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Database: UniProt
Entry: R0H495_9BRAS
LinkDB: R0H495_9BRAS
Original site: R0H495_9BRAS 
ID   R0H495_9BRAS            Unreviewed;       424 AA.
AC   R0H495;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Sucrose-phosphatase {ECO:0000256|RuleBase:RU368007};
DE            EC=3.1.3.24 {ECO:0000256|RuleBase:RU368007};
GN   ORFNames=CARUB_v10017320mg {ECO:0000313|EMBL:EOA24089.1};
OS   Capsella rubella.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX   NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA24089.1, ECO:0000313|Proteomes:UP000029121};
RN   [1] {ECO:0000313|Proteomes:UP000029121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX   PubMed=23749190; DOI=10.1038/ng.2669;
RA   Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA   Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA   Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA   Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA   Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA   Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT   "The Capsella rubella genome and the genomic consequences of rapid mating
RT   system evolution.";
RL   Nat. Genet. 45:831-835(2013).
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; KB870809; EOA24089.1; -; Genomic_DNA.
DR   RefSeq; XP_006291191.1; XM_006291129.1.
DR   AlphaFoldDB; R0H495; -.
DR   STRING; 81985.R0H495; -.
DR   GeneID; 17885460; -.
DR   KEGG; crb:17885460; -.
DR   OrthoDB; 638885at2759; -.
DR   UniPathway; UPA00371; UER00546.
DR   Proteomes; UP000029121; 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:SF13; SUCROSE-PHOSPHATASE 3B-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:UP000029121}.
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   424 AA;  48842 MW;  B1904B51E25FB10B CRC64;
     MERLVSHPPL MIVSDLDHTM VDHQDHENLS LLRFNSLWED AYRRDSLLVF STARSPILYK
     ELRKEKPLLT PDIIITSIGT EIAFGNSMVP DHAWVETLNS DKWNREIVLE ETKKFPELTL
     QPKTEQRLHK VSFYIDEGKG EALTKELSQL LEKRGLDVKI IYSWGKNVDV IPRGAGKGEA
     LEYLLKKLQG EGIFPVNTLA CGDSEHDAEL FSIPDVHGVM VSNSQEELLK WRSENALHNP
     KVIHSTERCA DGIIQAIGHF KLGPHISPRD VSEYLNRKTD ISNPGQEVVR FYLFYERLRR
     GEIKNYETYI ASFKESCLQA AIFFHPSGAE KSLRDTIDEL SNCHGDKRGK KFWVWVDQVL
     VMDTTPGKWT VKFNKWEQCD DERECCTTTI EFTSKGGDLE WEKVEQIWSE ESDVKDDDNS
     SWIL
//
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