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Database: UniProt
Entry: I1NED5_SOYBN
LinkDB: I1NED5_SOYBN
Original site: I1NED5_SOYBN 
ID   I1NED5_SOYBN            Unreviewed;       372 AA.
AC   I1NED5;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Sucrose-phosphatase {ECO:0000256|RuleBase:RU368007};
DE            EC=3.1.3.24 {ECO:0000256|RuleBase:RU368007};
GN   Name=100796915 {ECO:0000313|EnsemblPlants:KRG90144};
GN   ORFNames=GLYMA_20G070500 {ECO:0000313|EMBL:KRG90144.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRG90144};
RN   [1] {ECO:0000313|EMBL:KRG90144.1, ECO:0000313|EnsemblPlants:KRG90144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRG90144};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRG90144.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRG90144}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRG90144};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRG90144.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRG90144.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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   EMBL; CM000853; KRG90144.1; -; Genomic_DNA.
DR   RefSeq; XP_014627725.1; XM_014772239.1.
DR   AlphaFoldDB; I1NED5; -.
DR   EnsemblPlants; KRG90144; KRG90144; GLYMA_20G070500.
DR   Gramene; KRG90144; KRG90144; GLYMA_20G070500.
DR   HOGENOM; CLU_030534_1_0_1; -.
DR   OMA; MIDHQDR; -.
DR   OrthoDB; 276235at2759; -.
DR   UniPathway; UPA00371; UER00546.
DR   Proteomes; UP000008827; Chromosome 20.
DR   ExpressionAtlas; I1NED5; baseline and differential.
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:SF8; SUCROSE-PHOSPHATASE 3A-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:UP000008827}.
FT   DOMAIN          9..261
FT                   /note="Sucrose phosphatase-like"
FT                   /evidence="ECO:0000259|Pfam:PF05116"
FT   DOMAIN          262..364
FT                   /note="Sucrose-phosphatase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08472"
SQ   SEQUENCE   372 AA;  41905 MW;  C95A1CEED6248FD2 CRC64;
     MDRLNGSANL MIVSDLDFTM VDHDDPENLA LLRFNALWEA YYRHNSLLVF STGRSPTIYG
     ELRKQKPLLT PDITIMSVGT EITYGESMVP DDGWKQYLDH KWNRDIVMEE TAKFPELTLQ
     SETEQRPHKV SFYLEKGKAP NVTQTLSKRL ENRGLDVKII YSNGIALDVL PQAAGKGQAL
     AFLLEKLKAD EQGPINTLVC GDSGNDAELF TVPEVNGVLV SNAQEELLQW YAENARGNPR
     IIHATERCAA AIVQAIGNFS LGPNVSPRDI GDLMSNRKVH SPSHEVVMFY IFYERWRRGE
     VENPEQYIQK LKSVFHSTGN FVHPSGIDQP MHQTIDTLAK AFGDKTGKDF RVWVDCISLA
     EVMSHGVVQQ RL
//
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