SABS1_SALPM
ID SABS1_SALPM Reviewed; 581 AA.
AC A6XH06;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Sabinene synthase 1, chloroplastic {ECO:0000303|PubMed:17557809};
DE Short=Sp-SabS1 {ECO:0000303|PubMed:17557809};
DE EC=4.2.3.- {ECO:0000269|PubMed:17557809};
DE AltName: Full=Myrcene synthase {ECO:0000303|PubMed:17557809};
DE EC=4.2.3.15 {ECO:0000269|PubMed:17557809};
DE Flags: Precursor; Fragment;
GN Name=SabS1 {ECO:0000303|PubMed:17557809};
OS Salvia pomifera (Apple sage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Salviinae;
OC Salvia; Salvia incertae sedis.
OX NCBI_TaxID=396869;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF ILE-327; THR-328 AND
RP SER-436, CATALYTIC ACTIVITY, PATHWAY, AND SITE.
RX PubMed=17557809; DOI=10.1105/tpc.106.047779;
RA Kampranis S.C., Ioannidis D., Purvis A., Mahrez W., Ninga E.,
RA Katerelos N.A., Anssour S., Dunwell J.M., Degenhardt J., Makris A.M.,
RA Goodenough P.W., Johnson C.B.;
RT "Rational conversion of substrate and product specificity in a Salvia
RT monoterpene synthase: structural insights into the evolution of terpene
RT synthase function.";
RL Plant Cell 19:1994-2005(2007).
CC -!- FUNCTION: Monoterpene synthase (TPS) involved in the biosynthesis of
CC monoterpene natural products, components of the chemical defense
CC arsenal (PubMed:17557809). Catalyzes the conversion of (2E)-geranyl
CC diphosphate (GPP) into sabinene, and, as minor products, myrcene
CC (PubMed:17557809). {ECO:0000269|PubMed:17557809}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = diphosphate + sabinene;
CC Xref=Rhea:RHEA:68636, ChEBI:CHEBI:33019, ChEBI:CHEBI:50027,
CC ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:17557809};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68637;
CC Evidence={ECO:0000269|PubMed:17557809};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate;
CC Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.15;
CC Evidence={ECO:0000269|PubMed:17557809};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966;
CC Evidence={ECO:0000269|PubMed:17557809};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:17557809}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
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 {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; DQ785794; ABH07678.1; -; mRNA.
DR SMR; A6XH06; -.
DR BRENDA; 4.2.3.110; 15442.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0080015; F:sabinene synthase activity; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016099; P:monoterpenoid biosynthetic process; IDA:UniProtKB.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR InterPro; IPR001906; Terpene_synth_N.
DR InterPro; IPR036965; Terpene_synth_N_sf.
DR InterPro; IPR005630; Terpene_synthase_metal-bd.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT <1..28
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 29..581
FT /note="Sabinene synthase 1, chloroplastic"
FT /id="PRO_0000455077"
FT MOTIF 334..338
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 334
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 334
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 338
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 338
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 478
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 482
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 486
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT SITE 327
FT /note="Confers catalytic properties (activation of water
FT molecule and hydroxylation of the alpha-terpinyl cation)"
FT /evidence="ECO:0000269|PubMed:17557809"
FT MUTAGEN 327
FT /note="I->N: Slightly reduced ability to produce sabinene,
FT but acquired ability to produce limonene, 1,8-cineole and
FT alpha-terpineol from (2E)-geranyl diphosphate. Slightly
FT reduced ability to produce sabinene, but acquired ability
FT to produce limonene, 1,8-cineole and alpha-terpineol from
FT (2E)-geranyl diphosphate; when associated with A-328.
FT Slightly reduced ability to produce sabinene, lost ability
FT to produce myrcene, but acquired ability to produce alpha-
FT terpineol from (2E)-geranyl diphosphate; when associated
FT with A-328 and G-436."
FT /evidence="ECO:0000269|PubMed:17557809"
FT MUTAGEN 328
FT /note="T->A: Slightly reduced ability to produce sabinene,
FT but acquired ability to produce limonene, 1,8-cineole and
FT alpha-terpineol from (2E)-geranyl diphosphate; when
FT associated with N-327. Slightly reduced ability to produce
FT sabinene, lost ability to produce myrcene, but acquired
FT ability to produce alpha-terpineol from (2E)-geranyl
FT diphosphate; when associated with N-327 and G-436."
FT /evidence="ECO:0000269|PubMed:17557809"
FT MUTAGEN 436
FT /note="S->G: Slightly reduced ability to produce sabinene,
FT lost ability to produce myrcene, but acquired ability to
FT produce alpha-terpineol from (2E)-geranyl diphosphate; when
FT associated with N-327 and A-328."
FT /evidence="ECO:0000269|PubMed:17557809"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:ABH07678.1"
SQ SEQUENCE 581 AA; 68132 MW; 81FB5D8E9D9D82AA CRC64;
MPLNSLHNLE RKPSKAWSTS CTAPAARLQA SFSLQQEEPR QIRRSGDYQP SLWDFNYIQS
LNTPYKEQRY VNRQAELIMQ VRMLLKVKME AIQQLELIDD LQYLGLSYFF PDEIKQILSS
IHNEHRYFHN NDLYLTALGF RILRQHGFNV SEDVFDCFKT EKCSDFNANL AQDTKGMLQL
YEASFLLREG EDTLELARRF STRSLREKLD EDGDEIDEDL SSWIRHSLDL PLHWRIQGLE
ARWFLDAYAR RPDMNPLIFK LAKLNFNIVQ ATYQEELKDV SRWWNSSCLA EKLPFVRDRI
VECFFWAIGA FEPHQYSYQR KMAAIIITFV TIIDDVYDVY GTLEELELFT DMIRRWDNIS
ISQLPYYMQV CYLALYNFVS ERAYDILKDQ HFNSIPYLQR SWVSLVEGYL KEAYWYYNGY
KPSLEEYLNN AKISISAPTI ISQLYFTLAN STDETVIESL YEYHNILYLS GTILRLADDL
GTSQHELERG DVPKAIQCYM KDTNASEREA VEHVKFLIRE TWKEMNTVTT ASDCPFTDDL
VAVATNLARA AQFIYLDGDG HGVQHSEIHQ QMGGLLFQPY V
