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Germacradienol/geosmin synthase [Includes: Germacradienol/germacrene D synthase (EC 4.2.3.22) (EC 4.2.3.75) (Sesquiterpene cyclase) (Sesquiterpene synthase); Geosmin synthase (EC 4.1.99.16)]

 CYC2_STRCO              Reviewed;         726 AA.
Q9X839;
25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 105.
RecName: Full=Germacradienol/geosmin synthase;
Includes:
RecName: Full=Germacradienol/germacrene D synthase;
EC=4.2.3.22;
EC=4.2.3.75;
AltName: Full=Sesquiterpene cyclase;
AltName: Full=Sesquiterpene synthase;
Includes:
RecName: Full=Geosmin synthase;
EC=4.1.99.16;
Name=cyc2; OrderedLocusNames=SCO6073; ORFNames=SC9B1.20;
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces; Streptomyces albidoflavus group.
NCBI_TaxID=100226;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-471 / A3(2) / M145;
PubMed=12000953; DOI=10.1038/417141a;
Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
Hopwood D.A.;
"Complete genome sequence of the model actinomycete Streptomyces
coelicolor A3(2).";
Nature 417:141-147(2002).
[2]
PROTEIN SEQUENCE OF 2-10, FUNCTION, CATALYTIC ACTIVITY, DOMAIN,
KINETIC PARAMETERS, AND COFACTOR.
STRAIN=ATCC BAA-471 / A3(2) / M145;
PubMed=12556563; DOI=10.1073/pnas.0337625100;
Cane D.E., Watt R.M.;
"Expression and mechanistic analysis of a germacradienol synthase from
Streptomyces coelicolor implicated in geosmin biosynthesis.";
Proc. Natl. Acad. Sci. U.S.A. 100:1547-1551(2003).
[3]
DOMAIN, AND ROLE IN GEOSMIN BIOSYNTHESIS.
STRAIN=ATCC BAA-471 / A3(2) / M145;
PubMed=12563033; DOI=10.1073/pnas.0337542100;
Gust B., Challis G.L., Fowler K., Kieser T., Chater K.F.;
"PCR-targeted Streptomyces gene replacement identifies a protein
domain needed for biosynthesis of the sesquiterpene soil odor
geosmin.";
Proc. Natl. Acad. Sci. U.S.A. 100:1541-1546(2003).
[4]
FUNCTION IN GERMACRENE D PRODUCTION, AND REACTION STEREOCHEMISTRY.
STRAIN=ATCC BAA-471 / A3(2) / M145;
PubMed=14995166; DOI=10.1021/ja039929k;
He X., Cane D.E.;
"Mechanism and stereochemistry of the germacradienol/germacrene D
synthase of Streptomyces coelicolor A3(2).";
J. Am. Chem. Soc. 126:2678-2679(2004).
[5]
FUNCTION IN DIRECT GEOSMIN PRODUCTION, COFACTOR, AND REACTION
MECHANISM.
STRAIN=ATCC BAA-471 / A3(2) / M145;
PubMed=16787064; DOI=10.1021/ja062669x;
Jiang J., He X., Cane D.E.;
"Geosmin biosynthesis. Streptomyces coelicolor
germacradienol/germacrene D synthase converts farnesyl diphosphate to
geosmin.";
J. Am. Chem. Soc. 128:8128-8129(2006).
-!- FUNCTION: Tow-domain protein where the N-terminal domain catalyzes
the cyclization of farnesyl diphosphate (FPP) to a 85:15 mixture
of the sesquiterpene alcohol germacradienol and the sesquiterpene
hydrocarbon germacrene D. The C-terminal domain partially converts
the germacradienol formed into geosmin, the characteristic
odoriferous ('earthy aroma') constituent of Streptomyces species.
{ECO:0000269|PubMed:12556563, ECO:0000269|PubMed:12563033,
ECO:0000269|PubMed:14995166, ECO:0000269|PubMed:16787064}.
-!- CATALYTIC ACTIVITY: (2E,6E)-farnesyl diphosphate + H(2)O =
(1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + diphosphate.
{ECO:0000269|PubMed:12556563}.
-!- CATALYTIC ACTIVITY: (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol +
H(2)O = (-)-geosmin + acetone. {ECO:0000269|PubMed:12556563}.
-!- CATALYTIC ACTIVITY: (2E,6E)-farnesyl diphosphate = (-)-germacrene
D + diphosphate. {ECO:0000269|PubMed:12556563}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:12556563,
ECO:0000269|PubMed:16787064};
Note=Magnesium. Fe(2+) or Cu(2+) ions are very less efficient as
cofactors. {ECO:0000269|PubMed:12556563,
ECO:0000269|PubMed:16787064};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=62 nM for FPP {ECO:0000269|PubMed:12556563};
-!- PATHWAY: Secondary metabolite biosynthesis; geosmin biosynthesis.
-!- PATHWAY: Sesquiterpene biosynthesis; germacradienol biosynthesis;
germacradienol from farnesyl diphosphate: step 1/1.
-!- PATHWAY: Sesquiterpene biosynthesis; germacrene D biosynthesis;
germacrene D from farnesyl diphosphate: step 1/1.
-!- DOMAIN: Consists of 2 homologous sesquiterpene synthase domains.
The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the
catalytic activity, presumably through binding to Mg(2+).
{ECO:0000269|PubMed:12556563, ECO:0000269|PubMed:12563033}.
-!- MISCELLANEOUS: The earthy odorant geosmin is also responsible for
the 'off-flavor' of contaminated drinking water, wines, and other
foodstuffs.
-!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
-!- CAUTION: It is uncertain whether the initial Met is cleaved or
not. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The earth's perfume
- Issue 35 of June 2003;
URL="https://web.expasy.org/spotlight/back_issues/035";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AL939126; CAB41566.1; -; Genomic_DNA.
PIR; T35865; T35865.
RefSeq; NP_630182.1; NC_003888.3.
RefSeq; WP_011030632.1; NC_003888.3.
PDB; 5DW7; X-ray; 3.20 A; A=1-366.
PDB; 5DZ2; X-ray; 2.11 A; A/B=1-338.
PDBsum; 5DW7; -.
PDBsum; 5DZ2; -.
ProteinModelPortal; Q9X839; -.
SMR; Q9X839; -.
STRING; 100226.SCO6073; -.
PRIDE; Q9X839; -.
EnsemblBacteria; CAB41566; CAB41566; CAB41566.
GeneID; 1101514; -.
KEGG; sco:SCO6073; -.
PATRIC; fig|100226.15.peg.6175; -.
eggNOG; ENOG4105IK6; Bacteria.
eggNOG; ENOG410XSNU; LUCA.
HOGENOM; HOG000253477; -.
InParanoid; Q9X839; -.
KO; K10187; -.
OMA; RLPLFMP; -.
OrthoDB; POG091H0EGW; -.
BioCyc; MetaCyc:MONOMER-14022; -.
BRENDA; 4.1.99.16; 5998.
BRENDA; 4.2.3.22; 5998.
SABIO-RK; Q9X839; -.
UniPathway; UPA00209; -.
UniPathway; UPA00283; UER00583.
UniPathway; UPA00285; UER00584.
Proteomes; UP000001973; Chromosome.
GO; GO:0034004; F:germacradienol synthase activity; IEA:UniProtKB-EC.
GO; GO:0052577; F:germacrene-D synthase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
Gene3D; 1.10.600.10; -; 2.
InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
InterPro; IPR034686; Terpene_cyclase_like_2.
SFLD; SFLDG01020; Terpene_Cyclase_Like_2; 2.
SUPFAM; SSF48576; SSF48576; 2.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing; Lyase;
Magnesium; Metal-binding; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12556563}.
CHAIN 2 726 Germacradienol/geosmin synthase.
/FTId=PRO_0000247895.
REGION 2 354 Germacradienol/germacrene D synthase.
REGION 355 726 Geosmin synthase.
MOTIF 86 91 DDXXD motif 1; degenerate.
MOTIF 455 459 DDXXD motif 2; degenerate.
METAL 86 86 Magnesium. {ECO:0000255}.
METAL 91 91 Magnesium. {ECO:0000255}.
METAL 267 267 Magnesium. {ECO:0000255}.
METAL 271 271 Magnesium. {ECO:0000255}.
METAL 276 276 Magnesium. {ECO:0000255}.
METAL 455 455 Magnesium. {ECO:0000255}.
METAL 598 598 Magnesium. {ECO:0000255}.
METAL 602 602 Magnesium. {ECO:0000255}.
METAL 606 606 Magnesium. {ECO:0000255}.
HELIX 23 37 {ECO:0000244|PDB:5DZ2}.
STRAND 43 45 {ECO:0000244|PDB:5DZ2}.
HELIX 48 54 {ECO:0000244|PDB:5DZ2}.
HELIX 56 63 {ECO:0000244|PDB:5DZ2}.
HELIX 69 92 {ECO:0000244|PDB:5DZ2}.
TURN 93 97 {ECO:0000244|PDB:5DZ2}.
HELIX 99 108 {ECO:0000244|PDB:5DZ2}.
HELIX 109 112 {ECO:0000244|PDB:5DZ2}.
HELIX 127 139 {ECO:0000244|PDB:5DZ2}.
HELIX 140 142 {ECO:0000244|PDB:5DZ2}.
HELIX 145 171 {ECO:0000244|PDB:5DZ2}.
HELIX 177 187 {ECO:0000244|PDB:5DZ2}.
HELIX 190 200 {ECO:0000244|PDB:5DZ2}.
HELIX 206 209 {ECO:0000244|PDB:5DZ2}.
HELIX 212 239 {ECO:0000244|PDB:5DZ2}.
HELIX 247 255 {ECO:0000244|PDB:5DZ2}.
HELIX 259 282 {ECO:0000244|PDB:5DZ2}.
HELIX 284 291 {ECO:0000244|PDB:5DZ2}.
HELIX 296 320 {ECO:0000244|PDB:5DZ2}.
HELIX 324 326 {ECO:0000244|PDB:5DW7}.
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


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