PLR1_ARATH
ID PLR1_ARATH Reviewed; 365 AA.
AC Q56Y42; Q6NKP1; Q9FJC6;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Pyridoxal reductase, chloroplastic;
DE EC=1.1.1.65;
DE Flags: Precursor;
GN Name=PLR1; OrderedLocusNames=At5g53580; ORFNames=MNC6.12;
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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].
RA Cheuk R., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=21533842; DOI=10.1007/s11103-011-9777-x;
RA Herrero S., Gonzalez E., Gillikin J.W., Velez H., Daub M.E.;
RT "Identification and characterization of a pyridoxal reductase involved in
RT the vitamin B6 salvage pathway in Arabidopsis.";
RL Plant Mol. Biol. 76:157-169(2011).
CC -!- FUNCTION: Catalyzes the reduction of pyridoxal (PL) with NADPH and
CC oxidation of pyridoxine (PN) with NADP(+). Involved in the PLP salvage
CC pathway. {ECO:0000269|PubMed:21533842}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + pyridoxine = H(+) + NADPH + pyridoxal;
CC Xref=Rhea:RHEA:16129, ChEBI:CHEBI:15378, ChEBI:CHEBI:16709,
CC ChEBI:CHEBI:17310, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.65;
CC Evidence={ECO:0000269|PubMed:21533842};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6-7.5 for the reverse reaction.
CC {ECO:0000269|PubMed:21533842};
CC -!- PATHWAY: Cofactor degradation; B6 vitamer degradation; pyridoxal from
CC pyridoxine (dehydrogenase route): step 1/1.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, embryos, flowers, shoots,
CC roots and seeds. {ECO:0000269|PubMed:21533842}.
CC -!- MISCELLANEOUS: Mutants with reduced expression of PLR1 have lower
CC levels of total B6 vitamers but there is no reduction in PN or PNP
CC levels. {ECO:0000305|PubMed:21533842}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09734.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB015476; BAB09734.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96380.1; -; Genomic_DNA.
DR EMBL; BT012653; AAT06472.1; -; mRNA.
DR EMBL; AK221481; BAD94642.1; -; mRNA.
DR RefSeq; NP_200170.2; NM_124738.4.
DR AlphaFoldDB; Q56Y42; -.
DR SMR; Q56Y42; -.
DR STRING; 3702.AT5G53580.1; -.
DR PaxDb; Q56Y42; -.
DR PRIDE; Q56Y42; -.
DR ProteomicsDB; 236634; -.
DR EnsemblPlants; AT5G53580.1; AT5G53580.1; AT5G53580.
DR GeneID; 835440; -.
DR Gramene; AT5G53580.1; AT5G53580.1; AT5G53580.
DR KEGG; ath:AT5G53580; -.
DR Araport; AT5G53580; -.
DR TAIR; locus:2168601; AT5G53580.
DR eggNOG; KOG1575; Eukaryota.
DR HOGENOM; CLU_023205_2_3_1; -.
DR InParanoid; Q56Y42; -.
DR OMA; CGTWAWG; -.
DR OrthoDB; 1136766at2759; -.
DR PhylomeDB; Q56Y42; -.
DR BioCyc; ARA:AT5G53580-MON; -.
DR BioCyc; MetaCyc:MON-17899; -.
DR UniPathway; UPA00192; UER00307.
DR PRO; PR:Q56Y42; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q56Y42; baseline and differential.
DR Genevisible; Q56Y42; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IBA:GO_Central.
DR GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
DR GO; GO:0050236; F:pyridoxine:NADP 4-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IDA:UniProtKB.
DR GO; GO:0042821; P:pyridoxal biosynthetic process; IDA:UniProtKB.
DR GO; GO:0042820; P:vitamin B6 catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE 1: Evidence at protein level;
KW Chloroplast; NADP; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..15
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 16..365
FT /note="Pyridoxal reductase, chloroplastic"
FT /id="PRO_0000420551"
FT ACT_SITE 94
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CONFLICT 135
FT /note="W -> C (in Ref. 3; AAT06472)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 365 AA; 40576 MW; F2D313B8BF554DD8 CRC64;
MALTLSTTKT FTNINCSNNT SNITTFKPLK LPLFWPWQKV KMGPLSVSPM GFGTWAWGNQ
LLWGYQTSMD DQLQQAFELA LENGINLFDT ADSYGTGRLN GQSERLLGKF IKESQGLKGK
QNEVVVATKF AAYPWRLTSG QFVNACRASL DRLQIDQLGI GQLHWSTASY APLQELVLWD
GLVQMYEKGL VRAVGVSNYG PQQLVKIHDY LKTRGVPLCS AQVQFSLLSM GKEQLEIKSI
CDELGIRLIS YSPLGLGMLT GKYSSSKLPT GPRSLLFRQI LPGLEPLLLA LSEIAKKRGK
TMPQVAINWC ICKGTVPIPG IKSVRHVEDN LGALGWKLTN DEQLQLEYAA KESPKSMIQN
IFQTR
