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SPSA4_ORYSJ
ID   SPSA4_ORYSJ             Reviewed;        1066 AA.
AC   Q6ZHZ1; A0A0P0XEF8; Q6UU32;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Probable sucrose-phosphate synthase 4;
DE            EC=2.4.1.14;
DE   AltName: Full=Sucrose phosphate synthase 4F;
DE            Short=OsSPS4F;
DE   AltName: Full=UDP-glucose-fructose-phosphate glucosyltransferase;
GN   Name=SPS4; Synonyms=SPS8; OrderedLocusNames=Os08g0301500, LOC_Os08g20660;
GN   ORFNames=OJ1115_A07.105;
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].
RX   PubMed=14716315; DOI=10.1038/ng1289;
RA   Nagaki K., Cheng Z., Ouyang S., Talbert P.B., Kim M., Jones K.M.,
RA   Henikoff S., Buell C.R., Jiang J.;
RT   "Sequencing of a rice centromere uncovers active genes.";
RL   Nat. Genet. 36:138-145(2004).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [6]
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   [7]
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: Expressed in source leaves and sink leaves.
CC       {ECO:0000269|PubMed:21683881}.
CC   -!- INDUCTION: Circadian-regulated, with the highest expression 1 hour
CC       after the beginning of dark 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=AAQ56529.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY360393; AAQ56529.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP004041; BAC92378.1; -; Genomic_DNA.
DR   EMBL; AP008214; BAF23409.1; -; Genomic_DNA.
DR   EMBL; AP014964; BAT04814.1; -; Genomic_DNA.
DR   EMBL; AK101676; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015650062.1; XM_015794576.1.
DR   RefSeq; XP_015650063.1; XM_015794577.1.
DR   AlphaFoldDB; Q6ZHZ1; -.
DR   SMR; Q6ZHZ1; -.
DR   STRING; 4530.OS08T0301500-01; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   iPTMnet; Q6ZHZ1; -.
DR   PaxDb; Q6ZHZ1; -.
DR   PRIDE; Q6ZHZ1; -.
DR   EnsemblPlants; Os08t0301500-01; Os08t0301500-01; Os08g0301500.
DR   GeneID; 4345220; -.
DR   Gramene; Os08t0301500-01; Os08t0301500-01; Os08g0301500.
DR   KEGG; osa:4345220; -.
DR   eggNOG; KOG0853; Eukaryota.
DR   HOGENOM; CLU_009583_24_0_1; -.
DR   InParanoid; Q6ZHZ1; -.
DR   OMA; AWSKGIS; -.
DR   OrthoDB; 101620at2759; -.
DR   BRENDA; 2.4.1.14; 8948.
DR   PlantReactome; R-OSA-1119465; Sucrose biosynthesis.
DR   UniPathway; UPA00371; UER00545.
DR   Proteomes; UP000000763; Chromosome 8.
DR   Proteomes; UP000059680; Chromosome 8.
DR   Genevisible; Q6ZHZ1; OS.
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..1066
FT                   /note="Probable sucrose-phosphate synthase 4"
FT                   /id="PRO_0000413643"
FT   REGION          132..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          688..714
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..165
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..714
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        527
FT                   /note="N -> S (in Ref. 5; AK101676)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        615
FT                   /note="A -> T (in Ref. 5; AK101676)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        900
FT                   /note="E -> G (in Ref. 5; AK101676)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1066 AA;  118725 MW;  AB4AE780FEA070A2 CRC64;
     MAGNDWINSY LEAILDAGGA AGEISAAAGG GGDGAAATGE KRDKSSLMLR ERGRFSPARY
     FVEEVISGFD ETDLYKTWVR TAAMRSPQER NTRLENMSWR IWNLARKKKQ IEGEEASRLA
     KQRLEREKAR RYAAADMSED LSEGEKGENI NESSSTHDES TRGRMPRIGS TDAIEAWASQ
     HKDKKLYIVL ISIHGLIRGE NMELGRDSDT GGQVKYVVEL ARALGSTPGV YRVDLLTRQI
     SAPDVDWSYG EPTEMLSPRN SENFGHDMGE SSGAYIVRIP FGPRDKYIPK EHLWPHIQEF
     VDGALVHIMQ MSKVLGEQVG SGQLVWPVVI HGHYADAGDS AALLSGALNV PMIFTGHSLG
     RDKLEQLLKQ GRQTRDEINT IYKIMRRIEA EELCLDASEI IITSTRQEIE QQWGLYDGFD
     LTMARKLRAR IKRGVSCYGR YMPRMIAVPP GMEFSHIVPH DVDQDGEEAN EDGSGSTDPP
     IWADIMRFFS NPRKPMILAL ARPDPKKNIT TLVKAFGEHR ELRNLANLTL IMGNRDVIDE
     MSSTNSAVLT SILKLIDKYD LYGQVAYPKH HKQSEVPDIY RLAARTKGVF INCAFIEPFG
     LTLIEAAAYG LPMVATRNGG PVDIHRVLDN GILVDPHNQN EIAEALYKLV SDKQLWAQCR
     QNGLKNIHQF SWPEHCKNYL SRVGTLKPRH PRWQKSDDAT EVSEADSPGD SLRDVHDISL
     NLKLSLDSEK SSTKENSVRR NLEDAVQKLS RGVSANRKTE SVENMEATTG NKWPSLRRRK
     HIVVIAIDSV QDANLVEIIK NIFVASSNER LSGSVGFVLS TSRAISEVHS LLTSGGIEAT
     DFDAFICNSG SDLCYPSSNS EDMLSPAELP FMIDLDYHTQ IEYRWGGEGL RKTLICWAAE
     KSEGGQVVLV EDEECSSTYC ISFRVKNAEA VPPVKELRKT MRIQALRCHV LYSHDGSKLN
     VIPVLASRSQ ALRYLYIRWG VELSNMTVVV GESGDTDYEG LLGGVHKTII LKGSFNAVPN
     QVHAARSYSL QDVISFDKPG ITSIEGYGPD NLKSALQQFG ILKDNV
 
 
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