SPSA_VICFA
ID SPSA_VICFA Reviewed; 1059 AA.
AC Q43876;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Probable sucrose-phosphate synthase;
DE EC=2.4.1.14;
DE AltName: Full=UDP-glucose-fructose-phosphate glucosyltransferase;
GN Name=SPS;
OS Vicia faba (Broad bean) (Faba vulgaris).
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; Vicia.
OX NCBI_TaxID=3906;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Fribo; TISSUE=Seed coat;
RX PubMed=8921916; DOI=10.1016/0378-1119(96)00373-3;
RA Heim U., Weber H., Wobus U.;
RT "Cloning and characterization of full-length cDNA encoding sucrose
RT phosphate synthase from faba bean.";
RL Gene 178:201-203(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 198-314.
RC STRAIN=cv. Fribo;
RA Buchner P.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in photosynthetic sucrose synthesis by
CC catalyzing the rate-limiting step of sucrose biosynthesis from UDP-
CC glucose and fructose- 6-phosphate. Involved in the regulation of carbon
CC partitioning in the leaves of plants. May regulate the synthesis of
CC sucrose and therefore play a major role as a limiting factor in the
CC export of photoassimilates out of the leaf. Plays a role for sucrose
CC availability that is essential for plant growth and fiber elongation
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 6-phosphate + UDP-alpha-D-glucose = H(+) +
CC sucrose 6(F)-phosphate + UDP; Xref=Rhea:RHEA:22172,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57634, ChEBI:CHEBI:57723,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.14;
CC -!- ACTIVITY REGULATION: Activity is regulated by phosphorylation and
CC moderated by concentration of metabolites and light.
CC -!- PATHWAY: Glycan biosynthesis; sucrose biosynthesis; sucrose from D-
CC fructose 6-phosphate and UDP-alpha-D-glucose: step 1/2.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. {ECO:0000305}.
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DR EMBL; Z56278; CAA91217.1; -; mRNA.
DR EMBL; Z48640; CAA88587.1; -; mRNA.
DR PIR; S53083; S53083.
DR PIR; T12195; T12195.
DR AlphaFoldDB; Q43876; -.
DR SMR; Q43876; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR UniPathway; UPA00371; UER00545.
DR GO; GO:0016157; F:sucrose synthase activity; IEA:InterPro.
DR GO; GO:0046524; F:sucrose-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005986; P:sucrose biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16419; HAD_SPS; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006380; SPP_N.
DR InterPro; IPR044161; SPS.
DR InterPro; IPR035659; SPS_C.
DR InterPro; IPR012819; SPS_pln.
DR InterPro; IPR000368; Sucrose_synth.
DR PANTHER; PTHR46039; PTHR46039; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF05116; S6PP; 1.
DR Pfam; PF00862; Sucrose_synth; 1.
DR TIGRFAMs; TIGR02468; sucrsPsyn_pln; 1.
PE 2: Evidence at transcript level;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..1059
FT /note="Probable sucrose-phosphate synthase"
FT /id="PRO_0000204675"
FT REGION 95..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1059 AA; 118204 MW; FE3B49081A48EC99 CRC64;
MAGNDWLNSY LEAILDVGPG LDDAKSSLLL RERGRFSPTR YFVEEVIGFD ETDLYRSWVR
ASSSRSPQER NTRLENMCWR IWNLARQKKQ LESEAVQRVN KRRLERERGR REATADMSED
LSEGERGDPV SDVSTHGGGD SVKSRLPRIS SADAMETWVN SQKGKKLYIV LISIHGLIRG
ENMELGRDSD TGGQVKYVVE LARALGSMPG VYRVDLLTRQ VSSPDVDWSY GEPTEMLAPR
NTDEFGDDMG ESSGAYIIRI PFGPRNKYIP KEELWPYIPE FVDGAMGHII QMSKALGEQI
GSGHAVWPVA IHGHYADAGD SAALLSGALN VPMIFTGHSL GRDKLEQLLK QGRLSTDEIN
STYKIMRRIE AEELALDGTE IVITSTRQEI EEQWRLYNGF DPVLERKIRA RIRRNVSCYG
RYMPRMSVIP PGMEFHHIAP LDGDIETEPE GILDHPAPQD PPIWSEIMRF FSNPRKPVIL
ALARPDPKKN ITTLVKAFGE CRPLRELANL TLIMGNRDGI DEMSSTSSSV LLSVLKLIDK
YDLYGQVAYP KHHKQSDVPD IYRLAAKTKG VFINPAFIEP FGLTLIEAAA YGLPMVATKN
GGPVDIHRVL DNGLLIDPHD EKSIADALLK LVSNKQLWAK CRQNGLKNIH LFSWPEHCKT
YLSKIATCKP RHPQWQRSED GGESSESEES PGDSLRDIQD LSLNLKFSLD GERSGDSGND
NSLDPDGNAT DRTTKLENAV LSWSKGISKD TRRGGATEKS GQNSNASKFP PLRSRNRLFV
IAVDCDTTSG LLEMIKLIFE AAGEERAEGS VGFILSTSLT ISEIQSFLIS GGLSPNDFDA
YICNSGSDLY YPSLNSEDRL FVGDLYFHSH IEYRWGGEGL RKTLIRWASS ITDKKSENNE
QIVSPAEQLS TDYCYAFNVR KAGMAPPLKE LRKLMRIQAL RCHPIYCQNG TRLNVIPVLA
SRSQALRYLY VRWGFELSKM VVFVGECGDT DYEGLVGGLH KSVILKGVGS RAISQLHNNR
NYPLSDVMPL DSPNIVQATE GSSSADIQAL LEKVGYHKG
