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Database: UniProt
Entry: A0A0D3FTE2_9ORYZ
LinkDB: A0A0D3FTE2_9ORYZ
Original site: A0A0D3FTE2_9ORYZ 
ID   A0A0D3FTE2_9ORYZ        Unreviewed;       850 AA.
AC   A0A0D3FTE2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Sucrose synthase {ECO:0000256|ARBA:ARBA00012540, ECO:0000256|RuleBase:RU280817};
DE            EC=2.4.1.13 {ECO:0000256|ARBA:ARBA00012540, ECO:0000256|RuleBase:RU280817};
OS   Oryza barthii.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART04G05240.2};
RN   [1] {ECO:0000313|EnsemblPlants:OBART04G05240.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART04G05240.2};
RX   DOI=10.1007/s12284-009-9025-z;
RA   Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA   Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA   Knight J., Niazi F., Egholm M., Wing R.A.;
RT   "De novo next generation sequencing of plant genomes.";
RL   Rice 2:35-43(2009).
RN   [2] {ECO:0000313|EnsemblPlants:OBART04G05240.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
CC   -!- FUNCTION: Sucrose-cleaving enzyme that provides UDP-glucose and
CC       fructose for various metabolic pathways.
CC       {ECO:0000256|RuleBase:RU280817}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an NDP-alpha-D-glucose + D-fructose = a ribonucleoside 5'-
CC         diphosphate + H(+) + sucrose; Xref=Rhea:RHEA:16241,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17992, ChEBI:CHEBI:37721,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:76533; EC=2.4.1.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00000332,
CC         ECO:0000256|RuleBase:RU280817};
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. Plant sucrose
CC       synthase subfamily. {ECO:0000256|ARBA:ARBA00005894,
CC       ECO:0000256|RuleBase:RU280817}.
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DR   AlphaFoldDB; A0A0D3FTE2; -.
DR   STRING; 65489.A0A0D3FTE2; -.
DR   PaxDb; 65489-OBART04G05240-2; -.
DR   EnsemblPlants; OBART04G05240.2; OBART04G05240.2; OBART04G05240.
DR   Gramene; OBART04G05240.2; OBART04G05240.2; OBART04G05240.
DR   eggNOG; KOG0853; Eukaryota.
DR   Proteomes; UP000026960; Chromosome 4.
DR   GO; GO:0016157; F:sucrose synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005985; P:sucrose metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.120.1230; -; 1.
DR   Gene3D; 3.10.450.330; -; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR000368; Sucrose_synth.
DR   InterPro; IPR012820; Sucrose_synthase_pln/cyn.
DR   NCBIfam; TIGR02470; sucr_synth; 1.
DR   PANTHER; PTHR45839; -; 1.
DR   PANTHER; PTHR45839:SF4; SUCROSE SYNTHASE 5; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   Pfam; PF00862; Sucrose_synth; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU280817};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU280817}.
FT   DOMAIN          9..558
FT                   /note="Sucrose synthase"
FT                   /evidence="ECO:0000259|Pfam:PF00862"
FT   DOMAIN          569..732
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
SQ   SEQUENCE   850 AA;  96827 MW;  C38C7517C21BAD43 CRC64;
     MASKLSFKRM DSIAEAMPDA LRQSRYQMKR CFQRYVSKGK RLLKNQQLME ELEKSLDDKV
     EKEKLVEGFL GYIICSTQEA VVLPPFVAFA VRMNPGIWEY VKVHSDDLSV EGITPSEYLK
     FKETLYDEKW AKDDNSLEVD FGALDLSTPH LTLPSSIGNG LQFVSKFMSS KLGGKPESMK
     PLLDYLLTLN YRGEKLMIND TIDTVSKLQT ALLLAEVFVS GLPKYTPYLK FEQRFQEWGL
     EKGWGDTAER CKETLNCLSE VLQAPDPTNM EKFFSRVPSI FSIVIFSIHG YFGQEKVLGL
     PDTGGQVVYI LDQVRAMEEE LLQRIKQQGL HVTPKILVLT RLIPDAKGTK CNVELEPVEN
     TKYSHILRVP FKTEDGKDLR QWVSRFDIYP YLERYAQDSC AKILDILEGK PDLIIGNYTD
     GNLVASLLSN KLCVTQGTIA HALEKTKYED SDVKWREMDQ KYHFSCQFTA DMISMNTSDF
     IITSTYQEIA GSKEKPGQYE HHYAFTMPGL CRYATGINVF DPKFNIAAPG ADQSIYFPFT
     QKQKRLTDLH PQIDELLYSK DDTDEHIGYL ADRNKPIIFS MARLDKVKNI TGLVEWYGQN
     KKLRDLVNLV VVAGLLDASQ SKDREEIEEI NKMHNLMDRY QLKGQIRWIK AQTDRVRNGE
     LYRCIADTKG AFVQPALYEA FGLTVIEAMN CGLPTFATNQ GGPAEIIIDG VSGFHVNPIN
     GREAGIKIAD FFQKCKEDPS YWNKVSTAGL QRIYECYTWK IYATRVLNMG STYSFWKTLN
     KEERQAKQRY LQIFYNVQYR NLAKAVARAG DQQARQTTTG VAPSEIVKAA DSDAKVNACV
     FLFFAISLSI
//
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