ID A0A2I4E3Y8_JUGRE Unreviewed; 1063 AA.
AC A0A2I4E3Y8;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
GN Name=LOC108986051 {ECO:0000313|RefSeq:XP_018814107.1};
GN ORFNames=F2P56_023188 {ECO:0000313|EMBL:KAF5459215.1};
OS Juglans regia (English walnut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Juglandaceae; Juglans.
OX NCBI_TaxID=51240 {ECO:0000313|Proteomes:UP000235220, ECO:0000313|RefSeq:XP_018814107.1};
RN [1] {ECO:0000313|EMBL:KAF5459215.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5459215.1};
RA Martinez-Garcia P.J., Crepeau M.W., Puiu D., Gonzalez-Ibeas D., Whalen J.,
RA Stevens K., Paul R., Butterfield T., Britton M., Reagan R., Chakraborty S.,
RA Walawage S.L., Vasquez-Gross H.A., Cardeno C., Famula R., Pratt K.,
RA Kuruganti S., Aradhya M.K., Leslie C.A., Dandekar A.M., Salzberg S.L.,
RA Wegrzyn J.L., Langley C.H., Neale D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF5459215.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5459215.1};
RA Marrano A., Britton M., Zimin A.V., Zaini P.A., Workman R., Puiu D.,
RA Bianco L., Allen B.J., Troggio M., Leslie C.A., Timp W., Dendekar A.,
RA Salzberg S.L., Neale D.B.;
RT "Walnut 2.0.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:XP_018814107.1}
RP IDENTIFICATION.
RC TISSUE=Leaves {ECO:0000313|RefSeq:XP_018814107.1};
RG RefSeq;
RL Submitted (NOV-2023) 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|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 EMBL; LIHL02000010; KAF5459215.1; -; Genomic_DNA.
DR RefSeq; XP_018814107.1; XM_018958562.2.
DR STRING; 51240.A0A2I4E3Y8; -.
DR EnsemblPlants; Jr10_22650_p1; cds.Jr10_22650_p1; Jr10_22650.
DR GeneID; 108986051; -.
DR Gramene; Jr10_22650_p1; cds.Jr10_22650_p1; Jr10_22650.
DR KEGG; jre:108986051; -.
DR OrthoDB; 1206157at2759; -.
DR UniPathway; UPA00371; UER00545.
DR Proteomes; UP000235220; Chromosome 10.
DR Proteomes; UP000619265; Unassembled WGS sequence.
DR GO; GO:0016157; F:sucrose synthase activity; IEA:InterPro.
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; cd03800; GT4_sucrose_synthase; 1.
DR CDD; cd16419; HAD_SPS; 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 InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR023214; HAD_sf.
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:SF2; SUCROSE-PHOSPHATE SYNTHASE 1; 1.
DR PANTHER; PTHR46039; SUCROSE-PHOSPHATE SYNTHASE 3-RELATED; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF05116; S6PP; 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:RU368006};
KW Reference proteome {ECO:0000313|Proteomes:UP000235220};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368006}.
FT DOMAIN 168..432
FT /note="Sucrose synthase"
FT /evidence="ECO:0000259|Pfam:PF00862"
FT DOMAIN 472..645
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT DOMAIN 805..1006
FT /note="Sucrose phosphatase-like"
FT /evidence="ECO:0000259|Pfam:PF05116"
FT REGION 91..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1063 AA; 118858 MW; C85BF32DCC1E81E4 CRC64;
MAGNDWINSY LEAILDVGPG LDNAKSSLLL RERGHFSPTR YFVEEVITGF DETDLHRSWV
RAAATRSPQE RNTRLENLSW RIWNLARQKK QHEGEEAQRM AKRRLERERG RREVAADMSE
DLSEGEKGDV VSDMSAHGES NRPRLPRISS VDAMETWAAQ QKGKNLYIVL VSLHGLIRGE
NMELGRDSDT GGQVKYVVEL ARALGSMPGV YRVDLLTRQV SSPEVDWSYG EPTEMLTPRN
SEGYMDDMGE SSGAYIIRIP FGPKDKYIPK ELLWPHIPEF VDGALNHIIQ MSKVLGEQIG
GGHPIWPVAI HGHYADAGDS AALLSGALNV PMLFTGHSLG RDKLEQLLKQ GRLSKDEINT
TYKIMRRIEA EELSLDASEI LITSTRQEIE EQWRLYDGFD PVLQRKLRAR TRRNVSCYGR
FMPRMEVIPP GMEFHHIVPQ CGDMDGEIEG TEDHPASPDP HIWSEIMRFF TNPRKPMILA
LARADPKKNI TTLVKAFGEC RPLRELANLT LIMGNRDGID EMSSTNSSVL LSVLKLIDKY
DLYGQVAYPK HHKQSEVPDI YRLAAKTKGV FINPAFIEPF GLTLLEASAY GLPIVATKNG
GPVDIHRVLD NGLLVDPHDQ QSIADALLKL VADKQLWTRC QQNGLKNIHL FSWPEHCKTY
LSRIASCKAR YPQWQRNDDE DENSESESQG DSLRDMQDLS LKDLSLNLKF SFDGEKSGAG
GNDTSSESEG NAADRGSKLE TAVLTWSKGI SKDARKAGFT EKADQNSSAG RFPALRRRKY
LFVIAVDGDS DTGLLETVRK IFKAVEQGRS EGSIGFILST SLTISEIYEI LVSGGLKPND
FDAFICNSGS DLYYSSLNLE DGPFVVDLYY HSHIEYRWGA EGLRKALVRW AASITDKNTG
NEEQLVTTAE QLSTNYCYAF KVQKPGMLPH VKELRKWLRI QALRCHVICG QNGTRLNVIP
VLASRSQALR YLYVRWGAEL SKMVVFVGEC GDTDYEGLLG GLHKSVILKG TCSNDGSQLH
GNRSYPLSDV LPSDSPGIVQ TIEEGASDDD IRAALEKLVL LKG
//
