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Database: UniProt
Entry: A5BYM6_VITVI
LinkDB: A5BYM6_VITVI
Original site: A5BYM6_VITVI 
ID   A5BYM6_VITVI            Unreviewed;       850 AA.
AC   A5BYM6;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   24-JAN-2024, entry version 56.
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};
GN   ORFNames=VITISV_026353 {ECO:0000313|EMBL:CAN64012.1};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CAN64012.1};
RN   [1] {ECO:0000313|EMBL:CAN64012.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., Pruss D.,
RA   Pindo M., FitzGerald L.M., Vezzulli S., Reid J., Malacarne G., Iliev D.,
RA   Coppola G., Wardell B., Micheletti D., Macalma T., Facci M., Mitchell J.T.,
RA   Perazzolli M., Eldredge G., Gatto P., Oyzerski R., Moretto M., Gutin N.,
RA   Stefanini M., Chen Y., Segala C., Davenport C., Dematte L., Mraz A.,
RA   Battilana J., Stormo K., Costa F., Tao Q., Si-Ammour A., Harkins T.,
RA   Lackey A., Perbost C., Taillon B., Stella A., Solovyev V., Fawcett J.A.,
RA   Sterck L., Vandepoele K., Grando S.M., Toppo S., Moser C., Lanchbury J.,
RA   Bogden R., Skolnick M., Sgaramella V., Bhatnagar S.K., Fontana P.,
RA   Gutin A., Van de Peer Y., Salamini F., Viola R.;
RT   "The first genome sequence of an elite grapevine cultivar (Pinot noir Vitis
RT   vinifera L.): coping with a highly heterozygous genome.";
RL   PLoS ONE 2:e1326-e1326(2007).
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   EMBL; AM475935; CAN64012.1; -; Genomic_DNA.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   ExpressionAtlas; A5BYM6; baseline and differential.
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:SF24; SUCROSE SYNTHASE 6; 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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU280817}.
FT   DOMAIN          12..571
FT                   /note="Sucrose synthase"
FT                   /evidence="ECO:0000259|Pfam:PF00862"
FT   DOMAIN          583..749
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   REGION          800..850
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        826..840
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   850 AA;  95894 MW;  972DC5DDC515334F CRC64;
     MASSSAPVIK QQDIADTMPD ALKQSRYHMK RCFARFVGSG RRLMKYRHIM EEIEKSIEDK
     AERSRVMDGL LGYILNTTQE AAVVPPYVAF AVRPSPGLWE FVKVSADDLG VDGITSAEYL
     KFKETIFDEN WATDENTLEI DFGAFDYSTP HLTLNSSIGN GLNYVSKFMT SKLSGSSENA
     KPLVEYLLAM NHQGESLMIN EMLNTVSKLQ TALIVAEVFV SSLPKDTPYQ SFEQRLKDWG
     FEKGWGDSAE RVKDTMRTLS EVLQAPDPMK MELLFSRLPN MFNIVVFSPH GYFGQADVLG
     LPDTGGQVVY ILDQVKALEE ELLHRIKQQG LIVKPQILVV TRLIPDARGT KCDQEIEPVL
     NTKHSHILRV PFRTENGVLR QWVSRFDIYP YLERYAQACA LYRLYNPYAT DASAKILAHM
     ECKPDLIIGN YTDGNMVASL MASKLGVTQG TIAHALEKTK YEDSDVKWKE LDGKYHFSCQ
     FTADMFAMNA TDFIITSTFQ EIAGSKDRPG QYENHAAFTM PGLCRVVSGI NVFDTKFNIA
     APGADQSVYF PYMEKQKRLT SFHPAIEELL YSKEDNKEHL GYLSDRKKPI IFSMARLDTV
     KNITGLTEWY GKNKRLRSLV NLVVVAGFFD PSKSKDREEI AEIKKMHSLI EKYQLKGQLR
     WIAAQNDRNR NGELYRCIAD TKGAFVQPAL YEAFGLTVIE AMNCGLPTFA TNQGGPAEII
     FDGVSGFHID PXNGDESSBK IADFFEKCKT DSEYWNKIST AGLQRIYEWQ LNKDQKNAKN
     RYLQLFYNLQ FRKLAKGVPI LNEEPREEPQ QPAATAITKP QQPAPTEGAK PRPSAPTTAP
     KPQPAARHVA
//
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