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Coumarin 8-geranyltransferase 1, chloroplastic (EC 2.5.1.138) (Prenyltransferase 1) (ClPT1) (Umbelliferone 8-C-geranyltransferase) (U8GT)

 CGT1A_CITLI             Reviewed;         407 AA.
A0A077K8G3;
05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
29-OCT-2014, sequence version 1.
27-SEP-2017, entry version 9.
RecName: Full=Coumarin 8-geranyltransferase 1, chloroplastic;
EC=2.5.1.138 {ECO:0000269|PubMed:25077796};
AltName: Full=Prenyltransferase 1 {ECO:0000303|PubMed:25077796};
Short=ClPT1 {ECO:0000303|PubMed:25077796};
AltName: Full=Umbelliferone 8-C-geranyltransferase {ECO:0000303|PubMed:25077796};
Short=U8GT {ECO:0000303|PubMed:25077796};
Flags: Precursor;
Name=ClPT1 {ECO:0000303|PubMed:25077796};
Synonyms=PT1a {ECO:0000303|PubMed:25077796};
Citrus limon (Lemon) (Citrus medica var. limon).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Sapindales; Rutaceae; Aurantioideae;
Citrus.
NCBI_TaxID=2708 {ECO:0000312|EMBL:BAP27988.1};
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=cv. Lisbon;
PubMed=25077796; DOI=10.1104/pp.114.246892;
Munakata R., Inoue T., Koeduka T., Karamat F., Olry A., Sugiyama A.,
Takanashi K., Dugrand A., Froelicher Y., Tanaka R., Uto Y., Hori H.,
Azuma J., Hehn A., Bourgaud F., Yazaki K.;
"Molecular cloning and characterization of a geranyl diphosphate-
specific aromatic prenyltransferase from lemon.";
Plant Physiol. 166:80-90(2014).
-!- FUNCTION: Prenyltransferase specific for geranyl diphosphate as
prenyl donor and coumarin as prenyl acceptor. Can use
umbelliferone and esculetin as substrates, and with a lower
activity, 5,7-dihydroxy-coumarin and 5-methoxy-7-hydroxycoumarin.
No activity with 5-hydroxy-7-methoxycoumarin, bergaptol,
xanthotoxol, p-coumaric acid, caffeic acid, 2,4-dihydroxycinnamic
acid, kaempferol, genistein or homogentisate. No activity with
dimethylallyl diphosphate, farnesyl diphosphate or geranylgeranyl
diphosphate as prenyl donors. {ECO:0000269|PubMed:25077796}.
-!- CATALYTIC ACTIVITY: Geranyl diphosphate + umbelliferone =
diphosphate + 8-geranylumbelliferone.
{ECO:0000269|PubMed:25077796}.
-!- CATALYTIC ACTIVITY: Geranyl diphosphate + esculetin = diphosphate
+ 8-geranylesculetin. {ECO:0000269|PubMed:25077796}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:25077796};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=6.1 uM for umbelliferone {ECO:0000269|PubMed:25077796};
KM=4.8 uM for geranyl diphosphate {ECO:0000269|PubMed:25077796};
-!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
{ECO:0000269|PubMed:25077796}; Multi-pass membrane protein
{ECO:0000255}.
-!- TISSUE SPECIFICITY: Expressed in leaves. Detected in the flavedo
of lemon peels, but not in albedo. {ECO:0000269|PubMed:25077796}.
-!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
{ECO:0000305}.
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EMBL; AB813876; BAP27988.1; -; mRNA.
KEGG; ag:BAP27988; -.
KO; K21587; -.
GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004659; F:prenyltransferase activity; IDA:UniProtKB.
InterPro; IPR000537; UbiA_prenyltransferase.
Pfam; PF01040; UbiA; 1.
1: Evidence at protein level;
Chloroplast; Membrane; Plastid; Transferase; Transit peptide;
Transmembrane; Transmembrane helix.
TRANSIT 1 81 Chloroplast. {ECO:0000255}.
CHAIN 82 407 Coumarin 8-geranyltransferase 1,
chloroplastic.
/FTId=PRO_0000440665.
TRANSMEM 121 141 Helical. {ECO:0000255}.
TRANSMEM 184 204 Helical. {ECO:0000255}.
TRANSMEM 209 229 Helical. {ECO:0000255}.
TRANSMEM 248 268 Helical. {ECO:0000255}.
TRANSMEM 279 299 Helical. {ECO:0000255}.
TRANSMEM 328 348 Helical. {ECO:0000255}.
TRANSMEM 352 372 Helical. {ECO:0000255}.
TRANSMEM 386 406 Helical. {ECO:0000255}.
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


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