ID   RFS_ORYSJ               Reviewed;         783 AA.
AC   Q5VQG4; Q0JQC7;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Galactinol--sucrose galactosyltransferase;
DE            EC=2.4.1.82;
DE   AltName: Full=Raffinose synthase;
GN   Name=RFS; OrderedLocusNames=Os01g0170000, LOC_Os01g07530;
GN   ORFNames=OJ1276_B06.38, OsJ_00538, P0583G08.2;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC
RP   ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=17206375; DOI=10.1007/s10529-006-9268-3;
RA   Li S., Li T., Kim W.-D., Kitaoka M., Yoshida S., Nakajima M., Kobayashi H.;
RT   "Characterization of raffinose synthase from rice (Oryza sativa L. var.
RT   Nipponbare).";
RL   Biotechnol. Lett. 29:635-640(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
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. Specific for galactinol and p-nitrophenyl-
CC       alpha-D-galactoside as galactosyl donors. Able to utilize sucrose,
CC       lactose, 4-beta-galactobiose, N-acetyl-D-lactosamine, trehalose and
CC       lacto-N-biose as acceptors. May also act as a glycoside hydrolase.
CC       {ECO:0000269|PubMed:17206375}.
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:17206375};
CC   -!- ACTIVITY REGULATION: Inhibited by Ag(2)+, Hg(2+), Zn(2+), p-
CC       chloromercuribenzoate (pCMB) and 1-deoxygalactonojirimycin.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=25.6 nmol/sec/mg enzyme toward raffinose for the raffinose
CC         synthesis activity {ECO:0000269|PubMed:17206375};
CC         Vmax=6.8 nmol/sec/mg enzyme toward p-nitrophenyl-alpha-D-galactoside
CC         for the hydrolysis activity {ECO:0000269|PubMed:17206375};
CC         Vmax=8.5 nmol/sec/mg enzyme toward galactinol for the hydrolysis
CC         activity {ECO:0000269|PubMed:17206375};
CC         Vmax=5.7 nmol/sec/mg enzyme toward raffinose for the hydrolysis
CC         activity {ECO:0000269|PubMed:17206375};
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:17206375};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.
CC         {ECO:0000269|PubMed:17206375};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolases 36 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF04051.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP003282; BAD68247.1; -; Genomic_DNA.
DR   EMBL; AP003339; BAD68321.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF04051.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM000138; EAZ10704.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5VQG4; -.
DR   STRING; 4530.OS01T0170000-01; -.
DR   PaxDb; Q5VQG4; -.
DR   PRIDE; Q5VQG4; -.
DR   eggNOG; ENOG502QTKB; Eukaryota.
DR   HOGENOM; CLU_051121_0_0_1; -.
DR   InParanoid; Q5VQG4; -.
DR   PlantReactome; R-OSA-1119417; Stachyose biosynthesis.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000007752; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   Genevisible; Q5VQG4; OS.
DR   GO; GO:0047274; F:galactinol-sucrose galactosyltransferase activity; IDA:Gramene.
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; Direct protein sequencing; Glycosyltransferase;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000305|PubMed:17206375"
FT   CHAIN           2..783
FT                   /note="Galactinol--sucrose galactosyltransferase"
FT                   /id="PRO_0000389255"
SQ   SEQUENCE   783 AA;  85533 MW;  59BB443A5965DC1D CRC64;
     MAPNLSKAKD DLIGDVVAVD GLIKPPRFTL KGKDLAVDGH PFLLDVPANI RLTPASTLVP
     NSDVPAAAAG SFLGFDAPAA KDRHVVPIGK LRDTRFMSIF RFKVWWTTHW VGTNGRDVEN
     ETQMMILDQS GTKSSPTGPR PYVLLLPIVE GPFRACLESG KAEDYVHMVL ESGSSTVRGS
     VFRSAVYLHA GDDPFDLVKD AMRVVRAHLG TFRLMEEKTP PPIVDKFGWC TWDAFYLKVH
     PEGVWEGVRR LADGGCPPGL VLIDDGWQSI CHDDDDLGSG AEGMNRTSAG EQMPCRLIKF
     QENYKFREYK GGMGGFVREM KAAFPTVEQV YVWHALCGYW GGLRPGAPGL PPAKVVAPRL
     SPGLQRTMED LAVDKIVNNG VGLVDPRRAR ELYEGLHSHL QASGIDGVKV DVIHLLEMVC
     EEYGGRVELA KAYFAGLTES VRRHFNGNGV IASMEHCNDF MLLGTEAVAL GRVGDDFWCT
     DPSGDPDGTF WLQGCHMVHC AYNSLWMGAF IHPDWDMFQS THPCAAFHAA SRAVSGGPVY
     VSDAVGCHDF DLLRRLALPD GTILRCERYA LPTRDCLFAD PLHDGKTMLK IWNVNKFSGV
     LGAFNCQGGG WSREARRNMC AAGFSVPVTA RASPADVEWS HGGGGGDRFA VYFVEARKLQ
     LLRRDESVEL TLEPFTYELL VVAPVRAIVS PELGIGFAPI GLANMLNAGG AVQGFEAARK
     DGDVAAEVAV KGAGEMVAYS SARPRLCKVN GQDAEFKYED GIVTVDVPWT GSSKKLSRVE
     YFY