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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //