ID A0A2P5AEC9_PARAD Unreviewed; 1049 AA.
AC A0A2P5AEC9;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=PanWU01x14_340840 {ECO:0000313|EMBL:PON34895.1};
OS Parasponia andersonii (Sponia andersonii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX NCBI_TaxID=3476 {ECO:0000313|EMBL:PON34895.1, ECO:0000313|Proteomes:UP000237105};
RN [1] {ECO:0000313|Proteomes:UP000237105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) 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:PON34895.1}.
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DR EMBL; JXTB01000638; PON34895.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5AEC9; -.
DR STRING; 3476.A0A2P5AEC9; -.
DR OrthoDB; 1206157at2759; -.
DR UniPathway; UPA00371; UER00545.
DR Proteomes; UP000237105; Unassembled WGS sequence.
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; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR InterPro; IPR006380; SPP-like_dom.
DR InterPro; IPR035659; SPS_C.
DR InterPro; IPR012819; SPS_pln.
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; PF13579; Glyco_trans_4_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF05116; S6PP; 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:UP000237105};
KW Transferase {ECO:0000256|RuleBase:RU368006}.
FT DOMAIN 209..402
FT /note="Glycosyltransferase subfamily 4-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13579"
FT DOMAIN 491..664
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT DOMAIN 812..983
FT /note="Sucrose phosphatase-like"
FT /evidence="ECO:0000259|Pfam:PF05116"
SQ SEQUENCE 1049 AA; 117968 MW; 3F083D893E61C607 CRC64;
MARNEWINGY LEAILDVGKK NDGKLNNIAK FEVKEKDRQD KLFSPTKYFV EEVVNSFDES
DLHRTWIKVI ATRNTRERSN RLENMCWRIW HLARKKKQIA WDDAQRLAKR RIEREQGRHD
AAEDLSELSE GEKDIVKGDL KDTSTSTTTT LDHRPFTRIN SDIQIWPDHD DTINSTKSSS
SRNLYIVLIS MHGLVRGQNM ELGRDSDTGG QVKYVVELAR ALANTSGVYR VDLLTRQITS
PDVDSSYGEP NEMLCCPADA AGSCGAYIVR LPCGPRHEYI PKESLWPHIP EFVDGAMAHV
VNMARVLGDQ VNAGKPAWPY VIHGHYADGG EAAVRLSAAL NVPMVMTGHS LGRNKFEQLL
KQGRFSREDI NATYRIVRRI EAEELALDTA EMVVTSTRQE IDEQWGLYDG FDLKLERKLR
VRRRRGVSCL GRYMPRMVVI PPGMDFTNLT TTTDITETDT ADLKSLIDSD RAQTKTNLPP
IWSEVMRFFT NPHKPIILAL SRPDPKKNVT TLLKAYGECQ ALRELANLTL ILGNRDDIEE
MSNSSSVVLT TVLKLIDRYD LYGQVAYPKH HKQSDVPEIY RLAAKTKGVF INPALVEPFG
LTIIEAAAYG LPVVATKNGG PVDILKALNN GVLVDPHDQK AIEDALLKLV GDKNLWLECR
KNGLKNIHRF SWTEHCRNYL SHVEHCRNRH PTTRLEIMPA PEEPLSDSLK DVQDLSLRFS
VEASADFKSN AAESLDAATR QKELIEAITR SRSRASPNGK SGAAAYSPGK RQRLFVIATD
CYDEGRGDFA ESLLQQIMKN VTKAAATGLP GRTGFLLVTG SSLGETLEVL KRCQVNVQEL
DALVCSSGSE MYYPWIDLVA DADYESHVEY RWGGENVRSM AARLARAEGA DEDDIQGYAD
ASSTRCYSYT VKTGGKIRRV DDLRQRLRMR GFRCNLIYTR AASRLNVVPL YASRIQALRY
LSIRWGIDLS KMVVFTGEKG DTDTEDLFAG LQKTLILKGS VEYGSEKLLR SEDNFKREDV
VPQDSPNIAF SESYEAHHIS QALEALGMN
//
