RAS_PLESU
ID RAS_PLESU Reviewed; 430 AA.
AC A0PDV5;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Rosmarinate synthase;
DE Short=CbRAS;
DE EC=2.3.1.140;
DE AltName: Full=Hydroxycinnamoyl transferase;
DE Short=CbHCT1;
GN Name=RAS;
OS Plectranthus scutellarioides (Coleus) (Solenostemon scutellarioides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae;
OC Plectranthinae; Plectranthus.
OX NCBI_TaxID=4142;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 64-74; 175-180; 225-234;
RP 330-336; 340-350; 397-401 AND 418-425, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17047986; DOI=10.1007/s00425-006-0393-y;
RA Berger A., Meinhard J., Petersen M.;
RT "Rosmarinic acid synthase is a new member of the superfamily of BAHD
RT acyltransferases.";
RL Planta 224:1503-1510(2006).
RN [2]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=21318289; DOI=10.1007/s00425-011-1367-2;
RA Sander M., Petersen M.;
RT "Distinct substrate specificities and unusual substrate flexibilities of
RT two hydroxycinnamoyltransferases, rosmarinic acid synthase and
RT hydroxycinnamoyl-CoA:shikimate hydroxycinnamoyl-transferase, from Coleus
RT blumei Benth.";
RL Planta 233:1157-1171(2011).
CC -!- FUNCTION: Involved in the biosynthesis of rosmarinic acid, a compound
CC with antiviral, antimicrobial and anti-inflammatory activities. Can use
CC 4-coumaroyl- and caffeoyl-CoA as hydroxycinnamoyl donors and 4-
CC Hydroxyphenyllactate and 3.4-Dihydroxyphenyllactate, but not shikimate
CC or quinate, as hydroxycinnamoyl acceptors. Can also putatively catalyze
CC amide formation with D-amino acids as acceptors.
CC {ECO:0000269|PubMed:17047986}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-(3,4-dihydroxyphenyl)lactate + (E)-caffeoyl-CoA = (R)-
CC rosmarinate + CoA; Xref=Rhea:RHEA:22344, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:71492, ChEBI:CHEBI:71493, ChEBI:CHEBI:87136;
CC EC=2.3.1.140; Evidence={ECO:0000269|PubMed:17047986,
CC ECO:0000269|PubMed:21318289};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.7 uM for 4-coumaroyl-CoA (in the presence of 4-
CC Hydroxyphenyllactate) {ECO:0000269|PubMed:21318289};
CC KM=3.4 uM for caffeoyl-CoA (in the presence of 4-
CC Hydroxyphenyllactate) {ECO:0000269|PubMed:21318289};
CC KM=1.3 uM for 4-coumaroyl-CoA (in the presence of 3.4-
CC Dihydroxyphenyllactate) {ECO:0000269|PubMed:21318289};
CC KM=4.0 uM for caffeoyl-CoA (in the presence of 3.4-
CC Dihydroxyphenyllactate) {ECO:0000269|PubMed:21318289};
CC KM=39 uM for 4-Hydroxyphenyllactate (in the presence of 4-coumaroyl-
CC CoA) {ECO:0000269|PubMed:21318289};
CC KM=219 uM for 4-Hydroxyphenyllactate (in the presence of caffeoyl-
CC CoA) {ECO:0000269|PubMed:21318289};
CC KM=56 uM for 3.4-Dihydroxyphenyllactate (in the presence of 4-
CC coumaroyl-CoA) {ECO:0000269|PubMed:21318289};
CC KM=132 uM for 3.4-Dihydroxyphenyllactate (in the presence of
CC caffeoyl-CoA) {ECO:0000269|PubMed:21318289};
CC pH dependence:
CC Optimum pH is 7.8. {ECO:0000269|PubMed:21318289};
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; AM283092; CAK55166.1; -; mRNA.
DR PDB; 6MK2; X-ray; 3.35 A; A=1-430.
DR PDBsum; 6MK2; -.
DR AlphaFoldDB; A0PDV5; -.
DR SMR; A0PDV5; -.
DR BRENDA; 2.3.1.140; 1561.
DR GO; GO:0050266; F:rosmarinate synthase activity; IDA:UniProtKB.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Direct protein sequencing; Transferase.
FT CHAIN 1..430
FT /note="Rosmarinate synthase"
FT /id="PRO_0000422582"
FT REGION 178..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT CONFLICT 71..72
FT /note="YA -> SF (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:6MK2"
FT TURN 26..29
FT /evidence="ECO:0007829|PDB:6MK2"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:6MK2"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:6MK2"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:6MK2"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:6MK2"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:6MK2"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:6MK2"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:6MK2"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6MK2"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:6MK2"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:6MK2"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:6MK2"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:6MK2"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:6MK2"
FT HELIX 157..169
FT /evidence="ECO:0007829|PDB:6MK2"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:6MK2"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:6MK2"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:6MK2"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:6MK2"
FT HELIX 252..268
FT /evidence="ECO:0007829|PDB:6MK2"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:6MK2"
FT TURN 284..289
FT /evidence="ECO:0007829|PDB:6MK2"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:6MK2"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:6MK2"
FT HELIX 308..312
FT /evidence="ECO:0007829|PDB:6MK2"
FT HELIX 316..328
FT /evidence="ECO:0007829|PDB:6MK2"
FT HELIX 332..344
FT /evidence="ECO:0007829|PDB:6MK2"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:6MK2"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:6MK2"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:6MK2"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:6MK2"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:6MK2"
FT STRAND 409..416
FT /evidence="ECO:0007829|PDB:6MK2"
FT HELIX 417..420
FT /evidence="ECO:0007829|PDB:6MK2"
FT HELIX 422..427
FT /evidence="ECO:0007829|PDB:6MK2"
SQ SEQUENCE 430 AA; 47902 MW; C3FA18AD5C5F67EF CRC64;
MKIEVKDSTM IKPSAETPGG SLWLSNLDLL SPANYHTLSV HFYSHDGSDN FFDAAGLKES
LSRALVEFYP YAGRLKLNGN RLEIDCNNEG LLLVEAECDG ALDELGDFAP RPELNLIPKV
DYSRGISTYP LMVFQLTRFK CGGVALGVAN EHHLSDGVAA LHFINTWAHL SRGAPAPTPL
PHFDRSSLSA RNPPQPQFSH AEYQPPPTLE NPLPHTDIAH SRFKLTRDQL NSLKSKFKTA
PADGGAGKSY STFEVLAGHI WRSVCIARGL PEGQETKLHI PFDGRGRLQL PPGFFGNAIF
FATPIATCGE IESNSLNYAV RRVSDGVSRL DEDYLRSSID FLELQEDISK LAQGAHSFRC
PNLWVISWVW LPIYEPDFGW GKAVYMGPWA APFEGKSYLL PNPEKDGSLF VSITLHKQHM
ERFEKLFYEI
