SPSA2_ARATH
ID SPSA2_ARATH Reviewed; 1047 AA.
AC Q9FY54; Q8VYW8;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Probable sucrose-phosphate synthase 2;
DE EC=2.4.1.14;
DE AltName: Full=Protein KAONASHI 2;
DE AltName: Full=Sucrose-phosphate synthase 2F;
DE Short=AtSPS2F;
DE AltName: Full=Sucrose-phosphate synthase 5.2;
DE Short=AtSPS5.2;
DE AltName: Full=UDP-glucose-fructose-phosphate glucosyltransferase;
GN Name=SPS2; Synonyms=KNS2, SPS1, SPSA2; OrderedLocusNames=At5g11110;
GN ORFNames=T5K6.100;
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] OF 149-1047 AND 154-1047.
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.
RX PubMed=16876912; DOI=10.1016/j.jplph.2006.04.014;
RA Lutfiyya L.L., Xu N., D'Ordine R.L., Morrell J.A., Miller P.W., Duff S.M.;
RT "Phylogenetic and expression analysis of sucrose phosphate synthase
RT isozymes in plants.";
RL J. Plant Physiol. 164:923-933(2007).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF PRO-596.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=18779216; DOI=10.1093/pcp/pcn131;
RA Suzuki T., Masaoka K., Nishi M., Nakamura K., Ishiguro S.;
RT "Identification of kaonashi mutants showing abnormal pollen exine structure
RT in Arabidopsis thaliana.";
RL Plant Cell Physiol. 49:1465-1477(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=24670640; DOI=10.1038/nature13082;
RA Lin I.W., Sosso D., Chen L.-Q., Gase K., Kim S.-G., Kessler D.,
RA Klinkenberg P.M., Gorder M.K., Hou B.-H., Qu X.-Q., Carter C.J.,
RA Baldwin I.T., Frommer W.B.;
RT "Nectar secretion requires sucrose phosphate synthases and the sugar
RT transporter SWEET9.";
RL Nature 508:546-549(2014).
CC -!- FUNCTION: Plays a role in photosynthetic sucrose synthesis by
CC catalyzing the rate-limiting step of sucrose biosynthesis from UDP-
CC glucose and fructose- 6-phosphate. Involved in the regulation of carbon
CC partitioning in the leaves of plants. May regulate the synthesis of
CC sucrose and therefore play a major role as a limiting factor in the
CC export of photoassimilates out of the leaf. Plays a role for sucrose
CC availability that is essential for plant growth and fiber elongation.
CC Required for nectar secretion. {ECO:0000269|PubMed:18779216,
CC ECO:0000269|PubMed:24670640}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 6-phosphate + UDP-alpha-D-glucose = H(+) +
CC sucrose 6(F)-phosphate + UDP; Xref=Rhea:RHEA:22172,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57634, ChEBI:CHEBI:57723,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.14;
CC -!- ACTIVITY REGULATION: Activity is regulated by phosphorylation and
CC moderated by concentration of metabolites and light. {ECO:0000250}.
CC -!- PATHWAY: Glycan biosynthesis; sucrose biosynthesis; sucrose from D-
CC fructose 6-phosphate and UDP-alpha-D-glucose: step 1/2.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cauline leaves, flower buds,
CC flowers and anthers. Highly expressed in maturing nectaries.
CC {ECO:0000269|PubMed:18779216, ECO:0000269|PubMed:24670640}.
CC -!- DISRUPTION PHENOTYPE: Loss of nectar secretion accompanied by starch
CC accumulation in nectaries. {ECO:0000269|PubMed:24670640}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL47425.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL391222; CAC03459.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91636.1; -; Genomic_DNA.
DR EMBL; AY069868; AAL47425.1; ALT_INIT; mRNA.
DR EMBL; BT002697; AAO11613.1; -; mRNA.
DR PIR; T51800; T51800.
DR RefSeq; NP_196672.3; NM_121149.4.
DR AlphaFoldDB; Q9FY54; -.
DR SMR; Q9FY54; -.
DR STRING; 3702.AT5G11110.1; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR iPTMnet; Q9FY54; -.
DR SwissPalm; Q9FY54; -.
DR PaxDb; Q9FY54; -.
DR PRIDE; Q9FY54; -.
DR ProteomicsDB; 232574; -.
DR EnsemblPlants; AT5G11110.1; AT5G11110.1; AT5G11110.
DR GeneID; 830979; -.
DR Gramene; AT5G11110.1; AT5G11110.1; AT5G11110.
DR KEGG; ath:AT5G11110; -.
DR Araport; AT5G11110; -.
DR TAIR; locus:2184891; AT5G11110.
DR eggNOG; KOG0853; Eukaryota.
DR HOGENOM; CLU_009583_24_0_1; -.
DR InParanoid; Q9FY54; -.
DR OMA; GEMPGVY; -.
DR OrthoDB; 101620at2759; -.
DR PhylomeDB; Q9FY54; -.
DR BRENDA; 2.4.1.14; 399.
DR UniPathway; UPA00371; UER00545.
DR PRO; PR:Q9FY54; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FY54; baseline and differential.
DR Genevisible; Q9FY54; AT.
DR GO; GO:0016157; F:sucrose synthase activity; IEA:InterPro.
DR GO; GO:0046524; F:sucrose-phosphate synthase activity; IDA:TAIR.
DR GO; GO:0071836; P:nectar secretion; IMP:UniProtKB.
DR GO; GO:0010208; P:pollen wall assembly; IMP:UniProtKB.
DR GO; GO:0005986; P:sucrose biosynthetic process; IGI:TAIR.
DR CDD; cd16419; HAD_SPS; 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006380; SPP_N.
DR InterPro; IPR044161; SPS.
DR InterPro; IPR035659; SPS_C.
DR InterPro; IPR012819; SPS_pln.
DR InterPro; IPR000368; Sucrose_synth.
DR PANTHER; PTHR46039; PTHR46039; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF05116; S6PP; 1.
DR Pfam; PF00862; Sucrose_synth; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02468; sucrsPsyn_pln; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..1047
FT /note="Probable sucrose-phosphate synthase 2"
FT /id="PRO_0000413638"
FT REGION 101..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94BT0"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94BT0"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94BT0"
FT MUTAGEN 596
FT /note="P->L: In kns2-1; pollen grain with collapsed exine
FT structure."
FT /evidence="ECO:0000269|PubMed:18779216"
SQ SEQUENCE 1047 AA; 116966 MW; 0BA67F6E8DD9FA80 CRC64;
MVGNDWVNSY LEAILAAEPG IANSKPPGTG DSKSSLLLRE RGHFSPTRYF VEEVITGFDE
TDLHRSWVQA AATRSPQERN TRLENLCWRI WNLARQKKQV EGKNAKREAK REREREKARR
EVTAEMSEDF SEGEKADLPG EIPTPSDNNT KGRMSRISSV DVFENWFAQH KEKKLYIVLI
SLHGLIRGEN MELGRDSDTG GQVKYVVELA RALGSMPGVY RVDLLTRQVT APDVDSSYSE
PSEMLNPIDT DIEQENGESS GAYIIRIPFG PKDKYVPKEL LWPHIPEFVD RALSHIMQIS
KVLGEQIGGG QQVWPVSIHG HYADAGDSTA LLSGALNVPM VFTGHSLGRD KLEQLLKQGR
PKEEINSNYK IWRRIEAEEL CLDASEIVIT STRQEVDEQW RLYDGFDPVL ERKLRARMKR
GVSCLGRFMP RMVVIPPGME FHHIVPHDVD ADGDDENPQT ADPPIWSEIM RFFSNPRKPM
ILALARPDPK KNLVTLVKAF GECRPLRELA NLTLIMGNRN DIDELSSTNS SVLLSILKLI
DKYDLYGQVA MPKHHQQSDV PEIYRLAAKT KGVFINPAFI EPFGLTLIEA GAHGLPTVAT
INGGPVDIHR VLDNGLLVDP HDQQAIADAL LKLVSDRQLW GRCRQNGLNN IHLFSWPEHC
KTYLARIASC KQRHPKWQRV EFENSDSDSP SDSLRDINDI SLNLKLSLDG EKSGSNNGVD
TNLDAEDRAA ERKAEVEKAV STLAQKSKPT EKFDSKMPTL KRRKNIFVIS VDCSATSDLL
AVVKTVIDAA GRGSSTGFIL STSMTISETH TALLSGGLKP QDFDAVICSS GSELYFTSSG
SEDKTALPYT LDADYHSHIE FRWGGESLRK TLIRWISSVE EKKKTKKGEI LVEDESSSTN
YCLSFKVKDP ALMPPMKELR KLMRNQALRC NAVYCQNGAR LNVIPVLASR SQALRYLLVR
WGIDLSNMVV FVGDSGDTDY EGLLGGIHKT VILKGLASDL REQPGNRSYP MEDVTPLNSP
NITEAKECGR DAIKVALEKL GISLLKP
