SPSA5_ORYSJ
ID SPSA5_ORYSJ Reviewed; 1014 AA.
AC Q53JI9; Q0ITN3; Q53NB0;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Probable sucrose-phosphate synthase 5;
DE EC=2.4.1.14;
DE AltName: Full=Sucrose phosphate synthase 5F;
DE Short=OsSPS5F;
DE AltName: Full=UDP-glucose-fructose-phosphate glucosyltransferase;
GN Name=SPS5; Synonyms=SPS11; OrderedLocusNames=Os11g0236100, LOC_Os11g12810;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
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 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 [6]
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=BAF27932.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC135258; AAX96649.1; -; Genomic_DNA.
DR EMBL; AC147811; AAX95196.1; -; Genomic_DNA.
DR EMBL; DP000010; ABA92286.1; -; Genomic_DNA.
DR EMBL; AP008217; BAF27932.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015617675.1; XM_015762189.1.
DR AlphaFoldDB; Q53JI9; -.
DR SMR; Q53JI9; -.
DR STRING; 4530.OS11T0236100-01; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR iPTMnet; Q53JI9; -.
DR PaxDb; Q53JI9; -.
DR PRIDE; Q53JI9; -.
DR GeneID; 4350151; -.
DR KEGG; osa:4350151; -.
DR eggNOG; KOG0853; Eukaryota.
DR HOGENOM; CLU_009583_24_1_1; -.
DR InParanoid; Q53JI9; -.
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 11.
DR Proteomes; UP000059680; Chromosome 11.
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 Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006380; SPP_N.
DR InterPro; IPR044161; SPS.
DR InterPro; IPR035659; SPS_C.
DR InterPro; IPR012819; SPS_pln.
DR PANTHER; PTHR46039; PTHR46039; 1.
DR Pfam; PF13579; Glyco_trans_4_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF05116; S6PP; 1.
DR TIGRFAMs; TIGR02468; sucrsPsyn_pln; 1.
PE 2: Evidence at transcript level;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..1014
FT /note="Probable sucrose-phosphate synthase 5"
FT /id="PRO_0000413644"
FT REGION 29..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1014 AA; 108985 MW; 6AF4C8059E23B842 CRC64;
MVHHYSMSCP DLEAIEQVEW EFSRQLSRRR LEQELGSREA AADLSELSEG EKDGKPDTHP
PPAAAAAEAA ADDGGGGDHQ QQQQQPPPHQ LSRFARINSD PRIVSDEEEE VTTDRNLYIV
LISIHGLVRG ENMELGRDSD TGGQVKYVVE LARALAATPG VHRVDLLTRQ ISCPDVDWTY
GEPVEMLTVP AADADDEDGG GGSSGGAYIV RLPCGPRDKY LPKESLWPHI PEFVDRALAH
VTNVARALGE QLSPPPPSDG AGAAAQAVWP YVIHGHYADA AEVAALLASA LNVPMVMTGH
SLGRNKLEQL LKLGRMPRAE IQGTYKIARR IEAEETGLDA ADMVVTSTKQ EIEEQWGLYD
GFDLKVERKL RVRRRRGVSC LGRYMPRMVV IPPGMDFSYV DTQDLAADGA GGAGDAADLQ
LLINPNKAKK PLPPIWSEVL RFFTNPHKPM ILALSRPDPK KNVTTLLKAY GESRHLRELA
NLTLILGNRD DIEEMSGGAA TVLTAVLKLI DRYDLYGQVA YPKHHKQTDV PHIYRLAAKT
KGVFINPALV EPFGLTIIEA AAYGLPVVAT KNGGPVDILK VLSNGLLVDP HDAAAITAAL
LSLLADKSRW SECRRSGLRN IHRFSWPHHC RLYLSHVAAS CDHPAPHQLL RVPPSPSSSS
AAAAAAGGGG AAASSEPLSD SLRDLSLRIS VDAASPDLSA GDSAAAILDA LRRRRSTDRP
AASSAARAIG FAPGRRQSLL VVAIDCYGDD GKPNVEQLKK VVELAMSAGD GDDAGGRGYV
LSTGMTIPEA VDALRACGAD PAGFDALICS SGAEICYPWK GEQLAADEEY AGHVAFRWPG
DHVRSAVPRL GKADGAQEAD LAVDAAACSV HCHAYAAKDA SKVKKVDWIR QALRMRGFRC
NLVYTRACTR LNVVPLSASR PRALRYLSIQ WGIDLSKVAV LVGEKGDTDR ERLLPGLHRT
VILPGMVAAG SEELLRDEDG FTTEDVVAMD SPNIVTLADG QDIAAAAADL LKAI
