LNSA_STRCL
ID LNSA_STRCL Reviewed; 329 AA.
AC D5SL78;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=R-linalool synthase {ECO:0000303|PubMed:28966840};
DE Short=bLinS {ECO:0000303|PubMed:28966840};
DE EC=4.2.3.26 {ECO:0000269|PubMed:28966840};
DE AltName: Full=Monoterpene synthase {ECO:0000303|PubMed:28966840};
DE AltName: Full=Sesquiterpene synthase {ECO:0000303|PubMed:28966840};
GN ORFNames=SCLAV_p1185 {ECO:0000312|EMBL:EFG04671.2};
OS Streptomyces clavuligerus.
OG Plasmid pSCL4 {ECO:0000312|EMBL:EFG04671.2,
OG ECO:0000312|Proteomes:UP000002357}.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC 3585 / VKM Ac-602 {ECO:0000312|Proteomes:UP000002357};
RX PubMed=20624727; DOI=10.1093/gbe/evq013;
RA Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U.,
RA Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C., Bovenberg R.A.L.,
RA Breitling R., Takano E.;
RT "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich
RT evolutionary reservoir of secondary metabolic pathways.";
RL Genome Biol. Evol. 2:212-224(2010).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, SUBSTRATE SPECIFICITY, DOMAIN, AND SUBUNIT.
RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC 3585 / VKM Ac-602;
RX PubMed=28966840; DOI=10.1021/acscatal.7b01924;
RA Karuppiah V., Ranaghan K.E., Leferink N.G.H., Johannissen L.O.,
RA Shanmugam M., Cheallaigh A.N., Bennett N.J., Kearset L.J., Takano E.,
RA Gardiner J.M., van der Kamp M.W., Hay S., Mulholland A.J., Leys D.,
RA Scrutton N.S.;
RT "Structural basis of catalysis in the bacterial monoterpene synthases
RT linalool synthase and 1,8-cineole synthase.";
RL ACS Catal. 7:6268-6282(2017).
CC -!- FUNCTION: In vitro, catalyzes the formation of R-linalool from geranyl
CC diphosphate (GPP). Can also accept farnesyl diphosphate (FPP) as
CC substrate to produce trans-nerolidol. {ECO:0000269|PubMed:28966840}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (R)-linalool + diphosphate;
CC Xref=Rhea:RHEA:15809, ChEBI:CHEBI:28, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.26;
CC Evidence={ECO:0000269|PubMed:28966840};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (6E)-nerolidol +
CC diphosphate; Xref=Rhea:RHEA:56984, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:141283, ChEBI:CHEBI:175763;
CC Evidence={ECO:0000269|PubMed:28966840};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:28966840};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:B5GMG2};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:28966840}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp (DDXXD) and Asn-Xaa-Xaa-Xaa-Ser-Xaa-
CC Xaa-Xaa-Asp (NSD) motifs are important for the catalytic activity,
CC presumably through binding to Mg(2+). {ECO:0000305|PubMed:28966840}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; CM000914; EFG04671.2; -; Genomic_DNA.
DR RefSeq; WP_003963519.1; NZ_CP032054.1.
DR PDB; 5NX4; X-ray; 2.38 A; A/B=1-329.
DR PDB; 5NX5; X-ray; 1.82 A; A/B=1-329.
DR PDBsum; 5NX4; -.
DR PDBsum; 5NX5; -.
DR AlphaFoldDB; D5SL78; -.
DR SMR; D5SL78; -.
DR STRING; 443255.SCLAV_p1185; -.
DR GeneID; 61473876; -.
DR KEGG; sclf:BB341_30005; -.
DR eggNOG; COG2124; Bacteria.
DR OMA; AMEHWVI; -.
DR OrthoDB; 1869158at2; -.
DR Proteomes; UP000002357; Plasmid pSCL4.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0034008; F:R-linalool synthase activity; IDA:UniProtKB.
DR GO; GO:0045338; P:farnesyl diphosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0033383; P:geranyl diphosphate metabolic process; IDA:UniProtKB.
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; Plasmid; Reference proteome.
FT CHAIN 1..329
FT /note="R-linalool synthase"
FT /id="PRO_0000445229"
FT MOTIF 79..83
FT /note="DDXXD motif"
FT /evidence="ECO:0000305|PubMed:28966840"
FT MOTIF 218..226
FT /note="NXXXSXXXD motif"
FT /evidence="ECO:0000305|PubMed:28966840"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28966840,
FT ECO:0007744|PDB:5NX5"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28966840,
FT ECO:0007744|PDB:5NX5"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5GMG2"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5GMG2"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5GMG2"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28966840,
FT ECO:0007744|PDB:5NX5"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5GMG2"
FT BINDING 308..309
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5GMG2"
FT HELIX 18..31
FT /evidence="ECO:0007829|PDB:5NX5"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:5NX5"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:5NX5"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:5NX5"
FT HELIX 62..82
FT /evidence="ECO:0007829|PDB:5NX5"
FT HELIX 89..105
FT /evidence="ECO:0007829|PDB:5NX5"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:5NX4"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:5NX5"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:5NX5"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:5NX5"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:5NX5"
FT HELIX 178..189
FT /evidence="ECO:0007829|PDB:5NX5"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:5NX5"
FT HELIX 201..228
FT /evidence="ECO:0007829|PDB:5NX5"
FT HELIX 234..242
FT /evidence="ECO:0007829|PDB:5NX5"
FT HELIX 246..269
FT /evidence="ECO:0007829|PDB:5NX5"
FT HELIX 271..278
FT /evidence="ECO:0007829|PDB:5NX5"
FT HELIX 282..303
FT /evidence="ECO:0007829|PDB:5NX5"
SQ SEQUENCE 329 AA; 36397 MW; 0FBDBC7D8C878252 CRC64;
MQEFEFAVPA PSRVSPDLAR ARARHLDWVH AMDLVRGEEA RRRYEFSCVA DIGAYGYPHA
TGADLDLCVD VLGWTFLFDD QFDAGDGRER DALAVCAELT DLLWKGTAAT AASPPIVVAF
SDCWERMRAG MSDAWRRRTV HEWVDYLAGW PTKLADRAHG AVLDPAAHLR ARHRTICCRP
LFALAERVGG YEVPRRAWHS SRLDGMRFTT SDAVIGMNEL HSFEKDRAQG HANLVLSLVH
HGGLTGPEAV TRVCDLVQGS IESFLRLRSG LPELGRALGV EGAVLDRYAD ALSAFCRGYH
DWGRGASRYT TRDHPGDLGL ENLVARSSG
