ID Q40322_MENSP Unreviewed; 599 AA.
AC Q40322;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=4S-limonene synthase {ECO:0000313|EMBL:AAC37366.1};
OS Mentha spicata (Spearmint).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Menthinae;
OC Mentha.
OX NCBI_TaxID=29719 {ECO:0000313|EMBL:AAC37366.1};
RN [1] {ECO:0000313|EMBL:AAC37366.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:AAC37366.1};
RX PubMed=8226816;
RA Colby S.M., Alonso W.R., Katahira E.J., McGarvey D.J., Croteau R.;
RT "4S-limonene synthase from the oil glands of spearmint (Mentha spicata).
RT cDNA isolation, characterization, and bacterial expression of the
RT catalytically active monoterpene cyclase.";
RL J. Biol. Chem. 268:23016-23024(1993).
RN [2] {ECO:0007829|PDB:2ONG, ECO:0007829|PDB:2ONH}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 57-599 IN COMPLEX WITH MN(2+).
RX PubMed=17372193; DOI=10.1073/pnas.0700915104;
RA Hyatt D.C., Youn B., Zhao Y., Santhamma B., Coates R.M., Croteau R.B.,
RA Kang C.;
RT "Structure of limonene synthase, a simple model for terpenoid cyclase
RT catalysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5360-5365(2007).
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229}.
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DR EMBL; L13459; AAC37366.1; -; mRNA.
DR PIR; A48863; A48863.
DR PDB; 2ONG; X-ray; 2.70 A; A/B=57-599.
DR PDB; 2ONH; X-ray; 2.70 A; A/B=57-599.
DR PDBsum; 2ONG; -.
DR PDBsum; 2ONH; -.
DR AlphaFoldDB; Q40322; -.
DR SMR; Q40322; -.
DR KEGG; ag:AAC37366; -.
DR BioCyc; MetaCyc:MONOMER-6782; -.
DR SABIO-RK; Q40322; -.
DR EvolutionaryTrace; Q40322; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1.
DR Gene3D; 1.50.10.130; Terpene synthase, N-terminal domain; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034741; Terpene_cyclase-like_1_C.
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 PANTHER; PTHR31225; OS04G0344100 PROTEIN-RELATED; 1.
DR PANTHER; PTHR31225:SF223; TERPENE SYNTHASE 10-LIKE ISOFORM X1; 1.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SFLD; SFLDG01604; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SFLD; SFLDG01014; Terpene_Cyclase_Like_1_N-term; 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR SUPFAM; SSF48576; Terpenoid synthases; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:2ONG, ECO:0007829|PDB:2ONH};
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0007829|PDB:2ONG};
KW Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 68..245
FT /note="Terpene synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01397"
FT DOMAIN 304..542
FT /note="Terpene synthase metal-binding"
FT /evidence="ECO:0000259|Pfam:PF03936"
FT BINDING 352
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:2ONG, ECO:0007829|PDB:2ONH"
FT BINDING 356
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:2ONG, ECO:0007829|PDB:2ONH"
FT BINDING 430
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:2ONG, ECO:0007829|PDB:2ONH"
FT BINDING 496
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0007829|PDB:2ONG"
FT BINDING 496
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:2ONH"
FT BINDING 500
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0007829|PDB:2ONG"
FT BINDING 509
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:2ONG, ECO:0007829|PDB:2ONH"
SQ SEQUENCE 599 AA; 69843 MW; 8BF53D23329CAF65 CRC64;
MALKVLSVAT QMAIPSNLTT CLQPSHFKSS PKLLSSTNSS SRSRLRVYCS SSQLTTERRS
GNYNPSRWDV NFIQSLLSDY KEDKHVIRAS ELVTLVKMEL EKETDQIRQL ELIDDLQRMG
LSDHFQNEFK EILSSIYLDH HYYKNPFPKE ERDLYSTSLA FRLLREHGFQ VAQEVFDSFK
NEEGEFKESL SDDTRGLLQL YEASFLLTEG ETTLESAREF ATKFLEEKVN EGGVDGDLLT
RIAYSLDIPL HWRIKRPNAP VWIEWYRKRP DMNPVVLELA ILDLNIVQAQ FQEELKESFR
WWRNTGFVEK LPFARDRLVE CYFWNTGIIE PRQHASARIM MGKVNALITV IDDIYDVYGT
LEELEQFTDL IRRWDINSID QLPDYMQLCF LALNNFVDDT SYDVMKEKGV NVIPYLRQSW
VDLADKYMVE ARWFYGGHKP SLEEYLENSW QSISGPCMLT HIFFRVTDSF TKETVDSLYK
YHDLVRWSSF VLRLADDLGT SVEEVSRGDV PKSLQCYMSD YNASEAEARK HVKWLIAEVW
KKMNAERVSK DSPFGKDFIG CAVDLGRMAQ LMYHNGDGHG TQHPIIHQQM TRTLFEPFA
//
