RFS_PEA
ID RFS_PEA Reviewed; 798 AA.
AC Q8VWN6;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Galactinol--sucrose galactosyltransferase;
DE EC=2.4.1.82;
DE AltName: Full=Raffinose synthase;
GN Name=RFS;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Kelvedon Wonder; TISSUE=Seed;
RX PubMed=12244450; DOI=10.1007/s00425-002-0804-7;
RA Peterbauer T., Mach L., Mucha J., Richter A.;
RT "Functional expression of a cDNA encoding pea (Pisum sativum L.) raffinose
RT synthase, partial purification of the enzyme from maturing seeds, and
RT steady-state kinetic analysis of raffinose synthesis.";
RL Planta 215:839-846(2002).
CC -!- FUNCTION: Transglycosidase operating by a ping-pong reaction mechanism.
CC Involved in the synthesis of raffinose, a major soluble carbohydrate in
CC seeds, roots and tubers. Able to utilize D-ononitol and D-pinitol as
CC acceptors. May also act as a glycoside hydrolase.
CC {ECO:0000269|PubMed:12244450}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-galactosyl-(1->3)-1D-myo-inositol + sucrose = myo-
CC inositol + raffinose; Xref=Rhea:RHEA:20161, ChEBI:CHEBI:16634,
CC ChEBI:CHEBI:17268, ChEBI:CHEBI:17505, ChEBI:CHEBI:17992; EC=2.4.1.82;
CC Evidence={ECO:0000269|PubMed:12244450};
CC -!- ACTIVITY REGULATION: Inhibited by 1-deoxygalactonojirimycin. Not
CC inhibited by stachyose. Strong inhibition of the hydrolytic activity by
CC sucrose. {ECO:0000269|PubMed:12244450}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.3 mM for galactinol for the raffinose synthesis activity
CC {ECO:0000269|PubMed:12244450};
CC KM=22.9 mM for sucrose for the raffinose synthesis activity
CC {ECO:0000269|PubMed:12244450};
CC KM=1.0 mM for galactinol for the galactinol hydrolysis activity
CC {ECO:0000269|PubMed:12244450};
CC Vmax=199.2 pmol/sec/mg enzyme for the raffinose synthesis activity
CC {ECO:0000269|PubMed:12244450};
CC Vmax=27.3 pmol/sec/mg enzyme for the galactinol hydrolysis activity
CC {ECO:0000269|PubMed:12244450};
CC Note=partially purified enzyme.;
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:12244450};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolases 36 family.
CC {ECO:0000305}.
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DR EMBL; AJ426475; CAD20127.2; -; mRNA.
DR AlphaFoldDB; Q8VWN6; -.
DR CAZy; GH36; Glycoside Hydrolase Family 36.
DR PRIDE; Q8VWN6; -.
DR EnsemblPlants; Psat0s2597g0160.1; Psat0s2597g0160.1.cds; Psat0s2597g0160.
DR Gramene; Psat0s2597g0160.1; Psat0s2597g0160.1.cds; Psat0s2597g0160.
DR BioCyc; MetaCyc:MON-12496; -.
DR BRENDA; 2.4.1.82; 4872.
DR GO; GO:0047274; F:galactinol-sucrose galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR008811; Glycosyl_hydrolases_36.
DR PANTHER; PTHR31268; PTHR31268; 1.
DR Pfam; PF05691; Raffinose_syn; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycosyltransferase; Transferase.
FT CHAIN 1..798
FT /note="Galactinol--sucrose galactosyltransferase"
FT /id="PRO_0000389254"
SQ SEQUENCE 798 AA; 88717 MW; 8D3F3ED5BF8617B7 CRC64;
MAPPSITKTA TQQDVISTVD IGNSPLLSIS LDQSRNFLVN GHPFLTQVPP NITTTTTSTP
SPFLDFKSNK DTIANNNNTL QQQGCFVGFN TTEAKSHHVV PLGKLKGIKF TSIFRFKVWW
TTHWVGTNGH ELQHETQILI LDKNISLGRP YVLLLPILEN SFRTSLQPGL NDYVDMSVES
GSTHVTGSTF KACLYLHLSN DPYRLVKEAV KVIQTKLGTF KTLEEKTPPS IIEKFGWCTW
DAFYLKVHPK GVWEGVKALT DGGCPPGFVI IDDGWQSISH DDDDPVTERD GMNRTSAGEQ
MPCRLIKYEE NYKFREYENG DNGGKKGLVG FVRDLKEEFR SVESVYVWHA LCGYWGGVRP
KVCGMPEAKV VVPKLSPGVK MTMEDLAVDK IVENGVGLVP PNLAQEMFDG IHSHLESAGI
DGVKVDVIHL LELLSEEYGG RVELAKAYYK ALTSSVNKHF KGNGVIASME HCNDFFLLGT
EAISLGRVGD DFWCCDPSGD PNGTYWLQGC HMVHCAYNSL WMGNFIHPDW DMFQSTHPCA
EFHAASRAIS GGPVYVSDCV GNHNFKLLKS FVLPDGSILR CQHYALPTRD CLFEDPLHNG
KTMLKIWNLN KYAGVLGLFN CQGGGWCPET RRNKSASEFS HAVTCYASPE DIEWCNGKTP
MDIKGVDVFA VYFFKEKKLS LMKCSDRLEV SLEPFSFELM TVSPLKVFSK RLIQFAPIGL
VNMLNSGGAV QSLEFDDSAS LVKIGVRGCG ELSVFASEKP VCCKIDGVSV EFDYEDKMVR
VQILWPGSST LSLVEFLF