FN3KR_ORYSI
ID FN3KR_ORYSI Reviewed; 342 AA.
AC A2XBT1;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Protein-ribulosamine 3-kinase, chloroplastic {ECO:0000305};
DE EC=2.7.1.172 {ECO:0000250|UniProtKB:Q9LEW8};
DE AltName: Full=Fructosamine 3-kinase-related protein {ECO:0000250|UniProtKB:Q9LEW8};
DE Flags: Precursor;
GN ORFNames=OsI_09747;
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: Initiates a process leading to the deglycation of proteins.
CC Phosphorylates low-molecular-mass and protein-bound erythrulosamines
CC and ribulosamines, but not fructosamines or psicosamines, on the third
CC carbon of the sugar moiety. Protein-bound erythrulosamine 3-phosphates
CC and ribulosamine 3-phosphates are unstable and decompose under
CC physiological conditions. {ECO:0000250|UniProtKB:Q9LEW8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N(6)-D-ribulosyl-L-lysyl-[protein] = ADP + H(+) + N(6)-
CC (3-O-phospho-D-ribulosyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:48432,
CC Rhea:RHEA-COMP:12103, Rhea:RHEA-COMP:12104, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:90418, ChEBI:CHEBI:90420,
CC ChEBI:CHEBI:456216; EC=2.7.1.172;
CC Evidence={ECO:0000250|UniProtKB:Q9LEW8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48433;
CC Evidence={ECO:0000250|UniProtKB:Q9LEW8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N(6)-(D-erythrulosyl)-L-lysyl-[protein] = ADP + H(+) +
CC N(6)-(3-O-phospho-D-erythrulosyl)-L-lysyl-[protein];
CC Xref=Rhea:RHEA:61396, Rhea:RHEA-COMP:15794, Rhea:RHEA-COMP:15799,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:144587,
CC ChEBI:CHEBI:144624, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9LEW8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61397;
CC Evidence={ECO:0000250|UniProtKB:Q9LEW8};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the fructosamine kinase family. {ECO:0000305}.
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DR EMBL; CM000128; EAY88291.1; -; Genomic_DNA.
DR AlphaFoldDB; A2XBT1; -.
DR SMR; A2XBT1; -.
DR STRING; 39946.A2XBT1; -.
DR EnsemblPlants; BGIOSGA011722-TA; BGIOSGA011722-PA; BGIOSGA011722.
DR Gramene; BGIOSGA011722-TA; BGIOSGA011722-PA; BGIOSGA011722.
DR HOGENOM; CLU_036517_0_1_1; -.
DR OMA; GSFYSAY; -.
DR Proteomes; UP000007015; Chromosome 3.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0102193; F:protein-ribulosamine 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR016477; Fructo-/Ketosamine-3-kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR12149; PTHR12149; 1.
DR Pfam; PF03881; Fructosamin_kin; 1.
DR PIRSF; PIRSF006221; Ketosamine-3-kinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chloroplast; Kinase; Nucleotide-binding; Plastid;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..46
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 47..342
FT /note="Protein-ribulosamine 3-kinase, chloroplastic"
FT /id="PRO_0000413958"
FT ACT_SITE 246
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WI99"
FT BINDING 141..143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HA64"
SQ SEQUENCE 342 AA; 37791 MW; EB4F00D327FD9760 CRC64;
MANVALLSAA SPSTSSAAPR LRHVARRRPS RRSACPRSAA SRLSIMAALG EDPIRQWILT
EGKATKITGV SSIGGGCINS AQCYKTDAGS FFVKTNGRIG PSMFEGEALG LKAMYDTNSI
RVPLPYKVGS LPTGGSFIIM EFIEFGCSRG DQSALGRKLA EMHKAAKSDK GYGFYVDNTI
GSTPQINTWT ADWIEFYSKH RLGFQLELIT QRFGDSAIYD KGQRLIENMH PLFEGAVMEP
CLLHGDLWSG NISSDTDGEP VILDPACYYG HNEAEFGMSW CAGFGGEFYS SYFEVMPKQP
GFEKRRDLYL LYHYLNHYNL FGSGYRSSAM SIIDDYLRML KA
