ID   FNQ26_STRCM             Reviewed;         300 AA.
AC   A2AXG5;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Flaviolin linalyltransferase {ECO:0000305};
DE            EC=2.5.1.123 {ECO:0000269|PubMed:17543953};
GN   Name=fnq26 {ECO:0000303|PubMed:17103476};
OS   Streptomyces cinnamonensis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces virginiae group.
OX   NCBI_TaxID=1900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN FNQ I BIOSYNTHESIS, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=DSM 1042;
RX   PubMed=17103476; DOI=10.1002/cbic.200600338;
RA   Haagen Y., Gluck K., Fay K., Kammerer B., Gust B., Heide L.;
RT   "A gene cluster for prenylated naphthoquinone and prenylated phenazine
RT   biosynthesis in Streptomyces cinnamonensis DSM 1042.";
RL   ChemBioChem 7:2016-2027(2006).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RC   STRAIN=DSM 1042;
RX   PubMed=17543953; DOI=10.1016/j.febslet.2007.05.031;
RA   Haagen Y., Unsoeld I., Westrich L., Gust B., Richard S.B., Noel J.P.,
RA   Heide L.;
RT   "A soluble, magnesium-independent prenyltransferase catalyzes reverse and
RT   regular C-prenylations and O-prenylations of aromatic substrates.";
RL   FEBS Lett. 581:2889-2893(2007).
CC   -!- FUNCTION: Involved in the biosynthesis of furanonaphthoquinone I (FNQ
CC       I). Catalyzes C- and O-prenylations of different phenolic substrates.
CC       With flaviolin as substrate, catalyzes the formation of a carbon-
CC       carbon-bond between C-3 (rather than C-1) of geranyl diphosphate and C-
CC       3 of flaviolin. With 1,3-dihydroxynaphthalene and 4-hydroxybenzoate as
CC       substrates, catalyzes O-prenylations. {ECO:0000269|PubMed:17103476,
CC       ECO:0000269|PubMed:17543953}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate + flaviolin = 3-linalylflaviolin +
CC         diphosphate; Xref=Rhea:RHEA:17449, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58057, ChEBI:CHEBI:58696, ChEBI:CHEBI:78347;
CC         EC=2.5.1.123; Evidence={ECO:0000269|PubMed:17543953};
CC   -!- ACTIVITY REGULATION: Does not require magnesium or any other divalent
CC       metal ions for activity. {ECO:0000269|PubMed:17543953}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=21 uM for flaviolin {ECO:0000269|PubMed:17543953};
CC         KM=2.1 uM for geranyl diphosphate (with flaviolin as substrate)
CC         {ECO:0000269|PubMed:17543953};
CC         KM=1.9 mM for 1,3-dihydroxynaphthalene {ECO:0000269|PubMed:17543953};
CC         KM=5.6 mM for 4-hydroxybenzoate {ECO:0000269|PubMed:17543953};
CC         Note=kcat is 0.013 min(-1) for flaviolin. kcat is 0.14 min(-1) for 4-
CC         hydroxybenzoate. {ECO:0000269|PubMed:17543953};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17543953}.
CC   -!- DISRUPTION PHENOTYPE: Mutant still produces endophenazine A, but does
CC       not produce FNQ I. {ECO:0000269|PubMed:17103476}.
CC   -!- SIMILARITY: Belongs to the aromatic prenyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AM384985; CAL34104.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2AXG5; -.
DR   SMR; A2AXG5; -.
DR   PRIDE; A2AXG5; -.
DR   KEGG; ag:CAL34104; -.
DR   BRENDA; 2.5.1.123; 5996.
DR   GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   CDD; cd13931; PT-CloQ_NphB; 1.
DR   InterPro; IPR033964; Aro_prenylTrfase.
DR   InterPro; IPR020965; Prenyltransferase_CloQ.
DR   InterPro; IPR036239; PrenylTrfase-like_sf.
DR   Pfam; PF11468; PTase_Orf2; 1.
DR   SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR   SFLD; SFLDG01163; II; 1.
DR   SUPFAM; SSF143492; SSF143492; 1.
PE   1: Evidence at protein level;
KW   Prenyltransferase; Transferase.
FT   CHAIN           1..300
FT                   /note="Flaviolin linalyltransferase"
FT                   /id="PRO_0000430680"
SQ   SEQUENCE   300 AA;  32719 MW;  B2EEE136D68C2FE7 CRC64;
     MMSGTADLAG VYAAVEESAG LLDVSCAREK VWPILAAFED VLPTAVIAFR VATNARHEGE
     FDCRFTVPGS IDPYAVALDK GLTHRSGHPI ETLVADVQKH CAVDSYGVDF GVVGGFKKIW
     VYFPGGRHES LAHLGEIPSM PPGLAATEGF FARYGLADKV DLIGVDYASK TMNVYFAASP
     EVVSAPTVLA MHREIGLPDP SEQMLDFCSR AFGVYTTLNW DSSKVERIAY SVKTEDPLEL
     SARLGSKVEQ FLKSVPYGID TPKMVYAAVT AGGEEYYKLQ SYYQWRTDSR LNLSYIGGRS