ID A0A498KBY9_MALDO Unreviewed; 481 AA.
AC A0A498KBY9;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Sucrose-phosphatase {ECO:0000256|RuleBase:RU368007};
DE EC=3.1.3.24 {ECO:0000256|RuleBase:RU368007};
GN ORFNames=DVH24_006295 {ECO:0000313|EMBL:RXI05038.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXI05038.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXI05038.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXI05038.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXI05038.1}.
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DR EMBL; RDQH01000328; RXI05038.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498KBY9; -.
DR STRING; 3750.A0A498KBY9; -.
DR UniPathway; UPA00371; UER00546.
DR Proteomes; UP000290289; Chromosome 2.
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; 2.
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; 2.
DR Pfam; PF08472; S6PP_C; 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:UP000290289}.
FT DOMAIN 10..166
FT /note="Sucrose phosphatase-like"
FT /evidence="ECO:0000259|Pfam:PF05116"
FT DOMAIN 180..292
FT /note="Sucrose phosphatase-like"
FT /evidence="ECO:0000259|Pfam:PF05116"
FT DOMAIN 293..425
FT /note="Sucrose-phosphatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08472"
SQ SEQUENCE 481 AA; 55331 MW; B67517BE5EE30A58 CRC64;
MNCRLNGPAR LMLVSDLDYT LVDHDAPDNL SLLKFNALWE SYYRHDSLLV FSTGRSPITY
KPLRNQKPLL TPDITIMSVG TEIMYGGGTD MIPDLGWQQF LSHRWDRAIV VEETNQFPQL
TPQAEGEQRP HKVSFYVDKV MAFEIMKVLS QRLEKRGLRF PRLFSFYEPF CYTPEHSQLQ
LKTKLLDVKI IYSSGIALDV LPKGAGKGKA LAYLLKKFKF EEKLPHNTLV CGDSGNDAEL
FSLPQVYGVM VSNAQEELLQ WYEENASDNP NMLHATERCA AGIIQALGHF HLGPNVSPRD
FKDFRKCKVE MSSPAHEVVK FFLFYERWRR AEVEKSEEYI QNLKPVFHSS GIFVHPSGVE
LPIHQCIDSL AGLHGDKQGK QFWTWVDRLS LVQIGSNAWL VKFNKWELCE NERQCCLTTV
LMSSKAEVPD AFTWLHMHQT WLDGLEIKEQ ERWDILKMSV GVEVEKIFIV PEMDGTPRVI
I
//
