FUR7_STREO
ID FUR7_STREO Reviewed; 307 AA.
AC Q2L6E3;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Furaquinocin biosynthesis prenyltransferase {ECO:0000305};
DE EC=2.5.1.124 {ECO:0000269|PubMed:20937800};
DE EC=2.5.1.125 {ECO:0000269|PubMed:20937800};
DE AltName: Full=6-linalyl-2-O,3-dimethylflaviolin synthase {ECO:0000305};
DE AltName: Full=7-geranyloxy-5-hydroxy-2-methoxy-3-methylnaphthalene-1,4-dione synthase {ECO:0000305};
GN Name=fur7 {ECO:0000303|PubMed:20937800};
OS Streptomyces sp. (strain KO-3988).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=285219;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KO-3988;
RX PubMed=16452404; DOI=10.1128/jb.188.4.1236-1244.2006;
RA Kawasaki T., Hayashi Y., Kuzuyama T., Furihata K., Itoh N., Seto H.,
RA Dairi T.;
RT "Biosynthesis of a natural polyketide-isoprenoid hybrid compound,
RT furaquinocin A: identification and heterologous expression of the gene
RT cluster.";
RL J. Bacteriol. 188:1236-1244(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=KO-3988;
RX PubMed=20937800; DOI=10.1074/jbc.m110.153957;
RA Kumano T., Tomita T., Nishiyama M., Kuzuyama T.;
RT "Functional characterization of the promiscuous prenyltransferase
RT responsible for furaquinocin biosynthesis: identification of a
RT physiological polyketide substrate and its prenylated reaction products.";
RL J. Biol. Chem. 285:39663-39671(2010).
CC -!- FUNCTION: Involved in the biosynthesis of furaquinocin. Catalyzes the
CC transfer of a geranyl group to 2-methoxy-3-methyl-flaviolin to yield 6-
CC prenyl-2-methoxy-3-methyl-flaviolin and 7-O-geranyl-2-methoxy-3-methyl-
CC flaviolin in a 10:1 ratio. Can also use other substrates such as
CC flaviolin or 1,3-dihydroxy naphthalene, and can also use DMAPP as
CC prenyl donor. {ECO:0000269|PubMed:20937800}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + 2-O,3-dimethylflaviolin = 6-
CC linalyl-2-O,3-dimethylflaviolin + diphosphate; Xref=Rhea:RHEA:41007,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:78588,
CC ChEBI:CHEBI:78589; EC=2.5.1.124;
CC Evidence={ECO:0000269|PubMed:20937800};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + 2-O,3-dimethylflaviolin + H(+) = 7-
CC O-geranyl-2-O,3-dimethylflaviolin + diphosphate;
CC Xref=Rhea:RHEA:33839, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057, ChEBI:CHEBI:78589, ChEBI:CHEBI:78590;
CC EC=2.5.1.125; Evidence={ECO:0000269|PubMed:20937800};
CC -!- ACTIVITY REGULATION: Does not require any metal cations for activity.
CC {ECO:0000269|PubMed:20937800}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.054 mM for 6-prenyl-2-methoxy-3-methyl-flaviolin
CC {ECO:0000269|PubMed:20937800};
CC KM=0.098 mM for geranyl diphosphate {ECO:0000269|PubMed:20937800};
CC Vmax=1.1 nmol/min/mg enzyme {ECO:0000269|PubMed:20937800};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20937800}.
CC -!- SIMILARITY: Belongs to the aromatic prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB212624; BAE78975.1; -; Genomic_DNA.
DR EMBL; AB187171; BAF02319.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2L6E3; -.
DR SMR; Q2L6E3; -.
DR KEGG; ag:BAF02319; -.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IDA:UniProtKB.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
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 Isoprene biosynthesis; Prenyltransferase; Transferase.
FT CHAIN 1..307
FT /note="Furaquinocin biosynthesis prenyltransferase"
FT /id="PRO_0000431583"
SQ SEQUENCE 307 AA; 34248 MW; 7338EA5E4372414D CRC64;
MPGTDDVAVD VASVYSAIEK SAGLLDVTAA REVVWPVLTA FEDVLEQAVI AFRVATNARH
EGDFDVRFTV PEEVDPYAVA LSRSLIAKTD HPVGSLLSDI QQLCSVDTYG VDLGVKSGFK
KVWVYFPAGE HETLARLTGL TSMPGSLAGN VDFFTRYGLA DKVDVIGIDY RSRTMNVYFA
APSECFERET VLAMHRDIGL PSPSEQMFKF CENSFGLYTT LNWDTMEIER ISYGVKTENP
MTFFARLGTK VEHFVKNVPY GVDTQKMVYA AVTSSGEEYY KLQSYYRWRS VSRLNAAYIA
ARDKEST
