SUS1_HORVU
ID SUS1_HORVU Reviewed; 807 AA.
AC P31922;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Sucrose synthase 1;
DE EC=2.4.1.13;
DE AltName: Full=Sucrose-UDP glucosyltransferase 1;
GN Name=SS1;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Abyssinian 2231; TISSUE=Endosperm;
RX PubMed=1388123; DOI=10.1016/0014-5793(92)81143-a;
RA Sanchez de la Hoz P., Vicente-Carbajosa J., Mena M., Carbonero P.;
RT "Homologous sucrose synthase genes in barley (Hordeum vulgare) are located
RT in chromosomes 7H (syn. 1) and 2H. Evidence for a gene translocation?";
RL FEBS Lett. 310:46-50(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 223-807.
RC STRAIN=cv. Pallas;
RA Brandt J., Thordal-Christensen H., Collinge D.B.;
RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=12223688; DOI=10.1104/pp.114.1.55;
RA Guerin J., Carbonero P.;
RT "The spatial distribution of sucrose synthase isozymes in barley.";
RL Plant Physiol. 114:55-62(1997).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12773636; DOI=10.1093/pcp/pcg062;
RA Baroja-Fernandez E., Munoz F.J., Saikusa T., Rodriguez-Lopez M.,
RA Akazawa T., Pozueta-Romero J.;
RT "Sucrose synthase catalyzes the de novo production of ADPglucose linked to
RT starch biosynthesis in heterotrophic tissues of plants.";
RL Plant Cell Physiol. 44:500-509(2003).
CC -!- FUNCTION: Sucrose-cleaving enzyme that provides UDP-glucose and
CC fructose for various metabolic pathways. {ECO:0000269|PubMed:12773636}.
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:0000269|PubMed:12773636};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30 mM for Sucrose {ECO:0000269|PubMed:12223688};
CC KM=5 uM for UDP {ECO:0000269|PubMed:12223688};
CC -!- SUBUNIT: Forms homotetramers. In endosperm it forms both homotetramers
CC and heterotetramers with SS2, all three possible heterotetramers are
CC formed. {ECO:0000269|PubMed:12223688}.
CC -!- TISSUE SPECIFICITY: Highly expressed in developing endosperm and in
CC roots and, at lower levels, in coleoptiles and aleurone. In 3 day old
CC roots it is detected in cap cells and along the vascular strand,
CC starting just after the meristemic region. In 9 day old leaves it is
CC found in the phloem. In seeds it is distributed throughout the
CC endosperm and also found in the assimilate-unloading tissues, the
CC nucellar projection, the vascular area and at a high concentration in
CC the chalazal region. {ECO:0000269|PubMed:12223688}.
CC -!- DEVELOPMENTAL STAGE: Activity increases as seeds develop.
CC {ECO:0000269|PubMed:12773636}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. Plant sucrose
CC synthase subfamily. {ECO:0000305}.
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DR EMBL; X65871; CAA46701.1; -; mRNA.
DR EMBL; X66728; CAA47264.1; -; mRNA.
DR PIR; S29242; S29242.
DR AlphaFoldDB; P31922; -.
DR SMR; P31922; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR PRIDE; P31922; -.
DR BRENDA; 2.4.1.13; 2687.
DR SABIO-RK; P31922; -.
DR ExpressionAtlas; P31922; baseline and differential.
DR GO; GO:0016157; F:sucrose synthase activity; IEA:UniProtKB-EC.
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; Transferase.
FT CHAIN 1..807
FT /note="Sucrose synthase 1"
FT /id="PRO_0000204649"
FT REGION 272..748
FT /note="GT-B glycosyltransferase"
FT /evidence="ECO:0000250|UniProtKB:P49040"
FT CONFLICT 370
FT /note="I -> IL (in Ref. 2; CAA47264)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="I -> Y (in Ref. 2; CAA47264)"
FT /evidence="ECO:0000305"
FT CONFLICT 392..393
FT /note="NE -> KQ (in Ref. 2; CAA47264)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 807 AA; 92211 MW; A863A8C876A060C8 CRC64;
MAAKLTRLHS LRERLGATFS SHPNELIALF SRYVHQGKGM LQRHQLLAEF DALFESDKEK
YAPFEDILRA AQEAIVLPPW VALAIRPRTG VWDYIRVNVS ELAVEELTVS EYLAFKEQLV
DEHASRKFVL ELDFEPFNAS FPRPSMSKSY GKGVQFLNRH LSSKLFQDKE SLYPLLNFLK
AHNYKGTTMI LNDRIQSLRG LQSALRKAEE YLVSIPEDTP SSEFNHRFQE LGLEKGWGDT
AKRVHDTIHL LLDLLEAPDP ASLEKFLGTI PMMFNVVILS PHGYFAQSNV LGYPDTGGQV
VYILDQVRAL ENEMLLRIKQ QGLDITPKIL IVTRLLPDAV GTTCGQRLEK VIGTEHTDIL
RVPFRTENGI RKWISRFDVW PYLETYTEDV ANELMREMQT KPDLIIGNYS DGNLVATLLA
HKLGVTQCTI AHALEKTKYP NSDIYLDKFD SQYHFSCQFT ADLIAMNHTD FIITSTFQEI
AGSKDSVGQY ESHIAFTLPD LYRVVHGIDV FDPKFNIVSP GADMTVYFPY TETDKRLTAF
HSEIEELLYS DVENDEHKFV LKDRNKPIIF SMARLDRVKN MTGLVEMYGK NAHLKDLANL
VIVAGDHGKE SKDREEQAEF KRMYSLIEEY KLKGHIRWIS AQMNRVRNGE LYRYICDTKG
AFVQPAFYEA FGLTVIEAMT CGLPTIATCH GGPAEIIVDG VSGLHIDPYH SDKAADILVN
FFEKSTADPS YWDKISQGGL KRIYEKYTWK LYSERLMTLT GVYGFWKYVS NLERRETRRY
LEMFYALKYR SLAAAVPLAV DGESSGN
