ID A0A251K004_MANES Unreviewed; 424 AA.
AC A0A251K004;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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=MANES_10G071200 {ECO:0000313|EMBL:OAY39151.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY39151.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY39151.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY39151.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) 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; CM004396; OAY39150.1; -; Genomic_DNA.
DR EMBL; CM004396; OAY39151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251K004; -.
DR STRING; 3983.A0A251K004; -.
DR EnsemblPlants; OAY39150; OAY39150; MANES_10G071200.
DR EnsemblPlants; OAY39151; OAY39151; MANES_10G071200.
DR Gramene; OAY39150; OAY39150; MANES_10G071200.
DR Gramene; OAY39151; OAY39151; MANES_10G071200.
DR UniPathway; UPA00371; UER00546.
DR Proteomes; UP000091857; Chromosome lg10.
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; SFLDG01141; C2.B.1:_Sucrose_Phosphatase_Li; 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:UP000091857}.
FT DOMAIN 9..261
FT /note="Sucrose phosphatase-like"
FT /evidence="ECO:0000259|Pfam:PF05116"
FT DOMAIN 262..394
FT /note="Sucrose-phosphatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08472"
SQ SEQUENCE 424 AA; 48367 MW; 8C93094CCDB12127 CRC64;
MDRLSGSASL MIVSDLDFTM VDHLDQENLS LLRFNALWEA YYRQNSLLVF STGRSPTIYK
QLKNEKPLLT PDIAIMSVGT EIMYGESMIR DDDWEKYLNH KWNKEIVLEE TAKFPDLTPQ
AETEQRPHKV SFFVETIKAL EIIKTLRELL ENRGLDVKVI YSNAKALDIL PKRADKGQAL
SYLLKKFIAN GKVPISTLVC GDSGNDAELF SIPEVYGVMV SNAQEELLQW HAGNAKNNSK
IIHATERCAS GIIQAIGSFR LGPNVSPRDI KDIQTCKGEI FGPTHEVVKF YLFYERWRNA
EVEKSIEYMK ILRLVLFPLG TFVHPSGVEQ SVEHCIEAMT RLYGDKQGKQ YRVWLDQVSA
AQVGSDTWLV KFYKWELSGA ERHCCLTTAL LSSKAKVPDG FTWMHMHQTW LDGSAPEKQT
TWLF
//
