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Database: UniProt
Entry: A0A0D3B530_BRAOL
LinkDB: A0A0D3B530_BRAOL
Original site: A0A0D3B530_BRAOL 
ID   A0A0D3B530_BRAOL        Unreviewed;       424 AA.
AC   A0A0D3B530;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Sucrose-phosphatase {ECO:0000256|RuleBase:RU368007};
DE            EC=3.1.3.24 {ECO:0000256|RuleBase:RU368007};
GN   Name=106328025 {ECO:0000313|EnsemblPlants:Bo3g028580.1};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo3g028580.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo3g028580.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo3g028580.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the final step of sucrose synthesis.
CC       {ECO:0000256|ARBA:ARBA00003645, 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   RefSeq; XP_013621829.1; XM_013766375.1.
DR   RefSeq; XP_013621830.1; XM_013766376.1.
DR   AlphaFoldDB; A0A0D3B530; -.
DR   STRING; 109376.A0A0D3B530; -.
DR   EnsemblPlants; Bo3g028580.1; Bo3g028580.1; Bo3g028580.
DR   GeneID; 106328025; -.
DR   Gramene; Bo3g028580.1; Bo3g028580.1; Bo3g028580.
DR   KEGG; boe:106328025; -.
DR   eggNOG; ENOG502S8I4; Eukaryota.
DR   HOGENOM; CLU_030534_1_0_1; -.
DR   OMA; CTTAVKF; -.
DR   OrthoDB; 638885at2759; -.
DR   UniPathway; UPA00371; UER00546.
DR   Proteomes; UP000032141; Chromosome C3.
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   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; SFLDG01140; C2.B:_Phosphomannomutase_and_P; 1.
DR   SFLD; SFLDF00043; sucrose-phosphatase; 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:UP000032141}.
FT   DOMAIN          9..261
FT                   /note="Sucrose phosphatase-like"
FT                   /evidence="ECO:0000259|Pfam:PF05116"
FT   DOMAIN          262..395
FT                   /note="Sucrose-phosphatase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08472"
SQ   SEQUENCE   424 AA;  48017 MW;  7B277025E559A122 CRC64;
     MERLTSSARL MIVSDLDHTM VDHHDPENLS LLRFNSLWEH AYRRDSLLVF STGRSPTLYK
     ELRKEKPLLT PDVTIMSVGT EITYGNSMLP DHGWVDTLNN KWDLRVVKEE TGNFSELTLQ
     AETEQRPHKV SFYVDKSKAH QVTKELSQRL EKRGLDVKII YSGGMDLDIL PQGAGKGQAL
     AYLLKKLKSE GNLPVNTLAC GDSGNDAELF SVPDVYGVMV SNAQEELLKW HAENAKDNPK
     VIHAKERCAG GIIQAVGEFK LGPNLSPRDV SDFLECKADE NVNPGHEVVK FFLFYERWRR
     GEVENSEAYL ASLKASCLHD GVFVHPSGAE KSLVDTIDEL RKYHGDKQGK KFRVWVDQVL
     ATESAHGTWI VKLDKWEQSD DERRGCTTAV KFTAKEGEGL VWERVEQTWS EESKLKKDDS
     SWII
//
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