CYC2_KITGR
ID CYC2_KITGR Reviewed; 311 AA.
AC Q9AJE3;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Terpentetriene synthase;
DE EC=4.2.3.36;
GN Name=cyc2;
OS Kitasatospora griseola (Streptomyces griseolosporeus).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Kitasatospora.
OX NCBI_TaxID=2064;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=MF730-N6;
RX PubMed=11567009; DOI=10.1128/jb.183.20.6085-6094.2001;
RA Dairi T., Hamano Y., Kuzuyama T., Itoh N., Furihata K., Seto H.;
RT "Eubacterial diterpene cyclase genes essential for production of the
RT isoprenoid antibiotic terpentecin.";
RL J. Bacteriol. 183:6085-6094(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, AND SUBUNIT.
RC STRAIN=MF730-N6;
RX PubMed=12138123; DOI=10.1074/jbc.m206382200;
RA Hamano Y., Kuzuyama T., Itoh N., Furihata K., Seto H., Dairi T.;
RT "Functional analysis of eubacterial diterpene cyclases responsible for
RT biosynthesis of a diterpene antibiotic, terpentecin.";
RL J. Biol. Chem. 277:37098-37104(2002).
CC -!- FUNCTION: Involved in the production of the isoprenoid antibiotic
CC terpentecin. Converts terpentedienol diphosphate (TDP) into
CC terpentetriene (TTE). Can also accept geranylgeranyl diphosphate (GGDP)
CC and farnesyl diphosphate (FDP) as substrates.
CC {ECO:0000269|PubMed:12138123}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=terpentedienyl diphosphate = diphosphate + terpentetriene;
CC Xref=Rhea:RHEA:25617, ChEBI:CHEBI:33019, ChEBI:CHEBI:50302,
CC ChEBI:CHEBI:58821; EC=4.2.3.36;
CC Evidence={ECO:0000269|PubMed:12138123};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12138123};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.6 uM for TDP {ECO:0000269|PubMed:12138123};
CC KM=7.9 uM for GGDP {ECO:0000269|PubMed:12138123};
CC KM=61.7 uM for FDP {ECO:0000269|PubMed:12138123};
CC Vmax=114.6 nmol/min/mg enzyme with TDP as substrate
CC {ECO:0000269|PubMed:12138123};
CC Vmax=8.8 nmol/min/mg enzyme with GGDP as substrate
CC {ECO:0000269|PubMed:12138123};
CC Vmax=15.9 nmol/min/mg enzyme with FDP as substrate
CC {ECO:0000269|PubMed:12138123};
CC pH dependence:
CC Optimum pH is 6.8. {ECO:0000269|PubMed:12138123};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:12138123};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:11567009,
CC ECO:0000269|PubMed:12138123}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12138123}.
CC -!- DISRUPTION PHENOTYPE: Mutants do not produce terpentecin.
CC {ECO:0000269|PubMed:11567009}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; AB048795; BAB39207.1; -; Genomic_DNA.
DR RefSeq; WP_043911627.1; NZ_JXZB01000002.1.
DR AlphaFoldDB; Q9AJE3; -.
DR SMR; Q9AJE3; -.
DR KEGG; ag:BAB39207; -.
DR BRENDA; 4.2.3.36; 6030.
DR BRENDA; 4.2.3.B26; 6030.
DR BRENDA; 4.2.3.B27; 6030.
DR BRENDA; 4.2.3.B28; 6030.
DR BRENDA; 4.2.3.B29; 6030.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052679; F:terpentetriene synthase activity; IDA:UniProtKB.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..311
FT /note="Terpentetriene synthase"
FT /id="PRO_0000418818"
FT MOTIF 77..81
FT /note="DDXXD motif"
SQ SEQUENCE 311 AA; 34773 MW; 7D4E9C942B6EB9A2 CRC64;
MPDAIEFEHE GRRNPNSAEA ESAYSSIIAA LDLQESDYAV ISGHSRIVGA AALVYPDADA
ETLLAASLWT ACLIVNDDRW DYVQEDGGRL APGEWFDGVT EVVDTWRTAG PRLPDPFFEL
VRTTMSRLDA ALGAEAADEI GHEIKRAITA MKWEGVWNEY TKKTSLATYL SFRRGYCTMD
VQVVLDKWIN GGRSFAALRD DPVRRAIDDV VVRFGCLSND YYSWGREKKA VDKSNAVRIL
MDHAGYDEST ALAHVRDDCV QAITDLDCIE ESIKRSGHLG SHAQELLDYL ACHRPLIYAA
ATWPTETNRY R