RFS6_ARATH
ID RFS6_ARATH Reviewed; 749 AA.
AC Q8RX87; B9DFC4; B9DGW6; Q56X69;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Probable galactinol--sucrose galactosyltransferase 6;
DE EC=2.4.1.82;
DE AltName: Full=Protein DARK INDUCIBLE 10;
DE AltName: Full=Raffinose synthase 6;
GN Name=RFS6; Synonyms=DIN10, RS6; OrderedLocusNames=At5g20250;
GN ORFNames=F5O24.140;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP INDUCTION BY DARK AND SUCROSE, AND DEVELOPMENTAL STAGE.
RX PubMed=11240919; DOI=10.1034/j.1399-3054.2001.1110312.x;
RA Fujiki Y., Yoshikawa Y., Sato T., Inada N., Ito M., Nishida I.,
RA Watanabe A.;
RT "Dark-inducible genes from Arabidopsis thaliana are associated with leaf
RT senescence and repressed by sugars.";
RL Physiol. Plantarum 111:345-352(2001).
RN [7]
RP INDUCTION BY OXIDATIVE STRESS, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18502973; DOI=10.1104/pp.108.122465;
RA Nishizawa A., Yabuta Y., Shigeoka S.;
RT "Galactinol and raffinose constitute a novel function to protect plants
RT from oxidative damage.";
RL Plant Physiol. 147:1251-1263(2008).
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 (By similarity). {ECO:0000250}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8RX87-1; Sequence=Displayed;
CC -!- DEVELOPMENTAL STAGE: Expressed in 24 hours imbibed seeds and during
CC leaf senescence. {ECO:0000269|PubMed:11240919}.
CC -!- INDUCTION: By oxidative stress and by dark treatment. Down-regulated by
CC sucrose, but not by osmotic treatment. {ECO:0000269|PubMed:11240919,
CC ECO:0000269|PubMed:18502973}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolases 36 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL90901.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAN18198.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE99252.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF296825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92818.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92819.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92820.1; -; Genomic_DNA.
DR EMBL; AY090237; AAL90901.1; ALT_INIT; mRNA.
DR EMBL; BT000632; AAN18198.1; ALT_INIT; mRNA.
DR EMBL; AK227214; BAE99252.1; ALT_INIT; mRNA.
DR EMBL; AK221808; BAD93984.1; -; mRNA.
DR EMBL; AK316714; BAH19441.1; -; mRNA.
DR EMBL; AK317307; BAH19983.1; -; mRNA.
DR EMBL; AK318923; BAH57038.1; -; mRNA.
DR RefSeq; NP_001031910.1; NM_001036833.2. [Q8RX87-1]
DR RefSeq; NP_001190347.1; NM_001203418.1.
DR RefSeq; NP_197525.1; NM_122032.6. [Q8RX87-1]
DR RefSeq; NP_851044.2; NM_180713.4. [Q8RX87-1]
DR AlphaFoldDB; Q8RX87; -.
DR BioGRID; 17423; 3.
DR IntAct; Q8RX87; 2.
DR STRING; 3702.AT5G20250.4; -.
DR CAZy; GH36; Glycoside Hydrolase Family 36.
DR iPTMnet; Q8RX87; -.
DR PaxDb; Q8RX87; -.
DR PRIDE; Q8RX87; -.
DR ProteomicsDB; 236898; -. [Q8RX87-1]
DR EnsemblPlants; AT5G20250.1; AT5G20250.1; AT5G20250. [Q8RX87-1]
DR EnsemblPlants; AT5G20250.2; AT5G20250.2; AT5G20250. [Q8RX87-1]
DR EnsemblPlants; AT5G20250.3; AT5G20250.3; AT5G20250. [Q8RX87-1]
DR GeneID; 832147; -.
DR Gramene; AT5G20250.1; AT5G20250.1; AT5G20250. [Q8RX87-1]
DR Gramene; AT5G20250.2; AT5G20250.2; AT5G20250. [Q8RX87-1]
DR Gramene; AT5G20250.3; AT5G20250.3; AT5G20250. [Q8RX87-1]
DR KEGG; ath:AT5G20250; -.
DR Araport; AT5G20250; -.
DR eggNOG; ENOG502QPVE; Eukaryota.
DR HOGENOM; CLU_007066_0_0_1; -.
DR InParanoid; Q8RX87; -.
DR OMA; YCAKQTA; -.
DR OrthoDB; 142079at2759; -.
DR PhylomeDB; Q8RX87; -.
DR BioCyc; ARA:AT5G20250-MON; -.
DR BRENDA; 2.4.1.82; 399.
DR PRO; PR:Q8RX87; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8RX87; baseline and differential.
DR Genevisible; Q8RX87; AT.
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 2: Evidence at transcript level;
KW Alternative splicing; Carbohydrate metabolism; Glycosyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..749
FT /note="Probable galactinol--sucrose galactosyltransferase
FT 6"
FT /id="PRO_0000389259"
FT CONFLICT 302
FT /note="K -> R (in Ref. 5; BAH19983)"
FT /evidence="ECO:0000305"
FT CONFLICT 670
FT /note="M -> V (in Ref. 4; BAD93984)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 749 AA; 83116 MW; B8A9DEBB6A2407E7 CRC64;
MTIKPAVRIS DGNLIIKNRT ILTGVPDNVI TTSASEAGPV EGVFVGAVFN KEESKHIVPI
GTLRNSRFMS CFRFKLWWMA QRMGEMGRDI PYETQFLLVE SNDGSHLESD GANGVECNQK
VYTVFLPLIE GSFRSCLQGN VNDEVELCLE SGDVDTKRSS FTHSLYIHAG TDPFQTITDA
IRTVKLHLNS FRQRHEKKLP GIVDYFGWCT WDAFYQEVTQ EGVEAGLKSL AAGGTPPKFV
IIDDGWQSVE RDATVEAGDE KKESPIFRLT GIKENEKFKK KDDPNVGIKN IVKIAKEKHG
LKYVYVWHAI TGYWGGVRPG EEYGSVMKYP NMSKGVVEND PTWKTDVMTL QGLGLVSPKK
VYKFYNELHS YLADAGVDGV KVDVQCVLET LGGGLGGRVE LTRQFHQALD SSVAKNFPDN
GCIACMSHNT DALYCSKQAA VIRASDDFYP RDPVSHTIHI ASVAYNSVFL GEFMQPDWDM
FHSVHPAAEY HASARAISGG PLYVSDSPGK HNFELLRKLV LPDGSILRAR LPGRPTRDCL
FADPARDGVS LLKIWNMNKY TGVLGVYNCQ GAAWSSTERK NIFHQTKTDS LTGSIRGRDV
HSISEASTDP TTWNGDCAVY SQSRGELIVM PYNVSLPVSL KIREHEIFTV SPISHLVDGV
SFAPIGLVNM YNSGGAIEGL RYEAEKMKVV MEVKGCGKFG SYSSVKPKRC VVESNEIAFE
YDSSSGLVTF ELDKMPIENK RFHLIQVEL
