ID   SUS_SOYBN               Reviewed;         805 AA.
AC   P13708; O22624;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Sucrose synthase;
DE            EC=2.4.1.13;
DE   AltName: Full=Nodulin-100;
DE            Short=N-100;
DE   AltName: Full=Sucrose-UDP glucosyltransferase;
GN   Name=SS;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Hobbit; TISSUE=Root nodule;
RA   Zhang X.-Q., Verma D.P.S., Patil S., Arredondo-Peter R., Miao G.-H.,
RA   Kuismanen R., Klucas R.V., Chollet R.;
RT   "Cloning of a full-length sucrose synthase cDNA from soybean (Glycine max)
RT   root nodules.";
RL   (er) Plant Gene Register PGR97-173(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 679-805.
RC   STRAIN=cv. Prize; TISSUE=Root nodule;
RX   PubMed=2889731; DOI=10.1016/s0021-9258(18)47856-8;
RA   Thummler F., Verma D.P.S.;
RT   "Nodulin-100 of soybean is the subunit of sucrose synthase regulated by the
RT   availability of free heme in nodules.";
RL   J. Biol. Chem. 262:14730-14736(1987).
RN   [3]
RP   PHOSPHORYLATION.
RX   PubMed=9237614; DOI=10.1016/s0014-5793(97)00537-1;
RA   Zhang X.-Q., Chollet R.;
RT   "Seryl-phosphorylation of soybean nodule sucrose synthase (nodulin-100) by
RT   a Ca2+-dependent protein kinase.";
RL   FEBS Lett. 410:126-130(1997).
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   -!- SUBUNIT: Homotetramer.
CC   -!- PTM: Phosphorylated on serine residue(s). {ECO:0000269|PubMed:9237614}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. Plant sucrose
CC       synthase subfamily. {ECO:0000305}.
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DR   EMBL; AF030231; AAC39323.1; -; mRNA.
DR   PIR; A29484; A29484.
DR   RefSeq; NP_001237525.1; NM_001250596.1.
DR   AlphaFoldDB; P13708; -.
DR   SMR; P13708; -.
DR   STRING; 3847.GLYMA13G17421.1; -.
DR   iPTMnet; P13708; -.
DR   PRIDE; P13708; -.
DR   ProMEX; P13708; -.
DR   EnsemblPlants; KRH19379; KRH19379; GLYMA_13G114000.
DR   EnsemblPlants; KRH19380; KRH19380; GLYMA_13G114000.
DR   EnsemblPlants; KRH19381; KRH19381; GLYMA_13G114000.
DR   GeneID; 547508; -.
DR   Gramene; KRH19379; KRH19379; GLYMA_13G114000.
DR   Gramene; KRH19380; KRH19380; GLYMA_13G114000.
DR   Gramene; KRH19381; KRH19381; GLYMA_13G114000.
DR   KEGG; gmx:547508; -.
DR   eggNOG; KOG0853; Eukaryota.
DR   InParanoid; P13708; -.
DR   OrthoDB; 153947at2759; -.
DR   BioCyc; MetaCyc:MON-8881; -.
DR   BRENDA; 2.4.1.13; 2483.
DR   Proteomes; UP000008827; Chromosome 13.
DR   Genevisible; P13708; GM.
DR   GO; GO:0016157; F:sucrose synthase activity; IBA:GO_Central.
DR   GO; GO:0009877; P:nodulation; IEA:UniProtKB-KW.
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; Nodulation; Phosphoprotein; Reference proteome;
KW   Transferase.
FT   CHAIN           1..805
FT                   /note="Sucrose synthase"
FT                   /id="PRO_0000204663"
FT   REGION          275..752
FT                   /note="GT-B glycosyltransferase"
FT                   /evidence="ECO:0000250|UniProtKB:P49040"
FT   MOD_RES         11
FT                   /note="Phosphoserine; by CPK"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        680
FT                   /note="V -> L (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        737..738
FT                   /note="DK -> ET (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        804
FT                   /note="A -> V (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   805 AA;  92244 MW;  BB14E55EB4F5587B CRC64;
     MATDRLTRVH SLRERLDETL TANRNEILAL LSRIEAKGKG ILQHHQVIAE FEEIPEENRQ
     KLTDGAFGEV LRSTQEAIVL PPWVALAVRP RPGVWEYLRV NVHALVVEEL QPAEYLHFKE
     ELVDGSSNGN FVLELDFEPF NAAFPRPTLN KSIGNGVQFL NRHLSAKLFH DKESLHPLLE
     FLRLHSVKGK TLMLNDRIQN PDALQHVLRK AEEYLGTVPP ETPYSEFEHK FQEIGLERGW
     GDNAERVLES IQLLLDLLEA PDPCTLETFL GRIPMVFNVV ILSPHGYFAQ DNVLGYPDTG
     GQVVYILDQV RALENEMLHR IKQQGLDIVP RILIITRLLP DAVGTTCGQR LEKVFGTEHS
     HILRVPFRTE KGIVRKWISR FEVWPYLETY TEDVAHELAK ELQGKPDLIV GNYSDGNIVA
     SLLAHKLGVT QCTIAHALEK TKYPESDIYW KKLEERYHFS CQFTADLFAM NHTDFIITST
     FQEIAGSKDT VGQYESHTAF TLPGLYRVVH GIDVFDPKFN IVSPGADQTI YFPHTETSRR
     LTSFHPEIEE LLYSSVENEE HICVLKDRSK PIIFTMARLD RVKNITGLVE WYGKNAKLRE
     LVNLVVVAGD RRKESKDLEE KAEMKKMYGL IETYKLNGQF RWISSQMNRV RNGELYRVIC
     DTRGAFVQPA VYEAFGLTVV EAMTCGLPTF ATCNGGPAEI IVHGKSGFHI DPYHGDRAAD
     LLVDFFEKCK LDPTHWDKIS KAGLQRIEEK YTWQIYSQRL LTLTGVYGFW KHVSNLDRRE
     SRRYLEMFYA LKYRKLAESV PLAAE