CYC1_STRCO
ID CYC1_STRCO Reviewed; 361 AA.
AC Q9K499;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Epi-isozizaene synthase;
DE Short=EIZS;
DE EC=4.2.3.37;
DE AltName: Full=Sesquiterpene cyclase;
DE AltName: Full=Sesquiterpene synthase;
GN Name=cyc1; OrderedLocusNames=SCO5222; ORFNames=SC7E4.19;
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 FUNCTION, COFACTOR, KINETIC PARAMETERS, REACTION MECHANISM, AND REACTION
RP STEREOCHEMISTRY.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=16669656; DOI=10.1021/ja061292s;
RA Lin X., Hopson R., Cane D.E.;
RT "Genome mining in Streptomyces coelicolor. Molecular cloning and
RT characterization of a new sesquiterpene synthase.";
RL J. Am. Chem. Soc. 128:6022-6023(2006).
CC -!- FUNCTION: Catalyzes the cyclization of farnesyl diphosphate (FPP) to
CC the sesquiterpene epi-isozizaene. {ECO:0000269|PubMed:16669656}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-epi-isozizaene +
CC diphosphate; Xref=Rhea:RHEA:25992, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:51458, ChEBI:CHEBI:175763; EC=4.2.3.37;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16669656};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16669656};
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000269|PubMed:16669656};
CC Note=Binds 3 Mg(2+) ions per subunit. Can also use Mn(2+) and Fe(3+)
CC but less efficiently, and other divalent cations such as Zn(2+),
CC Fe(2+), Co(2+), Cu(2+) and Ni(2+) are nearly completely inefficient as
CC cofactors. {ECO:0000269|PubMed:16669656};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=147 nM for FPP {ECO:0000269|PubMed:16669656};
CC -!- PATHWAY: Sesquiterpene biosynthesis; epi-isozizaene biosynthesis.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL939123; CAB94607.1; -; Genomic_DNA.
DR RefSeq; NP_629369.1; NC_003888.3.
DR RefSeq; WP_011030119.1; NZ_VNID01000008.1.
DR PDB; 3KB9; X-ray; 1.60 A; A=2-361.
DR PDB; 3KBK; X-ray; 1.90 A; A=2-361.
DR PDB; 3LG5; X-ray; 1.64 A; A=1-361.
DR PDB; 3LGK; X-ray; 1.89 A; A=2-361.
DR PDB; 4LTV; X-ray; 2.40 A; A=2-361.
DR PDB; 4LTZ; X-ray; 2.45 A; A=2-361.
DR PDB; 4LUU; X-ray; 1.95 A; A=2-361.
DR PDB; 4LXW; X-ray; 2.09 A; A=2-361.
DR PDB; 4LZ0; X-ray; 1.75 A; A=2-361.
DR PDB; 4LZ3; X-ray; 2.10 A; A=2-361.
DR PDB; 4LZC; X-ray; 2.46 A; A=2-361.
DR PDB; 6AX9; X-ray; 2.40 A; A=2-361.
DR PDB; 6AXM; X-ray; 1.80 A; A=2-361.
DR PDB; 6AXN; X-ray; 1.90 A; A=2-361.
DR PDB; 6AXO; X-ray; 2.10 A; A=2-361.
DR PDB; 6AXU; X-ray; 1.82 A; A=2-361.
DR PDB; 6OFV; X-ray; 1.91 A; A=1-361.
DR PDB; 7KJ8; X-ray; 1.90 A; A=2-361.
DR PDB; 7KJ9; X-ray; 2.20 A; A=2-361.
DR PDB; 7KJD; X-ray; 1.50 A; A=2-361.
DR PDB; 7KJE; X-ray; 1.60 A; A=2-361.
DR PDB; 7KJF; X-ray; 1.40 A; A=2-361.
DR PDB; 7KJG; X-ray; 1.30 A; A=2-361.
DR PDBsum; 3KB9; -.
DR PDBsum; 3KBK; -.
DR PDBsum; 3LG5; -.
DR PDBsum; 3LGK; -.
DR PDBsum; 4LTV; -.
DR PDBsum; 4LTZ; -.
DR PDBsum; 4LUU; -.
DR PDBsum; 4LXW; -.
DR PDBsum; 4LZ0; -.
DR PDBsum; 4LZ3; -.
DR PDBsum; 4LZC; -.
DR PDBsum; 6AX9; -.
DR PDBsum; 6AXM; -.
DR PDBsum; 6AXN; -.
DR PDBsum; 6AXO; -.
DR PDBsum; 6AXU; -.
DR PDBsum; 6OFV; -.
DR PDBsum; 7KJ8; -.
DR PDBsum; 7KJ9; -.
DR PDBsum; 7KJD; -.
DR PDBsum; 7KJE; -.
DR PDBsum; 7KJF; -.
DR PDBsum; 7KJG; -.
DR AlphaFoldDB; Q9K499; -.
DR SMR; Q9K499; -.
DR STRING; 100226.SCO5222; -.
DR GeneID; 1100663; -.
DR KEGG; sco:SCO5222; -.
DR PATRIC; fig|100226.15.peg.5306; -.
DR eggNOG; ENOG5033S8Y; Bacteria.
DR HOGENOM; CLU_042538_4_1_11; -.
DR InParanoid; Q9K499; -.
DR OMA; DLIEYAM; -.
DR PhylomeDB; Q9K499; -.
DR BioCyc; MetaCyc:MON-13904; -.
DR BRENDA; 4.2.3.37; 5998.
DR SABIO-RK; Q9K499; -.
DR UniPathway; UPA00195; -.
DR EvolutionaryTrace; Q9K499; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0052680; F:epi-isozizaene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034686; Terpene_cyclase-like_2.
DR SFLD; SFLDG01020; Terpene_Cyclase_Like_2; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..361
FT /note="Epi-isozizaene synthase"
FT /id="PRO_0000247894"
FT MOTIF 99..103
FT /note="DDXXD motif"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:7KJG"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:7KJG"
FT HELIX 38..51
FT /evidence="ECO:0007829|PDB:7KJG"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:7KJG"
FT HELIX 69..74
FT /evidence="ECO:0007829|PDB:7KJG"
FT HELIX 82..107
FT /evidence="ECO:0007829|PDB:7KJG"
FT HELIX 111..126
FT /evidence="ECO:0007829|PDB:7KJG"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:7KJG"
FT HELIX 137..149
FT /evidence="ECO:0007829|PDB:7KJG"
FT HELIX 155..181
FT /evidence="ECO:0007829|PDB:7KJG"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:7KJG"
FT HELIX 200..211
FT /evidence="ECO:0007829|PDB:7KJG"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:7KJG"
FT HELIX 223..250
FT /evidence="ECO:0007829|PDB:7KJG"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:3LGK"
FT HELIX 257..265
FT /evidence="ECO:0007829|PDB:7KJG"
FT HELIX 269..301
FT /evidence="ECO:0007829|PDB:7KJG"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:7KJD"
FT HELIX 306..335
FT /evidence="ECO:0007829|PDB:7KJG"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:7KJG"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:7KJG"
SQ SEQUENCE 361 AA; 41388 MW; 227B08D792F36BB7 CRC64;
MHAFPHGTTA TPTAIAVPPS LRLPVIEAAF PRQLHPYWPK LQETTRTWLL EKRLMPADKV
EEYADGLCYT DLMAGYYLGA PDEVLQAIAD YSAWFFVWDD RHDRDIVHGR AGAWRRLRGL
LHTALDSPGD HLHHEDTLVA GFADSVRRLY AFLPATWNAR FARHFHTVIE AYDREFHNRT
RGIVPGVEEY LELRRLTFAH WIWTDLLEPS SGCELPDAVR KHPAYRRAAL LSQEFAAWYN
DLCSLPKEIA GDEVHNLGIS LITHHSLTLE EAIGEVRRRV EECITEFLAV ERDALRFADE
LADGTVRGKE LSGAVRANVG NMRNWFSSVY WFHHESGRYM VDSWDDRSTP PYVNNEAAGE
K
