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Entry: A0A2G5EF78_AQUCA
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ID   A0A2G5EF78_AQUCA        Unreviewed;       378 AA.
AC   A0A2G5EF78;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Sucrose-phosphatase {ECO:0000256|RuleBase:RU368007};
DE            EC=3.1.3.24 {ECO:0000256|RuleBase:RU368007};
GN   ORFNames=AQUCO_00900640v1 {ECO:0000313|EMBL:PIA54227.1};
OS   Aquilegia coerulea (Rocky mountain columbine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC   Aquilegia.
OX   NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA54227.1, ECO:0000313|Proteomes:UP000230069};
RN   [1] {ECO:0000313|EMBL:PIA54227.1, ECO:0000313|Proteomes:UP000230069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA   Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA   Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT   "WGS assembly of Aquilegia coerulea Goldsmith.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the final step of sucrose synthesis.
CC       {ECO:0000256|RuleBase:RU368007}.
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         ECO:0000256|RuleBase:RU368007};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|RuleBase:RU368007};
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, ECO:0000256|RuleBase:RU368007}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC       ECO:0000256|RuleBase:RU368007}.
CC   -!- SIMILARITY: Belongs to the sucrose phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00007211, ECO:0000256|RuleBase:RU368007}.
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DR   EMBL; KZ305026; PIA54227.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5EF78; -.
DR   UniPathway; UPA00371; UER00546.
DR   Proteomes; UP000230069; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050307; F:sucrose-phosphate phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005986; P:sucrose biosynthetic process; IEA:UniProtKB-UniRule.
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   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF54427; NTF2-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU368007};
KW   Magnesium {ECO:0000256|RuleBase:RU368007};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230069}.
FT   DOMAIN          2..215
FT                   /note="Sucrose phosphatase-like"
FT                   /evidence="ECO:0000259|Pfam:PF05116"
FT   DOMAIN          216..348
FT                   /note="Sucrose-phosphatase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08472"
SQ   SEQUENCE   378 AA;  42835 MW;  B5BA476DDF828429 CRC64;
     MLVFSTGRSC ISYKKLRKKK PLLTPDITVM SVGTEIAYGE EMIPDEGWVQ YLNHKWDRNI
     VLEETAKFPQ LKFQAESAQR PHKVSFFVGN DEAQEVIKVL PKRLENRGLD VKIIYSGGEA
     LDVLPQGAGK GQALAYLLKN LTSDGKQPVN TLVCGDSGND AELFSVPEVY GVMVSNAQEE
     LLQWHAENTI NNPKIIHASE RCAAGIIQAV GHFKLGVNKS PRDVMDISDD RIKTIHPSHE
     VVKFYMFYER WRRAEVENSE HYMQNLKEVS HLSGIFVHPS GVERPLHDCI DAMRMCYGDK
     QGIYFRVWVD RVSAAQIGSD AWLVKFDKWE SSEEGSNCCL VTALLSSKNA IPSGFTWVHV
     HQTWLTGYRV EDEQSWLF
//
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