STSYN_PEA
ID STSYN_PEA Reviewed; 853 AA.
AC Q93XK2; Q8H0M9;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Stachyose synthase;
DE EC=2.4.1.67;
DE AltName: Full=Galactinol--raffinose galactosyltransferase;
DE Flags: Precursor;
GN Name=STS1;
OS Pisum sativum (Garden pea).
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; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAC38094.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 12-36, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Kelvedon Wonder {ECO:0000269|PubMed:11675396};
RC TISSUE=Seed {ECO:0000312|EMBL:CAC38094.1};
RX PubMed=11675396; DOI=10.1074/jbc.m109734200;
RA Peterbauer T., Mucha J., Mach L., Richter A.;
RT "Chain elongation of raffinose in pea seeds. Isolation, characterization,
RT and molecular cloning of a multifunctional enzyme catalyzing the synthesis
RT of stachyose and verbascose.";
RL J. Biol. Chem. 277:194-200(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAD55555.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. SD1 {ECO:0000269|Ref.2};
RC TISSUE=Seed {ECO:0000312|EMBL:CAD55555.1};
RA Peterbauer T., Karner U., Mucha J., Mach L., Jones D.A., Hedley C.L.,
RA Richter A.;
RT "Enzymatic control of the accumulation of verbascose in pea seeds.";
RL Plant Cell Environ. 26:1385-1391(2003).
CC -!- FUNCTION: Catalyzes stachyose synthesis by transfer of a galactosyl
CC moiety from galactinol to raffinose. Also catalyzes verbascose
CC synthesis by galactosyl transfer from galactinol to stachyose or from
CC one stachyose molecule to another. Oligosaccharides of the raffinose
CC family play a protective role in maturation drying of seeds. They may
CC act as cryoprotectants in frost-hardy plants.
CC {ECO:0000269|PubMed:11675396, ECO:0000303|PubMed:11675396}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-galactosyl-(1->3)-1D-myo-inositol + raffinose = myo-
CC inositol + stachyose; Xref=Rhea:RHEA:20776, ChEBI:CHEBI:16634,
CC ChEBI:CHEBI:17164, ChEBI:CHEBI:17268, ChEBI:CHEBI:17505; EC=2.4.1.67;
CC Evidence={ECO:0000269|PubMed:11675396};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.9 mM for galactinol {ECO:0000269|PubMed:11675396};
CC KM=21.1 mM for raffinose {ECO:0000269|PubMed:11675396};
CC Vmax=1.1 nmol/sec/mg enzyme {ECO:0000269|PubMed:11675396};
CC Note=Vmax/KM ratio for galactosyl transfer from galactinol to
CC stachyose is 9.5 fold higher compared with galactosyl transfer from
CC one stachyose molecule to another. {ECO:0000269|PubMed:11675396};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:11675396};
CC -!- PATHWAY: Glycan metabolism; stachyose biosynthesis; stachyose from
CC raffinose: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- POLYMORPHISM: The enzyme from cv. SD1 has very low verbascose synthase
CC activity whereas stachyose synthase activity is normal.
CC {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolases 36 family.
CC {ECO:0000305}.
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DR EMBL; AJ311087; CAC38094.1; -; mRNA.
DR EMBL; AJ512932; CAD55555.1; -; mRNA.
DR AlphaFoldDB; Q93XK2; -.
DR CAZy; GH36; Glycoside Hydrolase Family 36.
DR BioCyc; MetaCyc:MON-12485; -.
DR BRENDA; 2.4.1.67; 4872.
DR SABIO-RK; Q93XK2; -.
DR UniPathway; UPA00925; UER00892.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0047268; F:galactinol-raffinose galactosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0033532; P:stachyose biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR008811; Glycosyl_hydrolases_36.
DR PANTHER; PTHR31268; PTHR31268; 1.
DR Pfam; PF05691; Raffinose_syn; 1.
DR SUPFAM; SSF51445; SSF51445; 2.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Direct protein sequencing;
KW Glycosyltransferase; Transferase.
FT PROPEP 1..11
FT /evidence="ECO:0000269|PubMed:11675396"
FT /id="PRO_0000022432"
FT CHAIN 12..853
FT /note="Stachyose synthase"
FT /evidence="ECO:0000269|PubMed:11675396"
FT /id="PRO_0000022433"
FT CONFLICT 90
FT /note="I -> L (in Ref. 2; CAD55555)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="S -> I (in Ref. 2; CAD55555)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="Y -> C (in Ref. 2; CAD55555)"
FT /evidence="ECO:0000305"
FT CONFLICT 317..318
FT /note="NN -> KK (in Ref. 2; CAD55555)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="G -> V (in Ref. 2; CAD55555)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="I -> F (in Ref. 2; CAD55555)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="H -> Q (in Ref. 2; CAD55555)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="Q -> K (in Ref. 2; CAD55555)"
FT /evidence="ECO:0000305"
FT CONFLICT 658
FT /note="V -> L (in Ref. 2; CAD55555)"
FT /evidence="ECO:0000305"
FT CONFLICT 706
FT /note="E -> Q (in Ref. 2; CAD55555)"
FT /evidence="ECO:0000305"
FT CONFLICT 718
FT /note="L -> F (in Ref. 2; CAD55555)"
FT /evidence="ECO:0000305"
FT CONFLICT 735
FT /note="S -> C (in Ref. 2; CAD55555)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 853 AA; 95890 MW; CB10F18C8D37B38C CRC64;
MAPPLNSTTS NLIKTESIFD LSERKFKVKG FPLFHDVPEN VSFRSFSSIC KPSESNAPPS
LLQKVLAYSH KGGFFGFSHE TPSDRLMNSI GSFNGKDFLS IFRFKTWWST QWIGKSGSDL
QMETQWILIE VPETKSYVVI IPIIEKCFRS ALFPGFNDHV KIIAESGSTK VKESTFNSIA
YVHFSENPYD LMKEAYSAIR VHLNSFRLLE EKTIPNLVDK FGWCTWDAFY LTVNPIGIFH
GLDDFSKGGV EPRFVIIDDG WQSISFDGYD PNEDAKNLVL GGEQMSGRLH RFDECYKFRK
YESGLLLGPN SPPYDPNNFT DLILKGIEHE KLRKKREEAI SSKSSDLAEI ESKIKKVVKE
IDDLFGGEQF SSGEKSEMKS EYGLKAFTKD LRTKFKGLDD VYVWHALCGA WGGVRPETTH
LDTKIVPCKL SPGLDGTMED LAVVEISKAS LGLVHPSQAN ELYDSMHSYL AESGITGVKV
DVIHSLEYVC DEYGGRVDLA KVYYEGLTKS IVKNFNGNGM IASMQHCNDF FFLGTKQISM
GRVGDDFWFQ DPNGDPMGSF WLQGVHMIHC SYNSLWMGQM IQPDWDMFQS DHVCAKFHAG
SRAICGGPIY VSDNVGSHDF DLIKKLVFPD GTIPKCIYFP LPTRDCLFKN PLFDHTTVLK
IWNFNKYGGV IGAFNCQGAG WDPIMQKFRG FPECYKPIPG TVHVTEVEWD QKEETSHLGK
AEEYVVYLNQ AEELSLMTLK SEPIQFTIQP STFELYSFVP VTKLCGGIKF APIGLTNMFN
SGGTVIDLEY VGNGAKIKVK GGGSFLAYSS ESPKKFQLNG CEVDFEWLGD GKLCVNVPWI
EEACGVSDME IFF
