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SPSA1_ORYSI
ID   SPSA1_ORYSI             Reviewed;        1084 AA.
AC   A2WYE9; Q43010; Q43802; Q5JLN3; Q94JN0;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Probable sucrose-phosphate synthase 1;
DE            EC=2.4.1.14;
DE   AltName: Full=UDP-glucose-fructose-phosphate glucosyltransferase;
GN   Name=SPS1; ORFNames=OsI_004842;
OS   Oryza sativa subsp. indica (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=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. IR36; TISSUE=Leaf;
RX   PubMed=8666248; DOI=10.1016/0378-1119(95)00854-3;
RA   Valdez-Alarcon J.J., Ferrando M., Jimenez-Moraila B., Herrera-Estrella L.;
RT   "Characterization of a rice sucrose-phosphate synthase-encoding gene.";
RL   Gene 170:217-222(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=11027714; DOI=10.1104/pp.124.2.641;
RA   Chavez-Barcenas A.T., Valdez-Alarcon J.J., Martinez-Trujillo M., Chen L.,
RA   Xoconostle-Cazares B., Lucas W.J., Herrera-Estrella L.;
RT   "Tissue-specific and developmental pattern of expression of the rice sps1
RT   gene.";
RL   Plant Physiol. 124:641-654(2000).
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 leaves mesophyll cells, scutellum of
CC       germinating seedlings and pollen of immature inflorescences.
CC       {ECO:0000269|PubMed:11027714, ECO:0000269|PubMed:8666248}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC49379.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAC49379.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR   EMBL; U33175; AAC49379.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CM000126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; JC4783; JC4783.
DR   AlphaFoldDB; A2WYE9; -.
DR   SMR; A2WYE9; -.
DR   STRING; 39946.A2WYE9; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   iPTMnet; A2WYE9; -.
DR   PRIDE; A2WYE9; -.
DR   BioCyc; MetaCyc:MON-1762; -.
DR   BRENDA; 2.4.1.14; 4460.
DR   UniPathway; UPA00371; UER00545.
DR   Proteomes; UP000007015; Chromosome 1.
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; 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; Reference proteome; Transferase.
FT   CHAIN           1..1084
FT                   /note="Probable sucrose-phosphate synthase 1"
FT                   /id="PRO_0000303664"
FT   REGION          25..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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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