SPSA3_ARATH
ID SPSA3_ARATH Reviewed; 1062 AA.
AC Q8RY24; Q9MAU0;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Probable sucrose-phosphate synthase 3;
DE EC=2.4.1.14;
DE AltName: Full=Sucrose phosphate synthase 3F;
DE Short=AtSPS3F;
DE AltName: Full=UDP-glucose-fructose-phosphate glucosyltransferase;
GN Name=SPS3; Synonyms=SPSB; OrderedLocusNames=At1g04920; ORFNames=F13M7.9;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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).
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 -!- 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 -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF40445.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004809; AAF40445.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27759.1; -; Genomic_DNA.
DR EMBL; AY078949; AAL84949.1; -; mRNA.
DR EMBL; BT002210; AAN72222.1; -; mRNA.
DR PIR; F86182; F86182.
DR RefSeq; NP_171984.2; NM_100370.3.
DR AlphaFoldDB; Q8RY24; -.
DR SMR; Q8RY24; -.
DR STRING; 3702.AT1G04920.1; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR iPTMnet; Q8RY24; -.
DR PaxDb; Q8RY24; -.
DR PRIDE; Q8RY24; -.
DR ProteomicsDB; 232488; -.
DR EnsemblPlants; AT1G04920.1; AT1G04920.1; AT1G04920.
DR GeneID; 839382; -.
DR Gramene; AT1G04920.1; AT1G04920.1; AT1G04920.
DR KEGG; ath:AT1G04920; -.
DR Araport; AT1G04920; -.
DR TAIR; locus:2010647; AT1G04920.
DR eggNOG; KOG0853; Eukaryota.
DR HOGENOM; CLU_009583_24_0_1; -.
DR InParanoid; Q8RY24; -.
DR OMA; TRMQIVP; -.
DR OrthoDB; 101620at2759; -.
DR PhylomeDB; Q8RY24; -.
DR BRENDA; 2.4.1.14; 399.
DR UniPathway; UPA00371; UER00545.
DR PRO; PR:Q8RY24; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RY24; baseline and differential.
DR Genevisible; Q8RY24; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0016157; F:sucrose synthase activity; IEA:InterPro.
DR GO; GO:0046524; F:sucrose-phosphate synthase activity; IDA:TAIR.
DR GO; GO:0005986; P:sucrose biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16419; HAD_SPS; 1.
DR InterPro; IPR001296; Glyco_trans_1.
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 TIGRFAMs; TIGR02468; sucrsPsyn_pln; 1.
PE 2: Evidence at transcript level;
KW Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..1062
FT /note="Probable sucrose-phosphate synthase 3"
FT /id="PRO_0000413639"
FT REGION 113..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94BT0"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F4JLK2"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F4JLK2"
SQ SEQUENCE 1062 AA; 119476 MW; E5AE17241C6892CA CRC64;
MAGNEWINGY LEAILDSQAQ GIEETQQKPQ ASVNLREGDG QYFNPTKYFV EEVVTGVDET
DLHRTWLKVV ATRNSRERNS RLENMCWRIW HLTRKKKQLE WEDSQRIANR RLEREQGRRD
ATEDLSEDLS EGEKGDGLGE IVQPETPRRQ LQRNLSNLEI WSDDKKENRL YVVLISLHGL
VRGENMELGS DSDTGGQVKY VVELARALAR MPGVYRVDLF TRQICSSEVD WSYAEPTEML
TTAEDCDGDE TGESSGAYII RIPFGPRDKY LNKEILWPFV QEFVDGALAH ILNMSKVLGE
QIGKGKPVWP YVIHGHYADA GDSAALLSGA LNVPMVLTGH SLGRNKLEQL LKQGRQSKED
INSTYKIKRR IEAEELSLDA AELVITSTRQ EIDEQWGLYD GFDVKLEKVL RARARRGVNC
HGRFMPRMAV IPPGMDFTNV EVQEDTPEGD GDLASLVGGT EGSSPKAVPT IWSEVMRFFT
NPHKPMILAL SRPDPKKNIT TLLKAFGECR PLRELANLTL IMGNRDDIDE LSSGNASVLT
TVLKLIDKYD LYGSVAYPKH HKQSDVPDIY RLAANTKGVF INPALVEPFG LTLIEAAAHG
LPMVATKNGG PVDIHRALHN GLLVDPHDQE AIANALLKLV SEKNLWHECR INGWKNIHLF
SWPEHCRTYL TRIAACRMRH PQWQTDADEV AAQDDEFSLN DSLKDVQDMS LRLSMDGDKP
SLNGSLEPNS ADPVKQIMSR MRTPEIKSKP ELQGKKQSDN LGSKYPVLRR RERLVVLAVD
CYDNEGAPDE KAMVPMIQNI IKAVRSDPQM AKNSGFAIST SMPLDELTRF LKSAKIQVSE
FDTLICSSGS EVYYPGGEEG KLLPDPDYSS HIDYRWGMEG LKNTVWKLMN TTAVGGEARN
KGSPSLIQED QASSNSHCVA YMIKDRSKVM RVDDLRQKLR LRGLRCHPMY CRNSTRMQIV
PLLASRSQAL RYLFVRWRLN VANMYVVVGD RGDTDYEELI SGTHKTVIVK GLVTLGSDAL
LRSTDLRDDI VPSESPFIGF LKVDSPVKEI TDIFKQLSKA TA
