FRIES_KALDA
ID FRIES_KALDA Reviewed; 767 AA.
AC E2IUA8;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Friedelin synthase;
DE Short=KdFRS;
DE EC=5.4.99.50;
OS Kalanchoe daigremontiana (Devil's backbone) (Bryophyllum daigremontianum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Saxifragales; Crassulaceae; Kalanchoe.
OX NCBI_TaxID=23013;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=20610397; DOI=10.1074/jbc.m109.098871;
RA Wang Z., Yeats T., Han H., Jetter R.;
RT "Cloning and characterization of oxidosqualene cyclases from Kalanchoe
RT daigremontiana: enzymes catalyzing up to 10 rearrangement steps yielding
RT friedelin and other triterpenoids.";
RL J. Biol. Chem. 285:29703-29712(2010).
CC -!- FUNCTION: Oxidosqualene cyclase that generates friedelin, a
CC triterpenoid product with the maximum number of rearrangements
CC possible. Friedelin is probably required to coat the leaf exterior as
CC defense compound against pathogens or herbivores.
CC {ECO:0000269|PubMed:20610397}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3-epoxysqualene = friedelin; Xref=Rhea:RHEA:31863,
CC ChEBI:CHEBI:5171, ChEBI:CHEBI:15441; EC=5.4.99.50;
CC Evidence={ECO:0000269|PubMed:20610397};
CC -!- TISSUE SPECIFICITY: Expressed only in the epidermal cells on both sides
CC of the leaf and not in internal leaf tissues.
CC {ECO:0000269|PubMed:20610397}.
CC -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC {ECO:0000305}.
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DR EMBL; HM623870; ADK35125.1; -; mRNA.
DR AlphaFoldDB; E2IUA8; -.
DR SMR; E2IUA8; -.
DR KEGG; ag:ADK35125; -.
DR BioCyc; MetaCyc:MON-17975; -.
DR GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR GO; GO:0016866; F:intramolecular transferase activity; IDA:UniProtKB.
DR GO; GO:0016104; P:triterpenoid biosynthetic process; IDA:UniProtKB.
DR CDD; cd02892; SQCY_1; 1.
DR InterPro; IPR032696; SQ_cyclase_C.
DR InterPro; IPR032697; SQ_cyclase_N.
DR InterPro; IPR018333; Squalene_cyclase.
DR InterPro; IPR002365; Terpene_synthase_CS.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11764; PTHR11764; 1.
DR Pfam; PF13243; SQHop_cyclase_C; 1.
DR Pfam; PF13249; SQHop_cyclase_N; 1.
DR SFLD; SFLDG01016; Prenyltransferase_Like_2; 1.
DR SUPFAM; SSF48239; SSF48239; 2.
DR TIGRFAMs; TIGR01787; squalene_cyclas; 1.
DR PROSITE; PS01074; TERPENE_SYNTHASES; 1.
PE 1: Evidence at protein level;
KW Isomerase; Repeat.
FT CHAIN 1..767
FT /note="Friedelin synthase"
FT /id="PRO_0000418483"
FT REPEAT 148..189
FT /note="PFTB 1"
FT REPEAT 640..681
FT /note="PFTB 2"
FT ACT_SITE 485
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P48449"
SQ SEQUENCE 767 AA; 88396 MW; A9F85D0CFB092B74 CRC64;
MWKLKIAEGG SDPYIYTTNN FVGRQIWEFD PQATDPQQLA KVEAARLNFY NHRHKIKPSS
DLLWRLQFLE EKDFRQNIAQ VKVEDGEEVS YEAATAALKR GVHFYSALQA SDGHWPAENA
GPMFFMSPLV MCLYITGHLN TIFTEEHRRE TLRYIYYHQN EDGGWGFHIE GQSTMFGTVL
NYICMRLLGE GPEGGQDNAV SRGRKWILDH GGATAIPSWG KTWLSIMGLC DWSGCNPMPP
EFWLLPSYLP MHPAKMWCYC RMVYMPMSYL YGKRFTTHIT PLILQLREEL HTQPYDQINW
KKVRHVCCKE DTYYPHPILQ DLIWDTLYLT TEPLLTRWPL NKLIRERALK KTMKHIHYED
ENSRYIVIGA VEKVLCMLAC WVEDPNGDYF KKHLARVPDY FWVAEDGMKI QSFGSQHWDT
AFFVQALLAS DMTDEIRTTL AKAHDCIKKS QVKDNPSGDF RSMYRHISKG AWTFSDQDHG
WQLSDCTAEG LKCCLLFSLM QPEVVGEAMP PERLYDSVNV LLYLQSKNGG MPGWEPAGES
EWLELLNPTE FFENIVIEHE YVECTSSAVQ ALVLFKKLYP LHRRKEVERF ITNGAKYLED
IQMPDGSWYG NWGVCFTYGA WFALEGLSAA GKTYNNCAAV RKGVDFLLNI QLEDGGWGES
YQSCPDKKYV PLEDNRSNLV QTSWALMGLI YAGQADRDPT PLHRAAKLLI NSQLEDGDFP
QQEIAGVFKM NCTLHFAAYR NIFPIWALAV YRRFCNPNSE AISKPSK