CGT1A_CITLI
ID CGT1A_CITLI Reviewed; 407 AA.
AC A0A077K8G3;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Coumarin 8-geranyltransferase 1, chloroplastic;
DE EC=2.5.1.138 {ECO:0000269|PubMed:25077796};
DE AltName: Full=Prenyltransferase 1 {ECO:0000303|PubMed:25077796};
DE Short=ClPT1 {ECO:0000303|PubMed:25077796};
DE AltName: Full=Umbelliferone 8-C-geranyltransferase {ECO:0000303|PubMed:25077796};
DE Short=U8GT {ECO:0000303|PubMed:25077796};
DE Flags: Precursor;
GN Name=ClPT1 {ECO:0000303|PubMed:25077796};
GN Synonyms=PT1a {ECO:0000303|PubMed:25077796};
OS Citrus limon (Lemon) (Citrus medica var. limon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2708 {ECO:0000312|EMBL:BAP27988.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Lisbon;
RX PubMed=25077796; DOI=10.1104/pp.114.246892;
RA Munakata R., Inoue T., Koeduka T., Karamat F., Olry A., Sugiyama A.,
RA Takanashi K., Dugrand A., Froelicher Y., Tanaka R., Uto Y., Hori H.,
RA Azuma J., Hehn A., Bourgaud F., Yazaki K.;
RT "Molecular cloning and characterization of a geranyl diphosphate-specific
RT aromatic prenyltransferase from lemon.";
RL Plant Physiol. 166:80-90(2014).
CC -!- FUNCTION: Prenyltransferase specific for geranyl diphosphate as prenyl
CC donor and coumarin as prenyl acceptor. Can use umbelliferone and
CC esculetin as substrates, and with a lower activity, 5,7-dihydroxy-
CC coumarin and 5-methoxy-7-hydroxycoumarin. No activity with 5-hydroxy-7-
CC methoxycoumarin, bergaptol, xanthotoxol, p-coumaric acid, caffeic acid,
CC 2,4-dihydroxycinnamic acid, kaempferol, genistein or homogentisate. No
CC activity with dimethylallyl diphosphate, farnesyl diphosphate or
CC geranylgeranyl diphosphate as prenyl donors.
CC {ECO:0000269|PubMed:25077796}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + umbelliferone = 8-
CC geranylumbelliferone + diphosphate; Xref=Rhea:RHEA:51860,
CC ChEBI:CHEBI:27510, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:134358; EC=2.5.1.138;
CC Evidence={ECO:0000269|PubMed:25077796};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + esculetin = 8-geranylesculetin +
CC diphosphate; Xref=Rhea:RHEA:51864, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057, ChEBI:CHEBI:134359, ChEBI:CHEBI:490095;
CC EC=2.5.1.138; Evidence={ECO:0000269|PubMed:25077796};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25077796};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.1 uM for umbelliferone {ECO:0000269|PubMed:25077796};
CC KM=4.8 uM for geranyl diphosphate {ECO:0000269|PubMed:25077796};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:25077796}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. Detected in the flavedo of
CC lemon peels, but not in albedo. {ECO:0000269|PubMed:25077796}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB813876; BAP27988.1; -; mRNA.
DR AlphaFoldDB; A0A077K8G3; -.
DR SMR; A0A077K8G3; -.
DR KEGG; ag:BAP27988; -.
DR BRENDA; 2.5.1.138; 1413.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004659; F:prenyltransferase activity; IDA:UniProtKB.
DR Gene3D; 1.10.357.140; -; 1.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR044878; UbiA_sf.
DR Pfam; PF01040; UbiA; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Membrane; Plastid; Transferase; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..81
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 82..407
FT /note="Coumarin 8-geranyltransferase 1, chloroplastic"
FT /id="PRO_0000440665"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 407 AA; 45250 MW; 66C15B12EFAA5F70 CRC64;
MLQMHSNSSF SPKCYYPLQH AGCVKTLQLP LTKVHGGLNR SESKNYAIKC TQSDSFYSTN
KIRNNENSSS RNCKPFNKYR VAVTLQQQDC ASNNEDDINS TSFRDVLLKK LHALYVFTRP
FAMIGTIVGI TSIAILPLQS FADLTPKYFM EFLKALLSAV LMNNYVGTVN QVADVEIDKV
NKPGLPLASG DLSVGTGLAI TLILSLTSLA IALSLQSPPL IFGLIVWFLL GTAYSVDLPF
LRWKTNPFLA GMCMVIVFGL VYQFSFFIHF QKYVLGRPVV ITRPLIFAAA IISTISAVMS
LLKDIPDEDG DKQFGYQSIS SKLGKENVLR LCVYALFFAY GVAVIVGASS SFQLGKLVSI
IGHSTLAFLL WLRAQTVDLS NNASTFSFYL FVWKLFYGEY LLIHFLR
