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
//