ID A0A2T7D5Z2_9POAL Unreviewed; 1061 AA.
AC A0A2T7D5Z2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-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=GQ55_6G127700 {ECO:0000313|EMBL:PUZ51007.1};
OS Panicum hallii var. hallii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC Panicum sect. Panicum.
OX NCBI_TaxID=1504633 {ECO:0000313|EMBL:PUZ51007.1, ECO:0000313|Proteomes:UP000244336};
RN [1] {ECO:0000313|EMBL:PUZ51007.1, ECO:0000313|Proteomes:UP000244336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HAL2 {ECO:0000313|Proteomes:UP000244336};
RA Lovell J., Jenkins J., Lowry D., Mamidi S., Sreedasyam A., Weng X.,
RA Barry K., Bonette J., Campitelli B., Daum C., Gordon S., Gould B.,
RA Lipzen A., MacQueen A., Palacio-Mejia J., Plott C., Shakirov E., Shu S.,
RA Yoshinaga Y., Zane M., Rokhsar D., Grimwood J., Schmutz J., Juenger T.;
RT "WGS assembly of Panicum hallii var. hallii HAL2.";
RL Submitted (APR-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}.
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DR EMBL; CM009754; PUZ51007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7D5Z2; -.
DR STRING; 1504633.A0A2T7D5Z2; -.
DR EnsemblPlants; PUZ51007; PUZ51007; GQ55_6G127700.
DR Gramene; PUZ51007; PUZ51007; GQ55_6G127700.
DR UniPathway; UPA00371; UER00545.
DR Proteomes; UP000244336; Chromosome 6.
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; cd16419; HAD_SPS; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR001296; Glyco_trans_1.
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:UP000244336};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368006}.
FT DOMAIN 187..452
FT /note="Sucrose synthase"
FT /evidence="ECO:0000259|Pfam:PF00862"
FT DOMAIN 489..662
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT DOMAIN 902..1006
FT /note="Sucrose phosphatase-like"
FT /evidence="ECO:0000259|Pfam:PF05116"
FT REGION 135..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1061 AA; 118369 MW; C35EE453BDB2D520 CRC64;
MAGNDWINSY LEAILDAGGA AGEISAAAGG GGGIEGASGE KRDKSSLMLR ERGRFSPARY
FVEEVISGFD ETDLYKTWVR TSAMRSPQER NTRLENMSWR IWNLARKKKQ IEGEEASRLS
KQRLEREKAR QYAAADFSED LSEGEKGENS NEPSIHDERT RTRMPRIGST DAIEAWASQH
KDKKLYIVLI SIHGLIRGEN MELGRDSDTG GQVKYVVELA RALGSTPGVY RVDLLTRQIS
APDVDWSYGE PTEMLSPICS ENFGHEMGES SGAYIVRIPF GPRDKYIPKE HLWPYIQEFV
DGALVHIVQM SKVLGEQVGS GQPVWPVVIH GHYADAGDST ALLSGALNVP MVFTGHSLGR
DKLEQILKQG RQTRDEINAT YKIMRRIEAE ELCLDASEII ITSTRQEIEQ QWGLYDGFDL
TMARKLRARI KRGVSCFGRY MPRMIAIPPG MEFSHIAPHD VDLDGEEGNE DGSASPDPPI
WADIMRFFSN PRKPMILALA RPDPKKNITT LVKAFGEHRE LRNLANLTLI MGNRDVIDEM
SSTNAAVLTS VLKLIDKYDL YGQVAYPKHH KQSEVPDIYR LAARTKGVFI NCAFIEPFGL
TLIEAAAYGL PMVATRNGGP VDIHRVLDNG ILVDPHNQNE IAEALYKLVS DKHLWAQCRQ
NGLENIHQFS WPEHCKNYLS RVGTLKPRHP RWQKSNDATE ISEADSPEDS LRDIHDISLN
LKLSLDSEKS GSKDGNSNTV RRHLEDAVQK LSRDVSDSRM EVLSENGRWP SLRGRKQIIV
IAVDSVQDAD FVQVIKNIFE ASSNGRLSGS VGFILSTSKA ISEIHALLIS GGIETSDFDA
FICNSGSDLC YPSSSSEDML SPAELPFMID LDYHSQIEYR WGGEGLRKTL IRWAAEKNNE
SGQNVIVEDE ECSSTYCISF KVMNTEAASP VKEIRRTMRI QALRCHVLYS HDGSKLNVIP
VLASRSQALR YLYIRWGFDL SNMTVVVGES GDTDYEVLIG GVHKTIILKG SFNAVPNQVH
TARSYSLQDV VSFEKPGIAS VEGYGPDNLK SALQQFGILK D
//
