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Database: UniProt
Entry: A0A1J6I8F8_NICAT
LinkDB: A0A1J6I8F8_NICAT
Original site: A0A1J6I8F8_NICAT 
ID   A0A1J6I8F8_NICAT        Unreviewed;      1054 AA.
AC   A0A1J6I8F8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 33.
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   Name=SPS {ECO:0000313|EMBL:OIS96831.1};
GN   ORFNames=A4A49_27050 {ECO:0000313|EMBL:OIS96831.1};
OS   Nicotiana attenuata (Coyote tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=49451 {ECO:0000313|EMBL:OIS96831.1, ECO:0000313|Proteomes:UP000187609};
RN   [1] {ECO:0000313|EMBL:OIS96831.1, ECO:0000313|Proteomes:UP000187609}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. UT {ECO:0000313|Proteomes:UP000187609};
RC   TISSUE=Leaves {ECO:0000313|EMBL:OIS96831.1};
RA   Xu S., Brockmoeller T., Gaquerel E., Navarro A., Kuhl H., Gase K., Ling Z.,
RA   Zhou W., Kreitzer C., Stanke M., Tang H., Lyons E., Pandey P., Pandey S.P.,
RA   Timmermann B., Baldwin I.T.;
RT   "The genome of Nicotiana attenuata.";
RL   Submitted (NOV-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:OIS96831.1}.
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DR   EMBL; MJEQ01037193; OIS96831.1; -; Genomic_DNA.
DR   RefSeq; XP_019255648.1; XM_019400103.1.
DR   AlphaFoldDB; A0A1J6I8F8; -.
DR   STRING; 49451.A0A1J6I8F8; -.
DR   EnsemblPlants; OIS96831; OIS96831; A4A49_27050.
DR   GeneID; 109234218; -.
DR   Gramene; OIS96831; OIS96831; A4A49_27050.
DR   KEGG; nau:109234218; -.
DR   OMA; AWSKGIS; -.
DR   OrthoDB; 1206157at2759; -.
DR   UniPathway; UPA00371; UER00545.
DR   Proteomes; UP000187609; Chromosome 11.
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: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:UP000187609};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368006}.
FT   DOMAIN          167..434
FT                   /note="Sucrose synthase"
FT                   /evidence="ECO:0000259|Pfam:PF00862"
FT   DOMAIN          470..643
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   DOMAIN          774..988
FT                   /note="Sucrose phosphatase-like"
FT                   /evidence="ECO:0000259|Pfam:PF05116"
FT   REGION          101..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          673..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..133
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1054 AA;  118610 MW;  E85EED8CACB2DEB4 CRC64;
     MAGNDWINSY LEAILDVGPG LDDKKSSLLL RERGRFSPTR YFVEEVITGF DETDLHRSWV
     RAQATRSPQE RNTRLENMCW RIWNLARQKK QLEGEQAQWM AKRRQEREKG RREAVADMSE
     DLSEGEKGDV VSDIPSHAES AKGRLPRISS VETMEAWVNQ QKGKKLYIVL ISLHGLIRGE
     NMELGRDSDT GGQVKYVVEL ARALGSMPGV YRVDLLTRQV SSPEVDWSYG EPTEMLPPRS
     TEGLMTEMGE SSGAYIIRIP FGPREKYIPK EQLWPYIPEF VDGALNHIIQ MSKVLGEQIG
     NGYPVWPVAI HGHYADAGDS AALLSGALNV PMLFTGHSLG RDKLDQLLRQ GRLSKDEINS
     TYKIMRRIEA EELTLDASEI VITSTRQEID EQWRLYDGFD PILERKLRAR IKRNVSCYGR
     FMPRMAVIPP GMEFHHIVPH EGDMDGETEG TEDGKAPDPP IWTEIMRFFS NPRKPMILAL
     ARPDPKKNLT TLVKAFGECR PLRELANLML IMGNRDNIDE MSSTNSSVLL SILKMIDKYD
     LYGQVAYPKH HKQADVPDIY RLAAKTKGVF INPAFIEPFG LTLIEAAAYG LPMVATKNGG
     PVDIHRVLDN GLLVDPHDQQ AIADALLKLV ADKHLWAKCR ANGLKNIHLF SWPEHCKTYL
     SRIASCKPRQ PRWLRADDDD DENSETDSPS DSLRDIHDIS LNLRFSLDGE KNDNKENADN
     TLDPEVRKSK LENAVLSWSK GVLKSTPKAW SSDKGDQNSG AGKFPAIRRR RHIFVIAVDC
     DASSGLSESV RKIFEAVEKE RAEGSIGFIL ASSFNISEVQ SFLGSEGMKP TDFDAYICNS
     GGDLYYSSFH SEQNPFVVDL YYHSHIEYRW GGEGLRKTLV RWAASSIDKK GENEDHIVVE
     DEDNSADYCY TFKVRKLGTV PPAKELRKLM RIQALRCHVV YCQNGSRINV IPVLASRSQA
     LRYLYLRWGM DLSKLVVFVG ESGDTDYEGL IGGLRKAVIM KGLCTSASSL IHGNRNYPLS
     DVLPFDSPNV VQAAEECSST EIRSSLEKLG VLKG
//
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