ID A0A371FQM0_MUCPR Unreviewed; 1037 AA.
AC A0A371FQM0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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};
DE Flags: Fragment;
GN Name=SPS4 {ECO:0000313|EMBL:RDX80552.1};
GN ORFNames=CR513_38890 {ECO:0000313|EMBL:RDX80552.1};
OS Mucuna pruriens (Velvet bean) (Dolichos pruriens).
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; indigoferoid/millettioid clade; Phaseoleae; Mucuna.
OX NCBI_TaxID=157652 {ECO:0000313|EMBL:RDX80552.1, ECO:0000313|Proteomes:UP000257109};
RN [1] {ECO:0000313|EMBL:RDX80552.1, ECO:0000313|Proteomes:UP000257109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jos {ECO:0000313|Proteomes:UP000257109};
RC TISSUE=Seed {ECO:0000313|EMBL:RDX80552.1};
RA Nnadi N.E., Vos R., Hasami M.H., Devisetty U.K., Aguiy J.C.;
RT "Draft genome of Mucuna pruriens seed.";
RL Submitted (MAY-2018) 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 {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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDX80552.1}.
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DR EMBL; QJKJ01008180; RDX80552.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371FQM0; -.
DR STRING; 157652.A0A371FQM0; -.
DR UniPathway; UPA00371; UER00545.
DR Proteomes; UP000257109; 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:0005986; P:sucrose biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd03800; GT4_sucrose_synthase; 1.
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; SUCROSE-PHOSPHATE SYNTHASE 3-RELATED; 1.
DR PANTHER; PTHR46039:SF1; SUCROSE-PHOSPHATE SYNTHASE 4; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368006}.
FT DOMAIN 183..409
FT /note="Sucrose synthase"
FT /evidence="ECO:0000259|Pfam:PF00862"
FT DOMAIN 487..659
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT DOMAIN 796..970
FT /note="Sucrose phosphatase-like"
FT /evidence="ECO:0000259|Pfam:PF05116"
FT REGION 125..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RDX80552.1"
SQ SEQUENCE 1037 AA; 117048 MW; 717E2D1B12B4BE82 CRC64;
MAAVNEWVNG YLEAILDVGS SIRKKKNDGK LKIKNIAKFD EEEEDNKDQR EEKLFNPTTK
YFVQEVVNSF DEHDLYRTWV KVIATRNMRE RSNRLENMCW RIWHLTRKKK QIAWDDGQKL
ARRRLAREQG RHDAANDLSE LSEGEKEKGD ANALEPALKD NISRITSEMQ LWLEDDNTRN
LYIVLISIHG LVRGDNMELG RDSDTGGQVK YVVELARALA NTKGVYRVDL LTRQIASPGE
VDSSYGEPIE MLSCPSDGSD CGGAYIIRLP CGPRDKYIPK ESLWPHLPEF VDGALSHIVN
MARVLGEHVN GGKPSWPYVI HGHYADAGEV AAHLSGALNV PMVLTGHSLG RNKFEQLLKQ
GRLSREAINA TYKIMRRIEA EELGVDAAEM VVTSTRQEIE EQWGLYDGFD LKLERKLRVR
RSRGVSCLGR HMPRMVVIPP GMDFSYVTTQ DSVEGEGDLN SLIGSDRAQS KRNLPPIWSE
IMRFFTNPHK PTILALSRPD PKKNVMTLLK AFGECQALRK LANLTLILGN RDDIEEMSNS
SSTVLTMVLK LIDKYDLYGQ VAYPKHHRQS DVPEIYRLAA KTKGVFINPA LVEPFGLTLI
EAAAYGLPVV ATKNGGPVDI LKALNNGLLI DPHDQKAIED ALLKLVADKN LWLECRINGL
KNIHRFSWPE HCRNYLSHVE HGRNRRSTSL LEITPIDEEP ISDSLRDVED ISFRFSTEGD
SKLNGEMDPA ARQKQIIEAI MCRVSSSGNS YANYFPGRRQ RLVVVAADCY HNDGKIAEAF
QAIIMNVMKA VRPGIRSGRV GVVLLTGLSL QETIEALNSF QLNIEEFDAV VCNSGSEMYY
PWKDLMADAD YEAHVEYAWP GENIRSTITR LARTDDGEEN DIVEYGNACS SRCYSYSVKP
GAMIRKIDEL RQRLRMRGLR CNLVYTHAGL RLNVIPLFAS RKQALRYLSV KWGIDLSKVV
VFVGEKGDTD YEELVAGLQK TLVLKGAVEC GSERLLHSED SFKREDVFSQ DSPNIFYAEK
SYEESDISAI LEHLKVS
//
