SUS3_ARATH
ID SUS3_ARATH Reviewed; 809 AA.
AC Q9M111; Q9SBD5;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Sucrose synthase 3;
DE Short=AtSUS3;
DE EC=2.4.1.13;
DE AltName: Full=Sucrose-UDP glucosyltransferase 3;
GN Name=SUS3; OrderedLocusNames=At4g02280; ORFNames=T2H3.8;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 GENE FAMILY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=14739263; DOI=10.1093/jxb/erh047;
RA Baud S., Vaultier M.N., Rochat C.;
RT "Structure and expression profile of the sucrose synthase multigene family
RT in Arabidopsis.";
RL J. Exp. Bot. 55:397-409(2004).
RN [5]
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=17257168; DOI=10.1111/j.1365-313x.2006.03011.x;
RA Bieniawska Z., Paul Barratt D.H., Garlick A.P., Thole V., Kruger N.J.,
RA Martin C., Zrenner R., Smith A.M.;
RT "Analysis of the sucrose synthase gene family in Arabidopsis.";
RL Plant J. 49:810-828(2007).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=18635527; DOI=10.1093/jxb/ern180;
RA Fallahi H., Scofield G.N., Badger M.R., Chow W.S., Furbank R.T., Ruan Y.L.;
RT "Localization of sucrose synthase in developing seed and siliques of
RT Arabidopsis thaliana reveals diverse roles for SUS during development.";
RL J. Exp. Bot. 59:3283-3295(2008).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20559653; DOI=10.1007/s00425-010-1207-9;
RA Angeles-Nunez J.G., Tiessen A.;
RT "Arabidopsis sucrose synthase 2 and 3 modulate metabolic homeostasis and
RT direct carbon towards starch synthesis in developing seeds.";
RL Planta 232:701-718(2010).
RN [8]
RP INDUCTION BY LEC2.
RX PubMed=22228409; DOI=10.1007/s11103-011-9871-0;
RA Angeles-Nunez J.G., Tiessen A.;
RT "Regulation of AtSUS2 and AtSUS3 by glucose and the transcription factor
RT LEC2 in different tissues and at different stages of Arabidopsis seed
RT development.";
RL Plant Mol. Biol. 78:377-392(2012).
RN [9]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22184213; DOI=10.1073/pnas.1117099109;
RA Baroja-Fernandez E., Munoz F.J., Li J., Bahaji A., Almagro G., Montero M.,
RA Etxeberria E., Hidalgo M., Sesma M.T., Pozueta-Romero J.;
RT "Sucrose synthase activity in the sus1/sus2/sus3/sus4 Arabidopsis mutant is
RT sufficient to support normal cellulose and starch production.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:321-326(2012).
CC -!- FUNCTION: Sucrose-cleaving enzyme that provides UDP-glucose and
CC fructose for various metabolic pathways. Modulates metabolic
CC homeostasis and direct carbon towards starch synthesis in developing
CC seeds. {ECO:0000269|PubMed:20559653}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an NDP-alpha-D-glucose + D-fructose = a ribonucleoside 5'-
CC diphosphate + H(+) + sucrose; Xref=Rhea:RHEA:16241,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17992, ChEBI:CHEBI:37721,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:76533; EC=2.4.1.13;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=41.96 mM for D-fructose (synthetic reaction) at pH 9.4
CC {ECO:0000269|PubMed:17257168};
CC KM=0.2 mM for UDP-glucose (synthetic reaction) at pH 9.4
CC {ECO:0000269|PubMed:17257168};
CC KM=108.2 mM for sucrose (degradative reaction) at pH 6
CC {ECO:0000269|PubMed:17257168};
CC KM=48 mM for sucrose (degradative reaction) at pH 7
CC {ECO:0000269|PubMed:22184213};
CC KM=0.09 mM for UDP (degradative reaction) at pH 6
CC {ECO:0000269|PubMed:17257168};
CC KM=0.25 mM for UDP (degradative reaction) at pH 7
CC {ECO:0000269|PubMed:22184213};
CC KM=0.15 mM for ADP (degradative reaction) at pH 7
CC {ECO:0000269|PubMed:22184213};
CC Vmax=7.32 umol/min/mg enzyme for synthetic reaction at pH 9.4
CC {ECO:0000269|PubMed:17257168};
CC Vmax=3.03 umol/min/mg enzyme for degradative reaction at pH 6
CC {ECO:0000269|PubMed:17257168};
CC Vmax=950 umol/min/mg enzyme for degradative reaction at pH 7
CC {ECO:0000269|PubMed:22184213};
CC pH dependence:
CC Optimum pH is 6.0-7.0 for degradative reaction (PubMed:22184213,
CC PubMed:17257168). Optimum pH is 7.0 for synthetic reaction
CC (PubMed:22184213). Optimum pH is 9.0-9.5 for synthetic reaction
CC (PubMed:17257168). {ECO:0000269|PubMed:17257168,
CC ECO:0000269|PubMed:22184213};
CC -!- TISSUE SPECIFICITY: Detected in the whole plant with highest expression
CC in developing siliques, vasculature of cotyledons and stomatal guard
CC cells. Also detected throughout the mature parts of the root but not in
CC the expanding zone. {ECO:0000269|PubMed:14739263,
CC ECO:0000269|PubMed:17257168, ECO:0000269|PubMed:18635527}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in late-maturing seeds and in
CC geminating seeds (at the protein level). {ECO:0000269|PubMed:14739263,
CC ECO:0000269|PubMed:17257168}.
CC -!- INDUCTION: By drought stress. By mannitol, an osmotic agent. Positively
CC regulated by LEC2. {ECO:0000269|PubMed:14739263,
CC ECO:0000269|PubMed:22228409}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Diminution of the starch
CC content of developing seeds and increased lipid accumulation early
CC during seed development. {ECO:0000269|PubMed:17257168,
CC ECO:0000269|PubMed:20559653}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. Plant sucrose
CC synthase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC28175.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF075597; AAC28175.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161494; CAB80721.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82150.1; -; Genomic_DNA.
DR EMBL; AY051001; AAK93678.1; -; mRNA.
DR EMBL; AY056784; AAL09730.1; -; mRNA.
DR EMBL; AY142511; AAN13112.1; -; mRNA.
DR PIR; B85029; B85029.
DR PIR; T01420; T01420.
DR RefSeq; NP_192137.1; NM_116461.4.
DR AlphaFoldDB; Q9M111; -.
DR SMR; Q9M111; -.
DR BioGRID; 13372; 1.
DR STRING; 3702.AT4G02280.1; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR iPTMnet; Q9M111; -.
DR PaxDb; Q9M111; -.
DR PRIDE; Q9M111; -.
DR ProteomicsDB; 228311; -.
DR EnsemblPlants; AT4G02280.1; AT4G02280.1; AT4G02280.
DR GeneID; 828081; -.
DR Gramene; AT4G02280.1; AT4G02280.1; AT4G02280.
DR KEGG; ath:AT4G02280; -.
DR Araport; AT4G02280; -.
DR TAIR; locus:2137829; AT4G02280.
DR eggNOG; KOG0853; Eukaryota.
DR HOGENOM; CLU_019158_1_0_1; -.
DR InParanoid; Q9M111; -.
DR OMA; WISRFEI; -.
DR OrthoDB; 170782at2759; -.
DR PhylomeDB; Q9M111; -.
DR BioCyc; MetaCyc:AT4G02280-MON; -.
DR BRENDA; 2.4.1.13; 399.
DR PRO; PR:Q9M111; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M111; baseline and differential.
DR Genevisible; Q9M111; AT.
DR GO; GO:0016157; F:sucrose synthase activity; IDA:UniProtKB.
DR GO; GO:0010555; P:response to mannitol; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR GO; GO:0010431; P:seed maturation; IMP:TAIR.
DR GO; GO:0005982; P:starch metabolic process; IMP:TAIR.
DR GO; GO:0005985; P:sucrose metabolic process; IMP:TAIR.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR000368; Sucrose_synth.
DR InterPro; IPR012820; Sucrose_synthase_pln/cyn.
DR PANTHER; PTHR45839; PTHR45839; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF00862; Sucrose_synth; 1.
DR TIGRFAMs; TIGR02470; sucr_synth; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Reference proteome; Stress response; Transferase.
FT CHAIN 1..809
FT /note="Sucrose synthase 3"
FT /id="PRO_0000418802"
FT REGION 277..755
FT /note="GT-B glycosyltransferase"
FT /evidence="ECO:0000250"
SQ SEQUENCE 809 AA; 92002 MW; BC5151F2FBF265D5 CRC64;
MANPKLTRVL STRDRVQDTL SAHRNELVAL LSRYVDQGKG ILQPHNLIDE LESVIGDDET
KKSLSDGPFG EILKSAMEAI VVPPFVALAV RPRPGVWEYV RVNVFELSVE QLTVSEYLRF
KEELVDGPNS DPFCLELDFE PFNANVPRPS RSSSIGNGVQ FLNRHLSSVM FRNKDCLEPL
LDFLRVHKYK GHPLMLNDRI QSISRLQIQL SKAEDHISKL SQETPFSEFE YALQGMGFEK
GWGDTAGRVL EMMHLLSDIL QAPDPSSLEK FLGMVPMVFN VVILSPHGYF GQANVLGLPD
TGGQVVYILD QVRALETEML LRIKRQGLDI SPSILIVTRL IPDAKGTTCN QRLERVSGTE
HTHILRVPFR SEKGILRKWI SRFDVWPYLE NYAQDAASEI VGELQGVPDF IIGNYSDGNL
VASLMAHRMG VTQCTIAHAL EKTKYPDSDI YWKDFDNKYH FSCQFTADLI AMNNADFIIT
STYQEIAGTK NTVGQYESHG AFTLPGLYRV VHGIDVFDPK FNIVSPGADM TIYFPYSEET
RRLTALHGSI EEMLYSPDQT DEHVGTLSDR SKPILFSMAR LDKVKNISGL VEMYSKNTKL
RELVNLVVIA GNIDVNKSKD REEIVEIEKM HNLMKNYKLD GQFRWITAQT NRARNGELYR
YIADTRGAFA QPAFYEAFGL TVVEAMTCGL PTFATCHGGP AEIIEHGLSG FHIDPYHPEQ
AGNIMADFFE RCKEDPNHWK KVSDAGLQRI YERYTWKIYS ERLMTLAGVY GFWKYVSKLE
RRETRRYLEM FYILKFRDLV KTVPSTADD
