ID A0A059DI12_EUCGR Unreviewed; 528 AA.
AC A0A059DI12;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=sucrose-phosphate phosphatase {ECO:0000256|ARBA:ARBA00013112};
DE EC=3.1.3.24 {ECO:0000256|ARBA:ARBA00013112};
GN ORFNames=EUGRSUZ_A02547 {ECO:0000313|EMBL:KCW90408.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW90408.1};
RN [1] {ECO:0000313|EMBL:KCW90408.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW90408.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the final step of sucrose synthesis.
CC {ECO:0000256|ARBA:ARBA00003645}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sucrose 6(F)-phosphate = phosphate + sucrose;
CC Xref=Rhea:RHEA:19289, ChEBI:CHEBI:15377, ChEBI:CHEBI:17992,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57723; EC=3.1.3.24;
CC Evidence={ECO:0000256|ARBA:ARBA00000719};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Glycan biosynthesis; sucrose biosynthesis; sucrose from D-
CC fructose 6-phosphate and UDP-alpha-D-glucose: step 2/2.
CC {ECO:0000256|ARBA:ARBA00005070}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the sucrose phosphatase family.
CC {ECO:0000256|ARBA:ARBA00007211}.
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DR EMBL; KK198753; KCW90408.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059DI12; -.
DR STRING; 71139.A0A059DI12; -.
DR EnsemblPlants; KCW90408; KCW90408; EUGRSUZ_A02547.
DR Gramene; KCW90408; KCW90408; EUGRSUZ_A02547.
DR eggNOG; ENOG502QTVT; Eukaryota.
DR InParanoid; A0A059DI12; -.
DR OMA; RRGEMEN; -.
DR UniPathway; UPA00371; UER00546.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0050307; F:sucrose-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0005986; P:sucrose biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02605; HAD_SPP; 1.
DR Gene3D; 3.10.450.50; -; 1.
DR Gene3D; 3.90.1070.10; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR006380; SPP-like_dom.
DR InterPro; IPR013679; SPP_C.
DR InterPro; IPR012847; Sucrose_phosphatase_pln/cyn.
DR NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR NCBIfam; TIGR01482; SPP-subfamily; 1.
DR NCBIfam; TIGR01485; SPP_plant-cyano; 1.
DR PANTHER; PTHR46521; SUCROSE-PHOSPHATASE 2-RELATED; 1.
DR PANTHER; PTHR46521:SF4; SUCROSE-PHOSPHATASE 2-RELATED; 1.
DR Pfam; PF05116; S6PP; 1.
DR Pfam; PF08472; S6PP_C; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00043; sucrose-phosphatase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF54427; NTF2-like; 1.
PE 3: Inferred from homology;
FT DOMAIN 112..364
FT /note="Sucrose phosphatase-like"
FT /evidence="ECO:0000259|Pfam:PF05116"
FT DOMAIN 365..497
FT /note="Sucrose-phosphatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08472"
SQ SEQUENCE 528 AA; 58735 MW; 8F798720C25EDDBE CRC64;
MAFTCLARIL SKLSYRDTHW ATKGSDRVAE ISVRGPIASL HEQAPTNLDP ILLLLLLLLS
PLLSLRLIAG PQNLSLSLCL TPLSGASIGF IAQSHSPQVE PNTMERLSSS AKLMVVSDLD
HTMVDHHDHE NMSLLRFNAL WESSYRHDSL LVFSTGRSPT LYKQLRKEKP MLTPDITIMS
VGTEITYGNS MVPDSGWEEI LNQNWDRNIV KEEASKFPEL TLQSETEQRP HKVSFYVDKS
KAQDVTKKLS ELLTKQGLDV KIIYSGGMDL DILAQGAGKG QALAYLLKKF KAEGKLPTNT
LVCGDSGNDA ELFSIPDVYG VMVSNAQEEL LQWHAENAKD NPKIIHATER CASGIIQAIG
HFGLGPNTSA RDEADLSGCK KENLSPGGEV VRFYLLHEKW RRGEMENSES YITTLEAVCQ
PPGVFVHPSG VEQSFRECIS ALKGNHGDQQ GKQYRVWVDQ VFPTKIGSDT WLVKFQKWEM
HGEEQQSCLC SAVLVTKDAD GSDGWTWRHL HQTWSSVAGA KDHLSWLL
//