FN3KR_ARATH
ID FN3KR_ARATH Reviewed; 326 AA.
AC Q9LEW8; Q8VYR1;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Protein-ribulosamine 3-kinase, chloroplastic {ECO:0000305};
DE EC=2.7.1.172 {ECO:0000269|PubMed:15705060};
DE AltName: Full=Fructosamine 3-kinase-related protein {ECO:0000303|PubMed:15705060};
DE Short=AtFN3K-RP {ECO:0000303|PubMed:15705060};
DE Flags: Precursor;
GN OrderedLocusNames=At3g61080; ORFNames=T27I15_170;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 (PubMed:15705060). Phosphorylates low-molecular-mass and protein-bound
CC erythrulosamines and ribulosamines, but not fructosamines or
CC psicosamines, on the third carbon of the sugar moiety
CC (PubMed:15705060). Protein-bound erythrulosamine 3-phosphates and
CC ribulosamine 3-phosphates are unstable and decompose under
CC physiological conditions (PubMed:15705060).
CC {ECO:0000269|PubMed:15705060}.
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:0000269|PubMed:15705060};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48433;
CC Evidence={ECO:0000269|PubMed:15705060};
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:0000269|PubMed:15705060};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61397;
CC Evidence={ECO:0000269|PubMed:15705060};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=135 uM for ribuloselysine {ECO:0000269|PubMed:15705060};
CC KM=25 uM for erythruloselysine {ECO:0000269|PubMed:15705060};
CC KM=274 uM for lysozyme glycated with ribose
CC {ECO:0000269|PubMed:15705060};
CC KM=104 uM for lysozyme glycated with erythrose
CC {ECO:0000269|PubMed:15705060};
CC Vmax=685 umol/min/g enzyme with ribuloselysine as substrate
CC {ECO:0000269|PubMed:15705060};
CC Vmax=749 umol/min/g enzyme with erythruloselysine as substrate
CC {ECO:0000269|PubMed:15705060};
CC Vmax=43 umol/min/g enzyme with lysozyme glycated with ribose as
CC substrate {ECO:0000269|PubMed:15705060};
CC Vmax=20 umol/min/g enzyme with lysozyme glycated with erythros as
CC substrate {ECO:0000269|PubMed:15705060};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the fructosamine kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB94144.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL358732; CAB94144.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80151.1; -; Genomic_DNA.
DR EMBL; AY070080; AAL49775.1; -; mRNA.
DR EMBL; AY117356; AAM51431.1; -; mRNA.
DR PIR; T50529; T50529.
DR RefSeq; NP_191667.2; NM_115972.4.
DR PDB; 6OID; X-ray; 2.37 A; A/B=30-326.
DR PDBsum; 6OID; -.
DR AlphaFoldDB; Q9LEW8; -.
DR SMR; Q9LEW8; -.
DR BioGRID; 10594; 1.
DR STRING; 3702.AT3G61080.1; -.
DR PaxDb; Q9LEW8; -.
DR PRIDE; Q9LEW8; -.
DR ProteomicsDB; 230590; -.
DR EnsemblPlants; AT3G61080.1; AT3G61080.1; AT3G61080.
DR GeneID; 825280; -.
DR Gramene; AT3G61080.1; AT3G61080.1; AT3G61080.
DR KEGG; ath:AT3G61080; -.
DR Araport; AT3G61080; -.
DR TAIR; locus:2101022; AT3G61080.
DR eggNOG; KOG3021; Eukaryota.
DR HOGENOM; CLU_036517_0_1_1; -.
DR InParanoid; Q9LEW8; -.
DR OMA; GSFYSAY; -.
DR PhylomeDB; Q9LEW8; -.
DR PRO; PR:Q9LEW8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LEW8; baseline and differential.
DR Genevisible; Q9LEW8; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; TAS:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA:TAIR.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chloroplast; Kinase; Nucleotide-binding;
KW Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..30
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 31..326
FT /note="Protein-ribulosamine 3-kinase, chloroplastic"
FT /id="PRO_0000216341"
FT ACT_SITE 230
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WI99"
FT BINDING 125..127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HA64"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:6OID"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:6OID"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:6OID"
FT STRAND 73..83
FT /evidence="ECO:0007829|PDB:6OID"
FT HELIX 86..100
FT /evidence="ECO:0007829|PDB:6OID"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:6OID"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:6OID"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:6OID"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:6OID"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:6OID"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:6OID"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:6OID"
FT HELIX 186..197
FT /evidence="ECO:0007829|PDB:6OID"
FT HELIX 200..211
FT /evidence="ECO:0007829|PDB:6OID"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:6OID"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6OID"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:6OID"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:6OID"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:6OID"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:6OID"
FT HELIX 256..260
FT /evidence="ECO:0007829|PDB:6OID"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:6OID"
FT HELIX 270..279
FT /evidence="ECO:0007829|PDB:6OID"
FT TURN 284..289
FT /evidence="ECO:0007829|PDB:6OID"
FT HELIX 290..305
FT /evidence="ECO:0007829|PDB:6OID"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:6OID"
FT HELIX 310..323
FT /evidence="ECO:0007829|PDB:6OID"
SQ SEQUENCE 326 AA; 36471 MW; AA9B5DC696DCFDA0 CRC64;
MAVASLSICF SARPHLLLRN FSPRPKFVAM AAMSEDPIRE WILTEGKATQ ITKIGSVGGG
CINLASHYQT DAGSFFVKTN RSIGPAMFEG EALGLEAMYE TRTIRVPNPH KAGELPTGGS
YIIMEFIDFG GSRGNQAELG RKLAEMHKAG KTSKGFGFEV DNTIGSTPQI NTWSSDWIEF
YGEKRLGYQL KLARDQYGDS AIYQKGHTLI QNMAPLFENV VIEPCLLHGD LWSGNIAYDK
NNEPVILDPA CYYGHNEADF GMSWCAGFGE SFYNAYFKVM PKQAGYEKRR DLYLLYHYLN
HYNLFGSGYR SSAMSIIDDY LRMLKA
