ID D7LZZ6_ARALL Unreviewed; 1045 AA.
AC D7LZZ6;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Sucrose-phosphate synthase {ECO:0000256|ARBA:ARBA00012536, ECO:0000256|RuleBase:RU368006};
DE EC=2.4.1.14 {ECO:0000256|ARBA:ARBA00012536, ECO:0000256|RuleBase:RU368006};
GN ORFNames=ARALYDRAFT_488935 {ECO:0000313|EMBL:EFH50247.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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 {ECO:0000256|RuleBase:RU368006}.
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 Evidence={ECO:0000256|ARBA:ARBA00001481,
CC ECO:0000256|RuleBase:RU368006};
CC -!- PATHWAY: Glycan biosynthesis; sucrose biosynthesis; sucrose from D-
CC fructose 6-phosphate and UDP-alpha-D-glucose: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005027, ECO:0000256|RuleBase:RU368006}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|ARBA:ARBA00011774,
CC ECO:0000256|RuleBase:RU368006}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC {ECO:0000256|ARBA:ARBA00006530, ECO:0000256|RuleBase:RU368006}.
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DR EMBL; GL348718; EFH50247.1; -; Genomic_DNA.
DR RefSeq; XP_002873988.1; XM_002873942.1.
DR AlphaFoldDB; D7LZZ6; -.
DR STRING; 81972.D7LZZ6; -.
DR EnsemblPlants; fgenesh2_kg.6__2069__AT5G20280.1; fgenesh2_kg.6__2069__AT5G20280.1; fgenesh2_kg.6__2069__AT5G20280.1.
DR Gramene; fgenesh2_kg.6__2069__AT5G20280.1; fgenesh2_kg.6__2069__AT5G20280.1; fgenesh2_kg.6__2069__AT5G20280.1.
DR eggNOG; KOG0853; Eukaryota.
DR HOGENOM; CLU_009583_24_0_1; -.
DR OrthoDB; 1206157at2759; -.
DR UniPathway; UPA00371; UER00545.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0016157; F:sucrose synthase activity; IEA:InterPro.
DR GO; GO:0046524; F:sucrose-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071836; P:nectar secretion; IEA:EnsemblPlants.
DR GO; GO:0005986; P:sucrose biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd16419; HAD_SPS; 1.
DR Gene3D; 3.90.1070.10; -; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006380; SPP-like_dom.
DR InterPro; IPR035659; SPS_C.
DR InterPro; IPR012819; SPS_pln.
DR InterPro; IPR000368; Sucrose_synth.
DR NCBIfam; TIGR02468; sucrsPsyn_pln; 1.
DR PANTHER; PTHR46039:SF2; SUCROSE-PHOSPHATE SYNTHASE 1; 1.
DR PANTHER; PTHR46039; SUCROSE-PHOSPHATE SYNTHASE 3-RELATED; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF05116; S6PP; 1.
DR Pfam; PF00862; Sucrose_synth; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU368006};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368006}.
FT DOMAIN 170..391
FT /note="Sucrose synthase"
FT /evidence="ECO:0000259|Pfam:PF00862"
FT DOMAIN 472..646
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT DOMAIN 770..994
FT /note="Sucrose phosphatase-like"
FT /evidence="ECO:0000259|Pfam:PF05116"
FT REGION 95..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1045 AA; 117348 MW; C9679015D922E5D5 CRC64;
MAGNDWVNSY LEAILDVGQG LDDARSSPSL LLRERGRFTP SRYFVEEVIT GYDETDLHRS
WVKAVATRSP QERNTRLENM CWRIWNLARQ KKQHEEKEAQ RLAKRRLERE KGRREATADM
SEEFSEGEKG DIISDISTHG ESTKPRLPRI NSAESMELWA SQQKGNKLYL VLISLHGLIR
GENMELGRDS DTGGQVKYVV ELARALGSMP GVYRVDLLTR QVSSPDVDYS YGEPTEMLTP
RDSEDFSDEM GESSGAYIVR IPFGPKDKYI PKELLWPHIA EFVDGAMNHI MQMSNVLGEQ
VGVGKPIWPA AIHGHYADAG DATALLSGAL NVPMLLTGHS LGRDKLEQLL RQGRLSKEEI
NSTYKIMRRI EGEELSLDVS EMVITSTRQE IDEQWRLYDG FDPILERKLR ARIKRNVSCY
GRFMPRMVKI PPGMEFNHIV PHGGDLEDTD GNEEHPTSPD PPIWAEIMRF FSNSRKPMIL
ALARPDPKKN ITTLVKAFGE CRPLRELANL ALIMGNRDGI DEMSSTSSSV LLSVLKLIDK
YDLYGQVAYP KHHKQSDVPD IYRLAAKSKG VFINPAIIEP FGLTLIEAAA HGLPMVATKN
GGPVDIHRVL DNGLLVDPHD QQSISEALLK LVADKHLWAK CRQNGLKNIH QFSWPEHCKT
YLSRITSFKP RHPQWQSDDG GDNSEPESPS DSLRDIQDIS LNLKFSFDGS GNDNYMNQEA
SSMDRKSKIE AAVQNWSKGK DSRKMGSLEK LEVNSGKFPA VRIRKFIVVI ALDFDGEQDT
LEATKRILDA VEKERAEGSV GFILSTSLTI SEVQSFLVSG GLNPNDFDAF ICNSGSDLHY
TSLNNEDGPF VVDFYYHSHI EYRWGGEGLR KTLIRWASSL NEKKADSDEQ IVTLAEHLST
DYCYTFTVKK PAAVPPVREL RKLLRIQALR CHVVYSQNGT RINVIPVLAS RIQALRYLFV
RWGIDMAKMA VFVGESGDTD YEGLLGGLHK SVVLEGVSCS ASNALHANRS YPLTDVISLE
SSNVVHAPPD SDVRDALKKL ELLKD
//
