Q9KZF5;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Biflaviolin synthase CYP158A1 {ECO:0000305};
DE EC=1.14.19.69 {ECO:0000269|PubMed:17614370, ECO:0000269|PubMed:22203090};
DE AltName: Full=Cytochrome P450 158A1 {ECO:0000303|PubMed:17614370};
DE Short=CYP158A1 {ECO:0000303|PubMed:17614370};
GN Name=cyp158a1 {ECO:0000303|PubMed:17614370};
GN OrderedLocusNames=SCO6998 {ECO:0000312|EMBL:CAB88975.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP MUTAGENESIS OF LYS-90, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY,
RP AND REGIOSPECIFICITY SITE.
RX PubMed=22203090; DOI=10.1016/j.abb.2011.12.007;
RA Zhao B., Bellamine A., Lei L., Waterman M.R.;
RT "The role of Ile87 of CYP158A2 in oxidative coupling reaction.";
RL Arch. Biochem. Biophys. 518:127-132(2012).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) IN COMPLEX WITH HEME AND FLAVIOLIN
RP ANALOG, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RX PubMed=17614370; DOI=10.1021/bi7006959;
RA Zhao B., Lamb D.C., Lei L., Kelly S.L., Yuan H., Hachey D.L.,
RA Waterman M.R.;
RT "Different binding modes of two flaviolin substrate molecules in cytochrome
RT P450 158A1 (CYP158A1) compared to CYP158A2.";
RL Biochemistry 46:8725-8733(2007).
CC -!- FUNCTION: Catalyzes oxidative C-C coupling reaction to polymerize
CC flaviolin and form highly conjugated pigments which protect the soil
CC bacterium from deleterious effects of UV irradiation (two isomers of
CC biflaviolin and one triflaviolin). {ECO:0000269|PubMed:17614370}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 flaviolin + H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] =
CC 3,3'-biflaviolin + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:26031, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:58696,
CC ChEBI:CHEBI:77877; EC=1.14.19.69;
CC Evidence={ECO:0000269|PubMed:17614370, ECO:0000269|PubMed:22203090};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 flaviolin + H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] =
CC 3,8'-biflaviolin + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:26035, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:58696,
CC ChEBI:CHEBI:77840; EC=1.14.19.69;
CC Evidence={ECO:0000269|PubMed:17614370, ECO:0000269|PubMed:22203090};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:17614370};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.5 uM for flaviolin (at pH 8.2 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:22203090};
CC Note=kcat is 0.9 min(-1) with flaviolin as substrate (at pH 8.2 and
CC 37 degrees Celsius). {ECO:0000269|PubMed:17614370};
CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000303|PubMed:17614370}.
CC -!- MISCELLANEOUS: The structural studies suggest catalysis likely occurs
CC through proton relay via a 'proton wire' formed by water molecules in
CC the active site. {ECO:0000250|UniProtKB:Q9FCA6}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AL939130; CAB88975.1; -; Genomic_DNA.
DR RefSeq; NP_631063.1; NC_003888.3.
DR RefSeq; WP_011031367.1; NZ_VNID01000012.1.
DR PDB; 2DKK; X-ray; 1.97 A; A=1-407.
DR PDB; 2NZ5; X-ray; 2.35 A; A/B=1-407.
DR PDB; 2NZA; X-ray; 2.90 A; A/B=1-407.
DR PDBsum; 2DKK; -.
DR PDBsum; 2NZ5; -.
DR PDBsum; 2NZA; -.
DR AlphaFoldDB; Q9KZF5; -.
DR SMR; Q9KZF5; -.
DR STRING; 100226.SCO6998; -.
DR GeneID; 1102436; -.
DR KEGG; sco:SCO6998; -.
DR PATRIC; fig|100226.15.peg.7100; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_033716_1_1_11; -.
DR InParanoid; Q9KZF5; -.
DR OMA; MREGPLT; -.
DR PhylomeDB; Q9KZF5; -.
DR BioCyc; MetaCyc:MON-18705; -.
DR BRENDA; 1.14.19.69; 5998.
DR EvolutionaryTrace; Q9KZF5; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0004497; F:monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IDA:UniProtKB.
DR GO; GO:0042440; P:pigment metabolic process; IDA:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002397; Cyt_P450_B.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00359; BP450.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..407
FT /note="Biflaviolin synthase CYP158A1"
FT /id="PRO_0000430792"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 92
FT /ligand="flaviolin"
FT /ligand_id="ChEBI:CHEBI:58696"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17614370,
FT ECO:0007744|PDB:2NZ5"
FT BINDING 199
FT /ligand="flaviolin"
FT /ligand_id="ChEBI:CHEBI:58696"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17614370,
FT ECO:0007744|PDB:2NZ5"
FT BINDING 290..291
FT /ligand="flaviolin"
FT /ligand_id="ChEBI:CHEBI:58696"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17614370,
FT ECO:0007744|PDB:2NZ5"
FT BINDING 356
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:17614370,
FT ECO:0007744|PDB:2DKK, ECO:0007744|PDB:2NZ5,
FT ECO:0007744|PDB:2NZA"
FT SITE 90
FT /note="Involved in determining product regiospecificity"
FT /evidence="ECO:0000269|PubMed:22203090"
FT MUTAGEN 90
FT /note="K->I: Normal activity. Reduced affinity for
FT flaviolin."
FT /evidence="ECO:0000269|PubMed:22203090"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:2DKK"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:2DKK"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:2DKK"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:2DKK"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:2DKK"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:2DKK"
FT HELIX 60..66
FT /evidence="ECO:0007829|PDB:2DKK"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2DKK"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:2DKK"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:2DKK"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:2NZA"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:2DKK"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:2DKK"
FT HELIX 117..141
FT /evidence="ECO:0007829|PDB:2DKK"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:2DKK"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:2DKK"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:2DKK"
FT HELIX 170..178
FT /evidence="ECO:0007829|PDB:2DKK"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:2DKK"
FT HELIX 189..207
FT /evidence="ECO:0007829|PDB:2DKK"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:2DKK"
FT HELIX 217..226
FT /evidence="ECO:0007829|PDB:2DKK"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:2NZA"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:2DKK"
FT HELIX 246..262
FT /evidence="ECO:0007829|PDB:2DKK"
FT HELIX 264..272
FT /evidence="ECO:0007829|PDB:2DKK"
FT HELIX 278..287
FT /evidence="ECO:0007829|PDB:2DKK"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:2DKK"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:2DKK"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:2DKK"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:2DKK"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:2DKK"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:2DKK"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:2DKK"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:2DKK"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:2NZA"
FT HELIX 359..376
FT /evidence="ECO:0007829|PDB:2DKK"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:2DKK"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:2DKK"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:2DKK"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:2DKK"
SQ SEQUENCE 407 AA; 44701 MW; 1FDD5A5496DB0DBE CRC64;
MTQETTTLTG QSPPPVRDWP ALDLDGPEFD PVLAELMREG PLTRVRLPHG EGWAWLATRY
DDVKAITNDP RFGRAEVTQR QITRLAPHFK PRPGSLAFAD QPDHNRLRRA VAGAFTVGAT
KRLRPRAQEI LDGLVDGILA EGPPADLVER VLEPFPIAVV SEVMGVPAAD RERVHSWTRQ
IISTSGGAEA AERAKRGLYG WITETVRARA GSEGGDVYSM LGAAVGRGEV GETEAVGLAG
PLQIGGEAVT HNVGQMLYLL LTRRELMARM RERPGARGTA LDELLRWISH RTSVGLARIA
LEDVEVHGTR IAAGEPVYVS YLAANRDPDV FPDPDRIDLD RDPNPHLAYG NGHHFCTGAV
LARMQTELLV DTLLERLPGL RLAVPAEQVA WRRKTMIRGP RTLPCTW
