ID   SUS2_MAIZE              Reviewed;         816 AA.
AC   P49036;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Sucrose synthase 2;
DE            EC=2.4.1.13;
DE   AltName: Full=Sucrose-UDP glucosyltransferase 2;
GN   Name=SUS1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8115551; DOI=10.1104/pp.104.1.293;
RA   Huang X.-F., Nguyen-Quoc B., Chourey P.S., Yelle S.;
RT   "Complete nucleotide sequence of the maize (Zea mays L.) sucrose synthase 2
RT   cDNA.";
RL   Plant Physiol. 104:293-294(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Wisconsin 22;
RA   Nguyen-Quoc B., Huang X.-F., Krivitzky M., Yelle S., Lecharny A.;
RT   "Maize sucrose synthase 2: gene eequence and expression in the developing
RT   leaf.";
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION AT SER-15.
RC   TISSUE=Leaf;
RX   PubMed=8883390; DOI=10.1104/pp.112.2.793;
RA   Huber S.C., Huber J.L., Liao P.-C., Gage D.A., McMichael R.W. Jr.,
RA   Chourey P.S., Hannah L.C., Koch K.;
RT   "Phosphorylation of serine-15 of maize leaf sucrose synthase. Occurrence in
RT   vivo and possible regulatory significance.";
RL   Plant Physiol. 112:793-802(1996).
CC   -!- FUNCTION: Sucrose-cleaving enzyme that provides UDP-glucose and
CC       fructose for various metabolic pathways.
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   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. Plant sucrose
CC       synthase subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L22296; AAA33514.1; -; mRNA.
DR   EMBL; L33244; AAA33515.1; -; Genomic_DNA.
DR   RefSeq; NP_001105323.1; NM_001111853.1.
DR   AlphaFoldDB; P49036; -.
DR   SMR; P49036; -.
DR   STRING; 4577.GRMZM2G152908_P01; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   iPTMnet; P49036; -.
DR   PaxDb; P49036; -.
DR   PRIDE; P49036; -.
DR   GeneID; 542247; -.
DR   KEGG; zma:542247; -.
DR   MaizeGDB; 13861; -.
DR   eggNOG; KOG0853; Eukaryota.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P49036; baseline and differential.
DR   GO; GO:0016157; F:sucrose synthase activity; IBA:GO_Central.
DR   GO; GO:0010037; P:response to carbon dioxide; IEA:EnsemblPlants.
DR   GO; GO:0005985; P:sucrose metabolic process; IEA:InterPro.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR000368; Sucrose_synth.
DR   InterPro; IPR012820; Sucrose_synthase_pln/cyn.
DR   PANTHER; PTHR45839; PTHR45839; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   Pfam; PF00862; Sucrose_synth; 1.
DR   TIGRFAMs; TIGR02470; sucr_synth; 1.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..816
FT                   /note="Sucrose synthase 2"
FT                   /id="PRO_0000204653"
FT   REGION          280..757
FT                   /note="GT-B glycosyltransferase"
FT                   /evidence="ECO:0000250|UniProtKB:P49040"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:8883390"
SQ   SEQUENCE   816 AA;  92939 MW;  E4DF863BE7AFC4C8 CRC64;
     MGEGAGDRVL SRLHSVRERI GDSLSAHPNE LVAVFTRLKN LGKGMLQPHQ IIAEYNNAIP
     EAEREKLKDG AFEDVLRAAQ EAIVIPPWVA LAIRPRPGVW EYVRVNVSEL AVEELRVPEY
     LQFKEQLVEE GPNNNFVLEL DFEPFNASFP RPSLSKSIGN GVQFLNRHLS SKLFHDKESM
     YPLLNFLRAH NYKGMTMMLN DRIRSLSALQ GALRKAEEHL STLQADTPYS EFHHRFQELG
     LEKGWGDCAK RAQETIHLLL DLLEAPDPST LEKFLGTIPM VFNVVILSPH GYFAQANVLG
     YPDTGGQVVY ILDQVRAMEN EMLLRIKQCG LDITPKILIV TRLLPDATGT TCGQRLEKVL
     GTEHCHILRV PFRTENGIVR KWISRFEVWP YLETYTDDVA HEIAGELQAN PDLIIGNYSD
     GNLVACLLAH KMGVTHCTIA HALEKTKYPN SDLYWKKFED HYHFSCQFTT DLIAMNHADF
     IITSTFQEIA GNKDTVGQYE SHMAFTMPGL YRVVHGIDVF DPKFNIVSPG ADLSIYFPYT
     ESHKRLTSLH PEIEELLYSQ TENTEHKFVL NDRNKPIIFS MARLDRVKNL TGLVELYGRN
     KRLQELVNLV VVCGDHGNPS KDKEEQAEFK KMFDLIEQYN LNGHIRWISA QMNRVRNGEL
     YRYICDTKGA FVQPAFYEAF GLTVVEAMTC GLPTFATAYG GPAEIIVHGV SGYHIDPYQG
     DKASALLVDF FDKCQAEPSH WSKISQGGLQ RIEEKYTWKL YSERLMTLTG VYGFWKYVSN
     LERRETRRYL EMLYALKYRT MASTVPLAVE GEPSSK