NUDT1_ROSHC
ID NUDT1_ROSHC Reviewed; 150 AA.
AC M4I1C6;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Geranyl diphosphate phosphohydrolase {ECO:0000305};
DE EC=3.6.1.68 {ECO:0000269|PubMed:26138978};
DE AltName: Full=Nudix hydrolase 1 {ECO:0000303|PubMed:26138978};
DE Short=RhNUDX1 {ECO:0000303|PubMed:26138978};
GN Name=NUDIX1 {ECO:0000303|PubMed:26138978};
OS Rosa hybrid cultivar.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC Rosa.
OX NCBI_TaxID=128735 {ECO:0000312|EMBL:AFW17224.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Papa Meilland;
RX PubMed=26138978; DOI=10.1126/science.aab0696;
RA Magnard J.L., Roccia A., Caissard J.C., Vergne P., Sun P., Hecquet R.,
RA Dubois A., Hibrand-Saint Oyant L., Jullien F., Nicole F., Raymond O.,
RA Huguet S., Baltenweck R., Meyer S., Claudel P., Jeauffre J., Rohmer M.,
RA Foucher F., Hugueney P., Bendahmane M., Baudino S.;
RT "PLANT VOLATILES. Biosynthesis of monoterpene scent compounds in roses.";
RL Science 349:81-83(2015).
CC -!- FUNCTION: Involved in a cytosolic pathway for the biosynthesis of free
CC monoterpene alcohols that contribute to fragrance. Lacks terpene
CC synthase activity, but has a diphosphohydrolase activity with geranyl
CC diphosphate and farnesyl diphosphate as substrates. No activity with 8-
CC oxo-dGTP and dGTP and unable to dephosphorylate geranyl phosphate to
CC geraniol. {ECO:0000269|PubMed:26138978}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (2E)-geranyl phosphate + H(+)
CC + phosphate; Xref=Rhea:RHEA:47944, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:88107; EC=3.6.1.68;
CC Evidence={ECO:0000269|PubMed:26138978};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=140 nM for geranyl diphosphate {ECO:0000269|PubMed:26138978};
CC KM=480 nM for farnesyl diphosphate {ECO:0000269|PubMed:26138978};
CC Note=kcat is 0.02 sec(-1) with geranyl diphosphate as substrate. kcat
CC is 0.0033 sec(-1) with farnesyl diphosphate as substrate.
CC {ECO:0000269|PubMed:26138978};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:26138978};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26138978}.
CC -!- TISSUE SPECIFICITY: Expressed in petals. Little or no expression in
CC stamens, sepals or young leaves. {ECO:0000269|PubMed:26138978}.
CC -!- DEVELOPMENTAL STAGE: Increased expression at later stages of flower
CC development. {ECO:0000269|PubMed:26138978}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC {ECO:0000255|RuleBase:RU003476}.
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DR EMBL; JQ820249; AFW17224.1; -; mRNA.
DR PDB; 6YPB; X-ray; 1.70 A; A=1-150.
DR PDB; 6YPF; X-ray; 1.45 A; A=1-150.
DR PDBsum; 6YPB; -.
DR PDBsum; 6YPF; -.
DR AlphaFoldDB; M4I1C6; -.
DR SMR; M4I1C6; -.
DR KEGG; ag:AFW17224; -.
DR BioCyc; MetaCyc:MON-19526; -.
DR BRENDA; 3.6.1.68; 7163.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR020476; Nudix_hydrolase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Magnesium; Metal-binding.
FT CHAIN 1..150
FT /note="Geranyl diphosphate phosphohydrolase"
FT /id="PRO_0000440620"
FT DOMAIN 14..147
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 48..69
FT /note="Nudix box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT BINDING 63
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT STRAND 15..25
FT /evidence="ECO:0007829|PDB:6YPF"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:6YPF"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:6YPF"
FT HELIX 56..68
FT /evidence="ECO:0007829|PDB:6YPF"
FT STRAND 72..84
FT /evidence="ECO:0007829|PDB:6YPF"
FT STRAND 93..105
FT /evidence="ECO:0007829|PDB:6YPF"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:6YPF"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:6YPF"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:6YPF"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:6YPF"
FT HELIX 135..142
FT /evidence="ECO:0007829|PDB:6YPF"
SQ SEQUENCE 150 AA; 16790 MW; 18B95E4B31592A6E CRC64;
MGNETVVVAE TAGSIKVAVV VCLLRGQNVL LGRRRSSLGD STFSLPSGHL EFGESFEECA
ARELKEETDL DIGKIELLTV TNNLFLDEAK PSQYVAVFMR AVLADPRQEP QNIEPEFCDG
WGWYEWDNLP KPLFWPLDNV VQDGFNPFPT
