CGT1B_CITLI
ID CGT1B_CITLI Reviewed; 407 AA.
AC A0A077K9K6;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 25-MAY-2022, entry version 13.
DE RecName: Full=Coumarin 8-geranyltransferase 1b, chloroplastic;
DE EC=2.5.1.138 {ECO:0000269|PubMed:25077796};
DE AltName: Full=Prenyltransferase 1b {ECO:0000303|PubMed:25077796};
DE Short=ClPT1ba {ECO:0000303|PubMed:25077796};
DE Flags: Precursor;
GN Name=Cl-PT1b {ECO:0000312|EMBL:BAP27989.1};
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:BAP27989.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000250|UniProtKB:A0A077K8G3}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB813877; BAP27989.1; -; mRNA.
DR AlphaFoldDB; A0A077K9K6; -.
DR SMR; A0A077K9K6; -.
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 1b, chloroplastic"
FT /id="PRO_0000440666"
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 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"
SQ SEQUENCE 407 AA; 45312 MW; 8A171E62EFBC33B8 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 NNASTYSFYM FIWKLFYAEY LLIHFLR
