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Database: UniProt
Entry: SPSA1_ORYSJ
LinkDB: SPSA1_ORYSJ
Original site: SPSA1_ORYSJ 
ID   SPSA1_ORYSJ             Reviewed;        1084 AA.
AC   Q0JGK4; Q43010; Q43802; Q5JLN3; Q94JN0;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   24-JAN-2024, entry version 94.
DE   RecName: Full=Probable sucrose-phosphate synthase 1;
DE            EC=2.4.1.14;
DE   AltName: Full=Sucrose phosphate synthase 1F;
DE            Short=OsSPS1F;
DE   AltName: Full=UDP-glucose-fructose-phosphate glucosyltransferase;
GN   Name=SPS1; OrderedLocusNames=Os01g0919400, LOC_Os01g69030;
GN   ORFNames=P0678F11.16;
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 [GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RA   Sakamoto M., Satozawa T., Kishimoto N., Higo K., Shimada H., Fujimura T.;
RT   "Structure and RFLP mapping of a rice sucrose phosphate synthase (SPS) gene
RT   that is specifically expressed in the source organ.";
RL   Plant Sci. 112:207-217(1995).
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 [MRNA] OF 102-199.
RC   STRAIN=cv. Stejaree45;
RA   Lee D.-S., Hur Y.;
RT   "Expression and regulation of genes involved in carbohydrate metabolism in
RT   rice.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [7]
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   [8]
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=21683881; DOI=10.1016/j.plantsci.2011.04.019;
RA   Okamura M., Aoki N., Hirose T., Yonekura M., Ohto C., Ohsugi R.;
RT   "Tissue specificity and diurnal change in gene expression of the sucrose
RT   phosphate synthase gene family in rice.";
RL   Plant Sci. 181:159-166(2011).
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       (By similarity). {ECO:0000250}.
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 germinating seeds.
CC       {ECO:0000269|PubMed:21683881}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in source leaves and at low
CC       levels in sink leaves. {ECO:0000269|PubMed:21683881}.
CC   -!- INDUCTION: Circadian-regulated, with the highest expression 1 hour
CC       before the beginning of light period (in 14 hours light/10 hours dark
CC       cycle). {ECO:0000269|PubMed:21683881}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF07124.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; D45890; BAA08304.1; -; Genomic_DNA.
DR   EMBL; AP003437; BAD87626.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF07124.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF378184; AAK54855.1; -; mRNA.
DR   PIR; T04103; T04103.
DR   RefSeq; XP_015621705.1; XM_015766219.1.
DR   RefSeq; XP_015621706.1; XM_015766220.1.
DR   AlphaFoldDB; Q0JGK4; -.
DR   SMR; Q0JGK4; -.
DR   STRING; 39947.Q0JGK4; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   PaxDb; 39947-Q0JGK4; -.
DR   EnsemblPlants; Os01t0919400-01; Os01t0919400-01; Os01g0919400.
DR   GeneID; 4324364; -.
DR   Gramene; Os01t0919400-01; Os01t0919400-01; Os01g0919400.
DR   KEGG; osa:4324364; -.
DR   eggNOG; KOG0853; Eukaryota.
DR   InParanoid; Q0JGK4; -.
DR   OrthoDB; 1206157at2759; -.
DR   BRENDA; 2.4.1.14; 8948.
DR   PlantReactome; R-OSA-1119465; Sucrose biosynthesis.
DR   UniPathway; UPA00371; UER00545.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:EnsemblPlants.
DR   GO; GO:0016157; F:sucrose synthase activity; IEA:InterPro.
DR   GO; GO:0046524; F:sucrose-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005986; P:sucrose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03800; GT4_sucrose_synthase; 1.
DR   CDD; cd16419; HAD_SPS; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR006380; SPP-like_dom.
DR   InterPro; IPR035659; SPS_C.
DR   InterPro; IPR012819; SPS_pln.
DR   InterPro; IPR000368; Sucrose_synth.
DR   NCBIfam; TIGR02468; sucrsPsyn_pln; 1.
DR   PANTHER; PTHR46039; SUCROSE-PHOSPHATE SYNTHASE 3-RELATED; 1.
DR   PANTHER; PTHR46039:SF5; SUCROSE-PHOSPHATE SYNTHASE 3-RELATED; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   Pfam; PF05116; S6PP; 1.
DR   Pfam; PF00862; Sucrose_synth; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   2: Evidence at transcript level;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..1084
FT                   /note="Probable sucrose-phosphate synthase 1"
FT                   /id="PRO_0000204672"
FT   REGION          25..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        49
FT                   /note="R -> S (in Ref. 1; BAA08304)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52..56
FT                   /note="AAGAA -> TTGTT (in Ref. 1; BAA08304)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        384
FT                   /note="I -> M (in Ref. 1; BAA08304)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        494
FT                   /note="M -> S (in Ref. 1; BAA08304)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        497
FT                   /note="L -> W (in Ref. 1; BAA08304)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        539
FT                   /note="I -> S (in Ref. 1; BAA08304)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        542
FT                   /note="N -> T (in Ref. 1; BAA08304)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        548
FT                   /note="E -> G (in Ref. 1; BAA08304)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        578
FT                   /note="H -> Y (in Ref. 1; BAA08304)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        623
FT                   /note="A -> G (in Ref. 1; BAA08304)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        767
FT                   /note="D -> E (in Ref. 1; BAA08304)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        950
FT                   /note="I -> M (in Ref. 1; BAA08304)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1084 AA;  119348 MW;  A42BA599C4DF4556 CRC64;
     MAGNEWINGY LEAILDSGGA AGGGGGGGGG GGGGGGGGGG GGGGGVDPRS PAAGAASPRG
     PHMNFNPTHY FVEEVVKGVD ESDLHRTWIK VVATRNARER STRLENMCWR IWHLARKKKQ
     LELEGILRIS ARRKEQEQVR RETSEDLAED LFEGEKADTV GELAQQDTPM KKKFQRNFSE
     LTVSWSDENK EKKLYIVLIS LHGLVRGDNM ELGRDSDTGG QVKYVVELAR ALAMMPGVYR
     VDLFTRQVSS PEVDWSYGEP TEMLTSGSTD GEGSGESAGA YIVRIPCGPR DKYLRKEALW
     PYLQEFVDGA LAHILNMSKA LGEQVSNGKL VLPYVIHGHY ADAGDVAALL SGALNVPMVL
     TGHSLGRNKL EQIMKQGRMS KEEIDSTYKI MRRIEGEELA LDAAELVITS TRQEIDEQWG
     LYDGFDVKLE KVLRARARRG VSCHGRFMPR MVVIPPGMDF SSVVVPEDTS DGDDGKDFEI
     ASPRSLPPIW AEVMRFLTNP HKPMILALSR PDPKKNITTL VKAFGECRPL RELANLILIM
     GNRDDIDEMS AGNASVLTTV LKLIDKYDLY GSVAFPKHHK QSDVPEIYRL TGKMKGVFIN
     PALVEPFGLT LIEAAAHGLP IVATKNGGPV DIKNALNNGL LVDPHDQHAI ADALLKLVAD
     KNLWQECRKN GLRNIQLYSW PEHCRTYLTR IAGCRIRNPR WLMDTPADAA AEEEEALEDS
     LMDVQDLSLR LSIDGERGSS MNDAPSSDPQ DSVQRIMNKI KRSSPADTDG AKIPAEAAAT
     ATSGAMNKYP LLRRRRRLFV IAVDCYGDDG SASKRMLQVI QEVFRAVRSD SQMSRISGFA
     LSTAMPLPET LKLLQLGKIP PTDFDALICG SGSEVYYPST AQCVDAGGRL RPDQDYLLHI
     NHRWSHDGAK QTIAKLAHDG SGTNVEPDVE SCNPHCVSFF IKDPNKVRTI DEMRERVRMR
     GLRCHLMYCR NATRLQVVPL LASRSQALRY LFVRWGLSVG NMYLIVGEHG DTDHEEMLSG
     LHKTVIIRGV TEKGSEQLVR SSGSYQREDV VPSESPLIAF TKGDLKADEI MRALKEVTKA
     ASGM
//
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