SEDS_STRE2
ID SEDS_STRE2 Reviewed; 365 AA.
AC B5HDJ6;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Selina-4(15),7(11)-diene synthase ((2E,6E)-farnesyl diphosphate cyclizing) {ECO:0000303|PubMed:23307484};
DE EC=4.2.3.181 {ECO:0000269|PubMed:23307484, ECO:0000269|PubMed:24890698};
DE AltName: Full=Selinadiene synthase {ECO:0000303|PubMed:24890698};
DE Short=SdS {ECO:0000303|PubMed:24890698};
DE AltName: Full=Terpene synthase {ECO:0000303|PubMed:23307484};
DE AltName: Full=Type I terpene cyclase {ECO:0000303|PubMed:23307484};
GN ORFNames=SSDG_02809 {ECO:0000312|EMBL:EDY64907.2};
OS Streptomyces pristinaespiralis (strain ATCC 25486 / DSM 40338 / CBS 914.69
OS / JCM 4507 / NBRC 13074 / NRRL 2958 / 5647).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=457429;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25486 / DSM 40338 / CBS 914.69 / JCM 4507 / NBRC 13074 / NRRL
RC 2958 / 5647 {ECO:0000312|Proteomes:UP000002805};
RG The Broad Institute Genome Sequencing Platform;
RA Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Straight P., Clardy J.,
RA Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., Lander E.,
RA Galagan J., Nusbaum C., Birren B.;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25486 / DSM 40338 / CBS 914.69 / JCM 4507 / NBRC 13074 / NRRL
RC 2958 / 5647 {ECO:0000312|EMBL:EDY64907.2,
RC ECO:0000312|Proteomes:UP000002805};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Streptomyces pristinaespiralis strain ATCC 25486.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND PATHWAY.
RC STRAIN=ATCC 25486 / DSM 40338 / CBS 914.69 / JCM 4507 / NBRC 13074 / NRRL
RC 2958 / 5647;
RX PubMed=23307484; DOI=10.1002/anie.201209103;
RA Rabe P., Dickschat J.S.;
RT "Rapid chemical characterization of bacterial terpene synthases.";
RL Angew. Chem. Int. Ed. 52:1810-1812(2013).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND
RP SUBSTRATE ANALOGS, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF
RP PHE-55; PHE-79; ASP-83; GLU-159; ARG-178; GLY-182 AND ALA-183, SUBSTRATE
RP SPECIFICITY, REACTION MECHANISM, DOMAIN, AND SUBUNIT.
RC STRAIN=ATCC 25486 / DSM 40338 / CBS 914.69 / JCM 4507 / NBRC 13074 / NRRL
RC 2958 / 5647;
RX PubMed=24890698; DOI=10.1002/anie.201403648;
RA Baer P., Rabe P., Fischer K., Citron C.A., Klapschinski T.A., Groll M.,
RA Dickschat J.S.;
RT "Induced-fit mechanism in class I terpene cyclases.";
RL Angew. Chem. Int. Ed. 53:7652-7656(2014).
CC -!- FUNCTION: Catalyzes the conversion of (2E,6E)-farnesyl diphosphate
CC (FPP) to yield the bicyclic sesquiterpene selina-4(15),7(11)-diene via
CC a 1,10-cyclization, which requires the abstraction of the pyrophosphate
CC from FPP leading to a (E,E)-germacradienyl cation (PubMed:23307484,
CC PubMed:24890698). The only accepted substrate is (2E,6E)-farnesyl
CC diphosphate (FPP) (PubMed:23307484, PubMed:24890698).
CC {ECO:0000269|PubMed:23307484, ECO:0000269|PubMed:24890698}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + selina-
CC 4(15),7(11)-diene; Xref=Rhea:RHEA:54112, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:138051, ChEBI:CHEBI:175763; EC=4.2.3.181;
CC Evidence={ECO:0000269|PubMed:23307484, ECO:0000269|PubMed:24890698};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24890698};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000269|PubMed:24890698};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:23307484}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24890698}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Xaa-Glu (DDXXXE) motif is important for the
CC catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000305|PubMed:24890698}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; CM000950; EDY64907.2; -; Genomic_DNA.
DR RefSeq; WP_005317515.1; NZ_CM000950.1.
DR PDB; 4OKM; X-ray; 2.10 A; A/B/C/D=1-365.
DR PDB; 4OKZ; X-ray; 1.90 A; A/B/C/D=1-365.
DR PDBsum; 4OKM; -.
DR PDBsum; 4OKZ; -.
DR AlphaFoldDB; B5HDJ6; -.
DR SMR; B5HDJ6; -.
DR STRING; 457429.ABJI02000529_gene6382; -.
DR EnsemblBacteria; EDY64907; EDY64907; SSDG_02809.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_042538_4_2_11; -.
DR OMA; AMETWVI; -.
DR BRENDA; 4.2.3.181; 12737.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000002805; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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..365
FT /note="Selina-4(15),7(11)-diene synthase ((2E,6E)-farnesyl
FT diphosphate cyclizing)"
FT /id="PRO_0000443243"
FT MOTIF 82..87
FT /note="DDXXXE motif"
FT /evidence="ECO:0000305|PubMed:24890698"
FT BINDING 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24890698,
FT ECO:0007744|PDB:4OKM, ECO:0007744|PDB:4OKZ"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24890698,
FT ECO:0007744|PDB:4OKM, ECO:0007744|PDB:4OKZ"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24890698,
FT ECO:0007744|PDB:4OKM, ECO:0007744|PDB:4OKZ"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24890698,
FT ECO:0007744|PDB:4OKM, ECO:0007744|PDB:4OKZ"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:24890698,
FT ECO:0007744|PDB:4OKM, ECO:0007744|PDB:4OKZ"
FT BINDING 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:24890698,
FT ECO:0007744|PDB:4OKM, ECO:0007744|PDB:4OKZ"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24890698,
FT ECO:0007744|PDB:4OKZ"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:24890698,
FT ECO:0007744|PDB:4OKM, ECO:0007744|PDB:4OKZ"
FT BINDING 310..311
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24890698,
FT ECO:0007744|PDB:4OKM, ECO:0007744|PDB:4OKZ"
FT SITE 55
FT /note="Plays a critical role in the stabilization of
FT intermediate cation"
FT /evidence="ECO:0000269|PubMed:24890698"
FT SITE 79
FT /note="Plays a critical role in the stabilization of
FT intermediate cation"
FT /evidence="ECO:0000269|PubMed:24890698"
FT SITE 83
FT /note="Plays a critical role for substrate recognition"
FT /evidence="ECO:0000269|PubMed:24890698"
FT SITE 159
FT /note="Plays a critical role for substrate recognition"
FT /evidence="ECO:0000269|PubMed:24890698"
FT SITE 182
FT /note="Plays a critical role for abstraction of the
FT pyrophosphate group"
FT /evidence="ECO:0000269|PubMed:24890698"
FT MUTAGEN 55
FT /note="F->L,W,Y: Drastically alters the product spectra
FT compared to the wild-type, comprising linear terpenoids in
FT addition to selina-4(15),7(11)-diene and germacrene B.
FT Yields only a small amount of selina-4(15),7(11)-diene
FT along with a considerable increase of germacrene B."
FT /evidence="ECO:0000269|PubMed:24890698"
FT MUTAGEN 79
FT /note="F->L,W,Y: Drastically alters the product spectra
FT compared to the wild-type, comprising linear terpenoids in
FT addition to selina-4(15),7(11)-diene and germacrene B.
FT Yields only a small amount of selina-4(15),7(11)-diene
FT along with a considerable increase of germacrene B."
FT /evidence="ECO:0000269|PubMed:24890698"
FT MUTAGEN 83
FT /note="D->E,N: Drastically alters the product spectra
FT compared to the wild-type, comprising linear terpenoids in
FT addition to germacrene B. Unable to produce selina-
FT 4(15),7(11)-diene."
FT /evidence="ECO:0000269|PubMed:24890698"
FT MUTAGEN 159
FT /note="E->D,Q: Drastically alters the product spectra
FT compared to the wild-type, comprising linear terpenoids in
FT addition to germacrene B. Unable to produce selina-
FT 4(15),7(11)-diene."
FT /evidence="ECO:0000269|PubMed:24890698"
FT MUTAGEN 178
FT /note="R->K,N,Q: Lack of cyclase activity."
FT /evidence="ECO:0000269|PubMed:24890698"
FT MUTAGEN 182
FT /note="G->A: Drastically alters the product spectra
FT compared to the wild-type, comprising linear terpenoids in
FT addition to selina-4(15),7(11)-diene and germacrene B.
FT Yields only a small amount of selina-4(15),7(11)-diene
FT along with a considerable increase of germacrene B."
FT /evidence="ECO:0000269|PubMed:24890698"
FT MUTAGEN 182
FT /note="G->P,V: Lack of cyclase activity."
FT /evidence="ECO:0000269|PubMed:24890698"
FT MUTAGEN 183
FT /note="A->F,V: Lack of cyclase activity."
FT /evidence="ECO:0000269|PubMed:24890698"
FT HELIX 22..35
FT /evidence="ECO:0007829|PDB:4OKZ"
FT HELIX 41..47
FT /evidence="ECO:0007829|PDB:4OKZ"
FT HELIX 52..59
FT /evidence="ECO:0007829|PDB:4OKZ"
FT HELIX 65..82
FT /evidence="ECO:0007829|PDB:4OKZ"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:4OKZ"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:4OKZ"
FT HELIX 95..110
FT /evidence="ECO:0007829|PDB:4OKZ"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:4OKZ"
FT HELIX 121..136
FT /evidence="ECO:0007829|PDB:4OKZ"
FT HELIX 139..165
FT /evidence="ECO:0007829|PDB:4OKZ"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:4OKZ"
FT HELIX 184..193
FT /evidence="ECO:0007829|PDB:4OKZ"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:4OKZ"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:4OKZ"
FT HELIX 207..233
FT /evidence="ECO:0007829|PDB:4OKZ"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:4OKZ"
FT HELIX 242..250
FT /evidence="ECO:0007829|PDB:4OKZ"
FT HELIX 254..282
FT /evidence="ECO:0007829|PDB:4OKZ"
FT HELIX 285..305
FT /evidence="ECO:0007829|PDB:4OKZ"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:4OKZ"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:4OKZ"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:4OKZ"
FT HELIX 342..347
FT /evidence="ECO:0007829|PDB:4OKZ"
SQ SEQUENCE 365 AA; 41238 MW; 4343D6861D47D323 CRC64;
MEPELTVPPL FSPIRQAIHP KHADIDVQTA AWAETFRIGS EELRGKLVTQ DIGTFSARIL
PEGREEVVSL LADFILWLFG VDDGHCEEGE LGHRPGDLAG LLHRLIRVAQ NPEAPMMQDD
PLAAGLRDLR MRVDRFGTAG QTARWVDALR EYFFSVVWEA AHRRAGTVPD LNDYTLMRLY
DGATSVVLPM LEMGHGYELQ PYERDRTAVR AVAEMASFII TWDNDIFSYH KERRGSGYYL
NALRVLEQER GLTPAQALDA AISQRDRVMC LFTTVSEQLA EQGSPQLRQY LHSLRCFIRG
AQDWGISSVR YTTPDDPANM PSVFTDVPTD DSTEPLDIPA VSWWWDLLAE DARSVRRQVP
AQRSA
