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FN3KR_ORYSJ
ID   FN3KR_ORYSJ             Reviewed;         342 AA.
AC   Q10SM2; A0A0P0VS86;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
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   OrderedLocusNames=Os03g0117800, LOC_Os03g02640; ORFNames=OsJ_09183;
OS   Oryza sativa subsp. japonica (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=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
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).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [7]
RP   IDENTIFICATION.
RX   PubMed=15705060; DOI=10.1042/bj20041976;
RA   Fortpied J., Gemayel R., Stroobant V., van Schaftingen E.;
RT   "Plant ribulosamine/erythrulosamine 3-kinase, a putative protein-repair
RT   enzyme.";
RL   Biochem. J. 388:795-802(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; DP000009; ABF93664.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF10682.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS81991.1; -; Genomic_DNA.
DR   EMBL; CM000140; EAZ25366.1; -; Genomic_DNA.
DR   EMBL; AK066948; BAG90193.1; -; mRNA.
DR   RefSeq; XP_015628896.1; XM_015773410.1.
DR   AlphaFoldDB; Q10SM2; -.
DR   SMR; Q10SM2; -.
DR   STRING; 4530.OS03T0117800-01; -.
DR   PaxDb; Q10SM2; -.
DR   PRIDE; Q10SM2; -.
DR   EnsemblPlants; Os03t0117800-01; Os03t0117800-01; Os03g0117800.
DR   GeneID; 4331411; -.
DR   Gramene; Os03t0117800-01; Os03t0117800-01; Os03g0117800.
DR   KEGG; osa:4331411; -.
DR   eggNOG; KOG3021; Eukaryota.
DR   HOGENOM; CLU_036517_0_1_1; -.
DR   InParanoid; Q10SM2; -.
DR   OMA; GSFYSAY; -.
DR   OrthoDB; 943202at2759; -.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000007752; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   Genevisible; Q10SM2; OS.
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; IBA:GO_Central.
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   2: Evidence at transcript level;
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_0000413959"
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;  37820 MW;  BBE98E7927F5B36D CRC64;
     MANVALLSAA SPSTSSAAPR LRHVARRRPS RRSACPRSAA SRLSIMAALG EDPIRQWILT
     EGKATKITGV SSIGGGCINS AQCYKTDASS FFVKTNGRIG PSMFEGEALG LKAMYDTNSI
     RVPLPYKVGS LPTGGSFIIM EFIEFGCSRG DQSALGRKLA EMHKAAKSDK GYGFYVDNTI
     GSTPQINTWT ADWIEFYSKH RLGFQLELIT QRFGDSAIYD KGQRLIENMH PLFEGAVMEP
     CLLHGDLWSG NISSDTNGEP VILDPACYYG HNEAEFGMSW CAGFGGEFYS SYFEVMPKQP
     GFEKRRDLYL LYHYLNHYNL FGSGYRSSAM SIIDDYLRML KA
 
 
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