ID A0A0D3BMH1_BRAOL Unreviewed; 423 AA.
AC A0A0D3BMH1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Sucrose-phosphatase {ECO:0000256|RuleBase:RU368007};
DE EC=3.1.3.24 {ECO:0000256|RuleBase:RU368007};
GN Name=106328735 {ECO:0000313|EnsemblPlants:Bo3g179590.1};
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:Bo3g179590.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo3g179590.1, 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:Bo3g179590.1}
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_013622684.1; XM_013767230.1.
DR RefSeq; XP_013622685.1; XM_013767231.1.
DR AlphaFoldDB; A0A0D3BMH1; -.
DR STRING; 109376.A0A0D3BMH1; -.
DR EnsemblPlants; Bo3g179590.1; Bo3g179590.1; Bo3g179590.
DR GeneID; 106328735; -.
DR Gramene; Bo3g179590.1; Bo3g179590.1; Bo3g179590.
DR KEGG; boe:106328735; -.
DR eggNOG; ENOG502S8I4; Eukaryota.
DR HOGENOM; CLU_030534_1_0_1; -.
DR OMA; VENCDAY; -.
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:SF7; SUCROSE-PHOSPHATASE 1-RELATED; 1.
DR PANTHER; PTHR46521; 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;
KW Hydrolase {ECO:0000256|RuleBase:RU368007};
KW Magnesium {ECO:0000256|RuleBase:RU368007};
KW Reference proteome {ECO:0000313|Proteomes:UP000032141}.
FT DOMAIN 9..262
FT /note="Sucrose phosphatase-like"
FT /evidence="ECO:0000259|Pfam:PF05116"
FT DOMAIN 263..395
FT /note="Sucrose-phosphatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08472"
SQ SEQUENCE 423 AA; 48406 MW; DD165EA2E4797A7A CRC64;
MERLTSPPRL MIVSDLDDTM VDHHNDPENL SLLRFSSLWE EAFRHDSLLV FSTGRTLPMY
KKLRKERPML TPDVIITSVG TEIAYGKSMV TDDSWIEIMN HKWDRGIVEE ETSKFSELTL
QRDCDQRPNK VSFFIDKSKA QEVTKELYQR LEKRGLEIKI IFSGGKALDV LPKGGGKGQA
LAYLLNKLKA EGRLPVNTLV CGDSGNDTEL FTIPNVYGVM VRNSQAELLE WYAENAKDNA
KIIHASERCV GGILEAIGHF KLGPNLSPRD VSDLFECKED NVNPGHEVVM FFLFYERWRR
GEVENCDAYI ASLKASCHPA AVFVHPSGTE KSLIDTIDEL GKYHGDKKDK KFRVWTDQVL
ATETTHGTWM VKLDKWEQTG NERKCCTTTV RFTSKENEEL VWENVQQTWS EESEMKNDSN
WII
//
