SUS2_HORVU
ID SUS2_HORVU Reviewed; 816 AA.
AC P31923; P83182; Q9ZR49;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Sucrose synthase 2;
DE EC=2.4.1.13;
DE AltName: Full=Sucrose-UDP glucosyltransferase 2;
GN Name=SS2;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Sundance; TISSUE=Endosperm;
RX PubMed=8458435; DOI=10.1016/0014-5793(93)80087-b;
RA Martinez de Ilarduya O., Vicente-Carbajosa J., Sanchez de la Hoz P.,
RA Carbonero P.;
RT "Sucrose synthase genes in barley. cDNA cloning of the Ss2 type and tissue-
RT specific expression of Ss1 and Ss2.";
RL FEBS Lett. 320:177-181(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Sundance; TISSUE=Endosperm;
RA Acevedo F., Martinez de Ilarduya O., Guerin J., Diaz I., Carbonero P.;
RT "Complete barley sucrose synthase type II.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 232-238 AND 393-402.
RC STRAIN=cv. Scarlet; TISSUE=Endosperm;
RA Baroja-Fernandez E., Munoz F.J., Saikusa T., Bastarrica-Berasategui A.,
RA Moreno-Bruna B., Zandueta-Criado A., Rodriguez-Lopez M., Akazawa T.,
RA Pozueta-Romero J.;
RL Submitted (NOV-2001) to UniProtKB.
RN [4]
RP 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 [5]
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 -!- SUBUNIT: Forms homotetramers and heterotetramers with SS1, all three
CC possible heterotetramers are formed. {ECO:0000269|PubMed:12223688}.
CC -!- TISSUE SPECIFICITY: Abundant in developing endosperm, low in aleurone,
CC and undetected in coleoptiles and roots. Also detected in crude
CC extracts of anthers and in immature embryos.
CC {ECO:0000269|PubMed:12223688, ECO:0000269|PubMed:8458435}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA75793.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X69931; CAA49551.1; -; mRNA.
DR EMBL; Y15802; CAA75793.1; ALT_FRAME; Genomic_DNA.
DR PIR; S32451; S32451.
DR AlphaFoldDB; P31923; -.
DR SMR; P31923; -.
DR IntAct; P31923; 1.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR SABIO-RK; P31923; -.
DR ExpressionAtlas; P31923; baseline.
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 Direct protein sequencing; Glycosyltransferase; Transferase.
FT CHAIN 1..816
FT /note="Sucrose synthase 2"
FT /id="PRO_0000204650"
FT REGION 280..757
FT /note="GT-B glycosyltransferase"
FT /evidence="ECO:0000250|UniProtKB:P49040"
FT CONFLICT 131
FT /note="S -> R (in Ref. 2; CAA75793)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="T -> A (in Ref. 2; CAA75793)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="T -> S (in Ref. 2; CAA75793)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="L -> F (in Ref. 2; CAA75793)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="C -> G (in Ref. 2; CAA75793)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="N -> K (in Ref. 2; CAA75793)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="P -> A (in Ref. 2; CAA75793)"
FT /evidence="ECO:0000305"
FT CONFLICT 729
FT /note="G -> D (in Ref. 2; CAA75793)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 816 AA; 92575 MW; CB90A9C42AAB1080 CRC64;
MGETAGERAL SRVHSVRERI GHSLSAHTNE LVAVFSRLVN QGKGMLQPHQ ITAEYNAAIP
EAEREKLKNT PFEDLLRGAQ EAIVIPPWVA LAIRPRPGVW EYVRVNVSEL GVEELSVLRY
LQFKEQLANG STDNNFVLEL DFGPFNASFP RPSLSKSIGN GVQFLNRHLS SKLFHDKESM
YPLLNFLRAH NYKGMTMMLN DRIRSLGTLQ GALRKAETHL SGLPADTPYT EFHHRFQELG
LEKGWGDCAQ RASETIHLLL DLLEAPDPSS LEKFLGTIPM VLNVVILSPH GYFAQANVLG
YPDTGGQVVY ILDQVRAMEN EMLLRIKQQG LDITPKILIV TRMLPDAHGT TCGQRLEKVL
GTEHTHILRV PFKTEDGIVR KWISRFEVWP YLEAYTDDVA HEIAGELQAN PDLIIGNYSD
GNLVACLLAH KLGVTHCTIA HALEKTKYPN SDLYWKKFED HYHFSCQFTA DLIAMNHADF
IITSTFQEIA GNKDTVGQYE SHMAFTMPGL YRVVHGIDVF DPKFNIVSPG ADMSIYFPYT
EQQKRLTSLH TEIEELLFSD VENAEHKFVL KDKKKPIIFS MARLDRVKNM TGLVEMYGRN
PRLQELVNLV VVCGDHGKVS KDKEEQVEFK KMFDLIEKYN LSGHIRWISA QMNRVRNGEL
YRYICDMKGA FVQPAFYEAF GLTVIEAMTC GLPTFATAYG GPAEIIVNGV SGYHIDPYQN
DKASALLVGF FGKCQEDPSH WNKISQGGLQ RIEEKYTWKL YSERLMTLSG VYGFWKYVSN
LDRRETRRYL EMLYALKYRK MAATVPLAVE GETSGE
