ID A0A0D3EXX4_9ORYZ Unreviewed; 1223 AA.
AC A0A0D3EXX4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=sucrose-phosphate synthase {ECO:0000256|ARBA:ARBA00012536};
DE EC=2.4.1.14 {ECO:0000256|ARBA:ARBA00012536};
DE AltName: Full=UDP-glucose-fructose-phosphate glucosyltransferase {ECO:0000256|ARBA:ARBA00031191};
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:OBART01G41950.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART01G41950.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART01G41950.1};
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:OBART01G41950.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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 {ECO:0000256|ARBA:ARBA00024883}.
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 Evidence={ECO:0000256|ARBA:ARBA00001481};
CC -!- PATHWAY: Glycan biosynthesis; sucrose biosynthesis; sucrose from D-
CC fructose 6-phosphate and UDP-alpha-D-glucose: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005027}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|ARBA:ARBA00011774}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC {ECO:0000256|ARBA:ARBA00006530}.
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DR AlphaFoldDB; A0A0D3EXX4; -.
DR STRING; 65489.A0A0D3EXX4; -.
DR PaxDb; 65489-OBART01G41950-1; -.
DR EnsemblPlants; OBART01G41950.1; OBART01G41950.1; OBART01G41950.
DR Gramene; OBART01G41950.1; OBART01G41950.1; OBART01G41950.
DR eggNOG; KOG0483; Eukaryota.
DR eggNOG; KOG0853; Eukaryota.
DR HOGENOM; CLU_009583_24_0_1; -.
DR UniPathway; UPA00371; UER00545.
DR Proteomes; UP000026960; Chromosome 1.
DR GO; GO:0005794; C:Golgi apparatus; IEA:EnsemblPlants.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
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 CDD; cd00086; homeodomain; 1.
DR Gene3D; 3.90.1070.10; -; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
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; PF00046; Homeodomain; 1.
DR Pfam; PF05116; S6PP; 1.
DR Pfam; PF00862; Sucrose_synth; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00108,
KW ECO:0000256|RuleBase:RU000682};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Homeobox {ECO:0000256|PROSITE-ProRule:PRU00108,
KW ECO:0000256|RuleBase:RU000682}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108,
KW ECO:0000256|RuleBase:RU000682};
KW Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 80..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1120..1180
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DNA_BIND 1122..1181
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT COILED 1179..1213
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1223 AA; 137956 MW; BAD1B03D9DE94401 CRC64;
MATWRRYWSP AAGAASPRGP HMNFNPTHYF VEEVVKGVDE SDLHRTWIKV VATRNARERS
TRLENMCWRI WHLARKKKQA CIDLSLSFSF FLVFMLELEG ILRISARRKE QEQVRRETSE
DLAEDLFEGE KADTVGELAQ QDTPMKKKFQ RNFSELTVSW SDENKEKKLY IVLISLHGLV
RGDNMELGRD SDTGGQVKYV VELARALAMM PGVYRVDLFT RQVSSPEVDW SYGEPTEMLT
SGSTDGEGSG ESAGAYIVRI PCGPRDKYLR KEALWPYLQE FVDGALAHIL NMSKALGEQV
SNGKLVLPYV IHGHYADAGD VAALLSGALN VPMVLTGHSL GRNKLEQIMK QGRMSKEEID
STYKIMRRIE GEELALDAAE LVITSTRQEI DEQWGLYDGF DVKLEKVLRA RARRGVSCHG
RFMPRMVVIP PGMDFSSVVV PEDTSDGDDG KDFEIASPRS LPPIWAEVMR FLTNPHKPMI
LALSRPDPKK NITTLVKAFG ECRPLRELAN LILIMGNRDD IDEMSAGNAS VLTTVLKLID
KYDLYGSVAF PKHHKQSDVP EIYRLTGKMK GVFINPALVE PFGLTLIEAA AHGLPIVATK
NGGPALNNGL LVDPHDQHAI ADALLKLVAD KNLWQECRKN GLRNIQLYSW PEHCRTYLTR
IAGCRIRNPR WLMDTPADAA AEEEEALEDS LMDVQDLSLR LSIDGERGSS MNDAPSSDPQ
DSVQRIMNKI KRSSPADTDG AKIPAEAAAT ATSGAMNKYP LLRRRRRLFV IAVDCYGDDG
SASKRMLQVI QEVFRAVRSD SQMSRISGFA LSTAMPLPET LKLLQLGKIP PTDFDALICG
SGSEVYYPGT AQCVDAGGRL RPDQDYLLHI NHRWSHDGAK QTIAKLAHDG SGTNVEPDVE
SCNPHCVSFF IKDPNKVRTI DEMRERMRMR GLRCHLMYCR NATRLQVVPL LASRSQALRY
LFVRWGLSVG NMYLIVGEHG DTDHEEMLSG LHKTVIIRGV TEKGSEQLVR SSGSYQREDV
VPSESPLIAF TKGDLKADEI MRALKEVTKA ASGMDWQRPL CKTAYWFQSR VYTNMEEKEE
MTMLSLGVGA ASKHSISNRK FRLKEVTDHK FNLGDQDHNS GHVRKKLRLS EEQLTVLENM
YEAGSNLDQA LKQGLAEKLN IKPRQFEVWF QNRRARTKHK QIEEECKNLK RWLEGLNKEN
QRLKMELMRN AQKDCIKKGI QQW
//
