ID I1QYU4_ORYGL Unreviewed; 1105 AA.
AC I1QYU4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Sucrose-phosphate synthase {ECO:0000256|ARBA:ARBA00012536, ECO:0000256|RuleBase:RU368006};
DE EC=2.4.1.14 {ECO:0000256|ARBA:ARBA00012536, ECO:0000256|RuleBase:RU368006};
OS Oryza glaberrima (African rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA11G0068600.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORGLA11G0068600.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-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, ECO:0000256|RuleBase:RU368006}.
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 ECO:0000256|RuleBase:RU368006};
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, ECO:0000256|RuleBase:RU368006}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|ARBA:ARBA00011774,
CC ECO:0000256|RuleBase:RU368006}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC {ECO:0000256|ARBA:ARBA00006530, ECO:0000256|RuleBase:RU368006}.
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DR AlphaFoldDB; I1QYU4; -.
DR STRING; 4538.I1QYU4; -.
DR EnsemblPlants; ORGLA11G0068600.1; ORGLA11G0068600.1; ORGLA11G0068600.
DR Gramene; ORGLA11G0068600.1; ORGLA11G0068600.1; ORGLA11G0068600.
DR eggNOG; KOG0853; Eukaryota.
DR HOGENOM; CLU_009583_24_0_1; -.
DR OMA; YEAHVEY; -.
DR UniPathway; UPA00371; UER00545.
DR Proteomes; UP000007306; Unassembled WGS sequence.
DR GO; GO:0046524; F:sucrose-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005986; P:sucrose biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd16419; HAD_SPS; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR InterPro; IPR006380; SPP-like_dom.
DR InterPro; IPR035659; SPS_C.
DR InterPro; IPR012819; SPS_pln.
DR NCBIfam; TIGR02468; sucrsPsyn_pln; 1.
DR PANTHER; PTHR46039; SUCROSE-PHOSPHATE SYNTHASE 3-RELATED; 1.
DR PANTHER; PTHR46039:SF1; SUCROSE-PHOSPHATE SYNTHASE 4; 1.
DR Pfam; PF13579; Glyco_trans_4_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF05116; S6PP; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU368006};
KW Transferase {ECO:0000256|RuleBase:RU368006}.
FT DOMAIN 233..444
FT /note="Glycosyltransferase subfamily 4-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13579"
FT DOMAIN 536..700
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT DOMAIN 896..1053
FT /note="Sucrose phosphatase-like"
FT /evidence="ECO:0000259|Pfam:PF05116"
FT REGION 122..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1105 AA; 119363 MW; DEEC119F7CA59958 CRC64;
MAVGNEWING YLEAILDAGV KLREQRGAAA VQLPPLLPAP EDAASAVATA ATYSPTRYFV
EEVVSRFDDR DLHKTWTKVV AMRNSQERNN RLENLCWRIW NVARRKKQVE WEFSRQLSRR
RLEQELGSRE AAADLSELSE GEKDGKPDTH PPPPAAAAEA AADDGGGGDH QQQQQQPPPH
QLSRFARINS DPRIVSDEEE EVTTDRNLYI VLISIHGLVR GENMELGRDS DTGGQVKYVV
ELARALAATP GVHRVDLLTR QISCPDVDWT YGEPVEMLTV PAADADDEDG GGGSSGGAYI
VRLPCGPRDK YLPKESLWPH IPEFVDRALA HVTNVARALG EQLSPPPPSD GAGAAAQAVW
PYVIHGHYAD AAEVAALLAS ALNVPMVMTG HSLGRNKLEQ LLKLGRMPRA EIQGTYKIAR
RIEAEETGLD AADMVVTSTK QEIEEQWGLY DGFDLKVERK LRVRRRRGVS CLGRYMPRMV
VIPPGMDFSY VDTQDLAADG AGGAGDAADL QLLINPNKAK KPLPPIWSEV LRFFTNPHKP
MILALSRPDP KKNVTTLLKA YGESRHLREL ANLTLILGNR DDIEEMSGGA ATVLTAVLKL
IDRYDLYGQV AYPKHHKQTD VPHIYRLAAK TKGVFINPAL VEPFGLTIIE AAAYGLPVVA
TKNGGPVDIL KVLSNGLLVD PHDAAAITAA LLSLLADKSR WSECRRSGLR NIHRFSWPHH
CRLYLSHVAA SCDHPAPHQL LRVPPSPSSS SATSAAAGGG GAAASSEPLS DSLRDLSLRI
SVDAASPDLS AGDSAAAILD ALRRRRSTDR PAASSAARAI GFAPGRRQSL LVVAVDCYGD
DGKPNVEQLK KVVELAMSAG DGDDAGGRGY VLSTGMTIPE AVDALRACGA DPAGFDALIC
SSGAEICYPW KGEKLAADEE YAGHVAFRWP GDHVRSAVPR LGKADGAQEA DLAVDAAACS
VHCHAYAAKD ASKVKKVDWI RQALRMRGFR CNLVYTRACT RLNVVPLSAS RPRALRYLSI
QWGIDLSKVA VLVGEKGDTD RERLLPGLHR TVILPGMVAA GSEELLRDED GFTTEDVVAM
DSPNIVTLAD GQDIAAAAAD LLKAI
//
