PULR_MENPI
ID PULR_MENPI Reviewed; 342 AA.
AC Q6WAU0; B0F4G8;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=(+)-pulegone reductase;
DE EC=1.3.1.81;
OS Mentha piperita (Peppermint) (Mentha aquatica x Mentha spicata).
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=34256;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=cv. Black Mitcham; TISSUE=Peltate glandular trichome;
RX PubMed=13679086; DOI=10.1016/s0003-9861(03)00390-4;
RA Ringer K.L., McConkey M.E., Davis E.M., Rushing G.W., Croteau R.;
RT "Monoterpene double-bond reductases of the (-)-menthol biosynthetic
RT pathway: isolation and characterization of cDNAs encoding (-)-
RT isopiperitenone reductase and (+)-pulegone reductase of peppermint.";
RL Arch. Biochem. Biophys. 418:80-92(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gupta M.K., Gupta S., Shasany A.K., Khanuja S.P.S.;
RT "Isolation of full-length genes of menthol biosynthesis pathway from Mentha
RT x piperita cv. Madhuras.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INDUCTION BY MENTHOFURAN, AND ACTIVITY REGULATION.
RX PubMed=14623962; DOI=10.1073/pnas.2436325100;
RA Mahmoud S.S., Croteau R.B.;
RT "Menthofuran regulates essential oil biosynthesis in peppermint by
RT controlling a downstream monoterpene reductase.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:14481-14486(2003).
CC -!- FUNCTION: Monoterpene synthase that catalyzes the specific reduction of
CC the 4,8-double bond of (+)-pulegone to produce both (-)-menthone and
CC (+)-isomenthone in a 70:30 ratio. Unable to utilize either (-)-
CC isopiperitenone or (+)-cis-isopulegone, or to catalyze the reverse
CC reaction with (-)-menthone or (+)-isomenthone. Has an absolute
CC requirement for NADPH.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,5R)-isomenthone + NADP(+) = (R)-pulegone + H(+) + NADPH;
CC Xref=Rhea:RHEA:25645, ChEBI:CHEBI:15378, ChEBI:CHEBI:35596,
CC ChEBI:CHEBI:36492, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.81;
CC Evidence={ECO:0000269|PubMed:13679086};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R,4S)-menthone + NADP(+) = (R)-pulegone + H(+) + NADPH;
CC Xref=Rhea:RHEA:25641, ChEBI:CHEBI:15378, ChEBI:CHEBI:15410,
CC ChEBI:CHEBI:35596, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.81;
CC Evidence={ECO:0000269|PubMed:13679086};
CC -!- ACTIVITY REGULATION: Not inhibited by (+)-menthofuran.
CC {ECO:0000269|PubMed:14623962}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.3 uM for (+)-pulegone {ECO:0000269|PubMed:13679086};
CC KM=6.9 uM for NADPH {ECO:0000269|PubMed:13679086};
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:13679086};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Down-regulated by (+)-menthofuran.
CC {ECO:0000269|PubMed:14623962}.
CC -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD family.
CC {ECO:0000305}.
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; AY300163; AAQ75423.1; -; mRNA.
DR EMBL; EU108701; ABW86885.1; -; mRNA.
DR PDB; 7EQL; X-ray; 2.72 A; A=1-342.
DR PDBsum; 7EQL; -.
DR AlphaFoldDB; Q6WAU0; -.
DR SMR; Q6WAU0; -.
DR KEGG; ag:AAQ75423; -.
DR BioCyc; MetaCyc:MON-6685; -.
DR BRENDA; 1.3.1.81; 3222.
DR UniPathway; UPA00213; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052579; F:(+)-pulegone reductase, (+)-isomenthone as substrate, activity; IDA:UniProtKB.
DR GO; GO:0052580; F:(+)-pulegone reductase, (-)-menthone as substrate, activity; IDA:UniProtKB.
DR GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
DR GO; GO:0042214; P:terpene metabolic process; IDA:UniProtKB.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR041694; ADH_N_2.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR045010; MDR_fam.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43205; PTHR43205; 1.
DR Pfam; PF16884; ADH_N_2; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; NADP; Oxidoreductase.
FT CHAIN 1..342
FT /note="(+)-pulegone reductase"
FT /id="PRO_0000398337"
FT BINDING 163..166
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 251..257
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 281..283
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT CONFLICT 35
FT /note="D -> N (in Ref. 2; ABW86885)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="R -> C (in Ref. 2; ABW86885)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="V -> I (in Ref. 2; ABW86885)"
FT /evidence="ECO:0000305"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:7EQL"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:7EQL"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:7EQL"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:7EQL"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:7EQL"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:7EQL"
FT STRAND 76..88
FT /evidence="ECO:0007829|PDB:7EQL"
FT STRAND 96..112
FT /evidence="ECO:0007829|PDB:7EQL"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:7EQL"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:7EQL"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:7EQL"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:7EQL"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:7EQL"
FT HELIX 166..176
FT /evidence="ECO:0007829|PDB:7EQL"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:7EQL"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:7EQL"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:7EQL"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:7EQL"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:7EQL"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:7EQL"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:7EQL"
FT STRAND 242..250
FT /evidence="ECO:0007829|PDB:7EQL"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:7EQL"
FT HELIX 267..271
FT /evidence="ECO:0007829|PDB:7EQL"
FT TURN 272..275
FT /evidence="ECO:0007829|PDB:7EQL"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:7EQL"
FT HELIX 283..289
FT /evidence="ECO:0007829|PDB:7EQL"
FT HELIX 290..297
FT /evidence="ECO:0007829|PDB:7EQL"
FT TURN 298..303
FT /evidence="ECO:0007829|PDB:7EQL"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:7EQL"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:7EQL"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:7EQL"
FT HELIX 319..327
FT /evidence="ECO:0007829|PDB:7EQL"
FT STRAND 333..339
FT /evidence="ECO:0007829|PDB:7EQL"
SQ SEQUENCE 342 AA; 37915 MW; 4BE6FB39761A1BDA CRC64;
MVMNKQIVLN NYINGSLKQS DLALRTSTIC MEIPDGCNGA ILVKNLYLSV NPYLILRMGK
LDIPQFDSIL PGSTIVSYGV SKVLDSTHPS YEKGELIWGS QAGWEEYTLI QNPYNLFKIQ
DKDVPLSYYV GILGMPGMTA YAGFFEICSP KKGETVFVTA AAGSVGQLVG QFAKMFGCYV
VGSAGSKEKV DLLKNKFGFD DAFNYKEESD YDTALKRHFP EGIDIYFDNV GGKMLEAVIN
NMRVHGRIAV CGMVSQYSLK QPEGVHNLLK LIPKQIRMQG FVVVDYYHLY PKFLEMVLPR
IKEGKVTYVE DISEGLESAP SALLGVYVGR NVGNQVVAVS RE
