CYC2_STRCO
ID CYC2_STRCO Reviewed; 726 AA.
AC Q9X839;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Germacradienol/geosmin synthase;
DE Includes:
DE RecName: Full=Germacradienol/germacrene D synthase;
DE EC=4.2.3.22;
DE EC=4.2.3.75;
DE AltName: Full=Sesquiterpene cyclase;
DE AltName: Full=Sesquiterpene synthase;
DE Includes:
DE RecName: Full=Geosmin synthase;
DE EC=4.1.99.16;
GN Name=cyc2; OrderedLocusNames=SCO6073; ORFNames=SC9B1.20;
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 PROTEIN SEQUENCE OF 2-10, FUNCTION, CATALYTIC ACTIVITY, DOMAIN, KINETIC
RP PARAMETERS, AND COFACTOR.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12556563; DOI=10.1073/pnas.0337625100;
RA Cane D.E., Watt R.M.;
RT "Expression and mechanistic analysis of a germacradienol synthase from
RT Streptomyces coelicolor implicated in geosmin biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1547-1551(2003).
RN [3]
RP DOMAIN, AND ROLE IN GEOSMIN BIOSYNTHESIS.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12563033; DOI=10.1073/pnas.0337542100;
RA Gust B., Challis G.L., Fowler K., Kieser T., Chater K.F.;
RT "PCR-targeted Streptomyces gene replacement identifies a protein domain
RT needed for biosynthesis of the sesquiterpene soil odor geosmin.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1541-1546(2003).
RN [4]
RP FUNCTION IN GERMACRENE D PRODUCTION, AND REACTION STEREOCHEMISTRY.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=14995166; DOI=10.1021/ja039929k;
RA He X., Cane D.E.;
RT "Mechanism and stereochemistry of the germacradienol/germacrene D synthase
RT of Streptomyces coelicolor A3(2).";
RL J. Am. Chem. Soc. 126:2678-2679(2004).
RN [5]
RP FUNCTION IN DIRECT GEOSMIN PRODUCTION, COFACTOR, AND REACTION MECHANISM.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=16787064; DOI=10.1021/ja062669x;
RA Jiang J., He X., Cane D.E.;
RT "Geosmin biosynthesis. Streptomyces coelicolor germacradienol/germacrene D
RT synthase converts farnesyl diphosphate to geosmin.";
RL J. Am. Chem. Soc. 128:8128-8129(2006).
CC -!- FUNCTION: Tow-domain protein where the N-terminal domain catalyzes the
CC cyclization of farnesyl diphosphate (FPP) to a 85:15 mixture of the
CC sesquiterpene alcohol germacradienol and the sesquiterpene hydrocarbon
CC germacrene D. The C-terminal domain partially converts the
CC germacradienol formed into geosmin, the characteristic odoriferous
CC ('earthy aroma') constituent of Streptomyces species.
CC {ECO:0000269|PubMed:12556563, ECO:0000269|PubMed:12563033,
CC ECO:0000269|PubMed:14995166, ECO:0000269|PubMed:16787064}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (1E,4S,5E,7R)-germacra-
CC 1(10),5-dien-11-ol + diphosphate; Xref=Rhea:RHEA:22436,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:46734,
CC ChEBI:CHEBI:175763; EC=4.2.3.22;
CC Evidence={ECO:0000269|PubMed:12556563};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + H2O = (-)-geosmin
CC + acetone; Xref=Rhea:RHEA:30371, ChEBI:CHEBI:15347,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:46702, ChEBI:CHEBI:46734;
CC EC=4.1.99.16; Evidence={ECO:0000269|PubMed:12556563};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (-)-germacrene D + diphosphate;
CC Xref=Rhea:RHEA:12016, ChEBI:CHEBI:33019, ChEBI:CHEBI:49044,
CC ChEBI:CHEBI:175763; EC=4.2.3.75;
CC Evidence={ECO:0000269|PubMed:12556563};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12556563, ECO:0000269|PubMed:16787064};
CC Note=Magnesium. Fe(2+) or Cu(2+) ions are very less efficient as
CC cofactors. {ECO:0000269|PubMed:12556563, ECO:0000269|PubMed:16787064};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=62 nM for FPP {ECO:0000269|PubMed:12556563};
CC -!- PATHWAY: Secondary metabolite biosynthesis; geosmin biosynthesis.
CC -!- PATHWAY: Sesquiterpene biosynthesis; germacradienol biosynthesis;
CC germacradienol from farnesyl diphosphate: step 1/1.
CC -!- PATHWAY: Sesquiterpene biosynthesis; germacrene D biosynthesis;
CC germacrene D from farnesyl diphosphate: step 1/1.
CC -!- DOMAIN: Consists of 2 homologous sesquiterpene synthase domains. The
CC Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic
CC activity, presumably through binding to Mg(2+).
CC {ECO:0000269|PubMed:12556563, ECO:0000269|PubMed:12563033}.
CC -!- MISCELLANEOUS: The earthy odorant geosmin is also responsible for the
CC 'off-flavor' of contaminated drinking water, wines, and other
CC foodstuffs.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether the initial Met is cleaved or not.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The earth's perfume - Issue
CC 35 of June 2003;
CC URL="https://web.expasy.org/spotlight/back_issues/035";
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DR EMBL; AL939126; CAB41566.1; -; Genomic_DNA.
DR PIR; T35865; T35865.
DR RefSeq; NP_630182.1; NC_003888.3.
DR RefSeq; WP_011030632.1; NZ_VNID01000009.1.
DR PDB; 5DW7; X-ray; 3.20 A; A=1-366.
DR PDB; 5DZ2; X-ray; 2.11 A; A/B=1-338.
DR PDBsum; 5DW7; -.
DR PDBsum; 5DZ2; -.
DR AlphaFoldDB; Q9X839; -.
DR SMR; Q9X839; -.
DR STRING; 100226.SCO6073; -.
DR GeneID; 1101514; -.
DR KEGG; sco:SCO6073; -.
DR PATRIC; fig|100226.15.peg.6175; -.
DR eggNOG; ENOG502Z881; Bacteria.
DR HOGENOM; CLU_372108_0_0_11; -.
DR InParanoid; Q9X839; -.
DR OMA; RLPLFMP; -.
DR BioCyc; MetaCyc:MON-14022; -.
DR BRENDA; 4.1.99.16; 5998.
DR BRENDA; 4.2.3.22; 5998.
DR SABIO-RK; Q9X839; -.
DR UniPathway; UPA00209; -.
DR UniPathway; UPA00283; UER00583.
DR UniPathway; UPA00285; UER00584.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0034004; F:germacradienol synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0052577; F:germacrene-D synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.600.10; -; 2.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034686; Terpene_cyclase-like_2.
DR SFLD; SFLDG01020; Terpene_Cyclase_Like_2; 2.
DR SUPFAM; SSF48576; SSF48576; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lyase; Magnesium; Metal-binding;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12556563"
FT CHAIN 2..726
FT /note="Germacradienol/geosmin synthase"
FT /id="PRO_0000247895"
FT REGION 2..354
FT /note="Germacradienol/germacrene D synthase"
FT REGION 355..726
FT /note="Geosmin synthase"
FT MOTIF 86..91
FT /note="DDXXD motif 1; degenerate"
FT MOTIF 455..459
FT /note="DDXXD motif 2; degenerate"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 271
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 598
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 602
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 606
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT HELIX 23..37
FT /evidence="ECO:0007829|PDB:5DZ2"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:5DZ2"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:5DZ2"
FT HELIX 56..63
FT /evidence="ECO:0007829|PDB:5DZ2"
FT HELIX 69..92
FT /evidence="ECO:0007829|PDB:5DZ2"
FT TURN 93..97
FT /evidence="ECO:0007829|PDB:5DZ2"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:5DZ2"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:5DZ2"
FT HELIX 127..139
FT /evidence="ECO:0007829|PDB:5DZ2"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:5DZ2"
FT HELIX 145..171
FT /evidence="ECO:0007829|PDB:5DZ2"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:5DZ2"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:5DZ2"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:5DZ2"
FT HELIX 212..239
FT /evidence="ECO:0007829|PDB:5DZ2"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:5DZ2"
FT HELIX 259..282
FT /evidence="ECO:0007829|PDB:5DZ2"
FT HELIX 284..291
FT /evidence="ECO:0007829|PDB:5DZ2"
FT HELIX 296..320
FT /evidence="ECO:0007829|PDB:5DZ2"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:5DW7"
SQ SEQUENCE 726 AA; 81474 MW; CB332AC7840EB81E CRC64;
MTQQPFQLPH FYLPHPARLN PHLDEARAHS TTWAREMGML EGSGVWEQSD LEAHDYGLLC
AYTHPDCDGP ALSLITDWYV WVFFFDDHFL EKYKRSQDRL AGKAHLDRLP LFMPLDDAAG
MPEPRNPVEA GLADLWTRTV PAMSADWRRR FAVATEHLLN ESMWELSNIN EGRVANPVEY
IEMRRKVGGA PWSAGLVEYA TAEVPAAVAG TRPLRVLMET FSDAVHLRND LFSYQREVED
EGELSNGVLV LETFFGCTTQ EAADLVNDVL TSRLHQFEHT AFTEVPAVAL EKGLTPLEVA
AVGAYTKGLQ DWQSGGHEWH MRSSRYMNKG ERPLAGWQAL TGPGTSAADV GALLADAVAQ
RARSYTYVPF QKVGPSVIPD IRMPYPLELS PALDGARRHL SEWCREMGIL SEGVWDEDKL
ESCDLPLCAA GLDPDATQDQ LDLASGWLAF GTYGDDYYPL VYGHRRDLAA ARLTTTRLSD
CMPLDGEPVP PPGNAMERSL IDLWVRTTAG MTPEERRPLK KAVDDMTEAW LWELSNQIQN
RVPDPVDYLE MRRATFGSDL TLGLCRAGHG PAVPPEVYRS GPVRSLENAA IDYACLLNDV
FSYQKEIEYE GEIHNAVLVV QNFFGVDYPA ALGVVQDLMN QRMRQFEHVV AHELPVVYDD
FQLSEEARTV MRGYVTDLQN WMAGILNWHR NVPRYKAEYL AGRTHGFLPD RIPAPPVPRS
SPALTH
