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Database: UniProt
Entry: A0A2G5D1P4_AQUCA
LinkDB: A0A2G5D1P4_AQUCA
Original site: A0A2G5D1P4_AQUCA 
ID   A0A2G5D1P4_AQUCA        Unreviewed;       422 AA.
AC   A0A2G5D1P4;
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_00900639v1 {ECO:0000313|EMBL:PIA54222.1},
GN   AQUCO_03000188v1 {ECO:0000313|EMBL:PIA37435.1};
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:PIA37435.1, ECO:0000313|Proteomes:UP000230069};
RN   [1] {ECO:0000313|EMBL:PIA37435.1, 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; KZ305047; PIA37435.1; -; Genomic_DNA.
DR   EMBL; KZ305026; PIA54222.1; -; Genomic_DNA.
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   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:UP000230069}.
FT   DOMAIN          9..261
FT                   /note="Sucrose phosphatase-like"
FT                   /evidence="ECO:0000259|Pfam:PF05116"
FT   DOMAIN          262..392
FT                   /note="Sucrose-phosphatase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08472"
SQ   SEQUENCE   422 AA;  48222 MW;  FFD248AC66067758 CRC64;
     MDKFNGPARL MIVSDLDHTM VDHHDEENLS LLRFNALWEA YYRHNSLLVF STGRSFTLYK
     ELRKEKPLLT PDITIMSVGT EITYGEAMIP DDGWEQYLNQ KWDRNIVMEE TANFSQMKLQ
     AESEQRPHKV SFYVEKKKAQ EVTTALAERL QNRGLDVKII YSGGVDLDIL PQGAGKGQAL
     AYLLKKFTAE GKRPANTLVC GDSGNDAELF SIPEVYGVMV NNAQEELLQW YKENARDNPK
     IIHASKKCAA GIIEAIGHFK LGLNKSPRDV MDFSEDKIDN IHPGHEVVKF YMFYERWRRA
     EVENSEHYMQ NLKEHPSGTF VHPGGVERSL YECIDAMQKC YGDKQGKNFR LWVDRVSATQ
     IGSDAWLVKF DKWESSEEGR NCCLVTALLS SKSDVPSGFS WVHVHQTWLD GYAAADKSAW
     LF
//
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