PTALR_ARATH
ID PTALR_ARATH Reviewed; 242 AA.
AC Q9SY73; Q8LA87;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=NADPH-dependent pterin aldehyde reductase {ECO:0000303|PubMed:17550420};
DE EC=1.1.1.- {ECO:0000305|PubMed:17550420};
GN OrderedLocusNames=At1g10310 {ECO:0000312|Araport:AT1G10310};
GN ORFNames=F14N23.19 {ECO:0000312|EMBL:AAD32881.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. No-0;
RX PubMed=17550420; DOI=10.1111/j.1365-313x.2007.03143.x;
RA Noiriel A., Naponelli V., Bozzo G.G., Gregory J.F., Hanson A.D.;
RT "Folate salvage in plants: pterin aldehyde reduction is mediated by
RT multiple non-specific aldehyde reductases.";
RL Plant J. 51:378-389(2007).
RN [7]
RP FUNCTION.
RX PubMed=17220358; DOI=10.1104/pp.106.093633;
RA Noiriel A., Naponelli V., Gregory J.F., Hanson A.D.;
RT "Pterin and folate salvage. Plants and Escherichia coli lack capacity to
RT reduce oxidized pterins.";
RL Plant Physiol. 143:1101-1109(2007).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: NADPH-dependent pterin aldehyde reductase involved in pterin
CC aldehyde salvage during folate turnover. Catalyzes the reduction of
CC diverse aromatic and aliphatic aldehydes (e.g. acetaldehyde, n-
CC propanal, 1-naphthaldehyde, benzaldehyde, cinnamaldehyde, n-butanal, n-
CC hexanal, n-pentanal, 2-naphthaldehyde, n-octanal, n-nonanal and n-
CC heptanal), in addition to the conversion of pterin-6-aldehyde (PtCHO)
CC to 6-hydroxymethylpterin (PtCH(2)OH), and the conversion of
CC dihydropterin-6-aldehyde (H(2)PtCHO) to 6-hydroxymethyldihydropterin
CC (H(2)PtCH(2)OH) (PubMed:17550420). Cannot reduce the pterin ring
CC (PubMed:17220358). {ECO:0000269|PubMed:17550420,
CC ECO:0000305|PubMed:17220358}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=36 uM for pterin-6-aldehyde {ECO:0000269|PubMed:17550420};
CC KM=56 uM for dihydropterin-6-aldehyde {ECO:0000269|PubMed:17550420};
CC KM=1.9 uM for NADPH {ECO:0000269|PubMed:17550420};
CC KM=2.3 mM for NADH {ECO:0000269|PubMed:17550420};
CC Vmax=212 nmol/min/mg enzyme with pterin-6-aldehyde as substrate
CC {ECO:0000269|PubMed:17550420};
CC Vmax=343 nmol/min/mg enzyme with dihydropterin-6-aldehyde as
CC substrate {ECO:0000269|PubMed:17550420};
CC Note=Cold-active enzyme with an unusually high activity with
CC dihydropterin-6-aldehyde as substrate at 0 degrees Celsius.
CC {ECO:0000269|PubMed:17550420};
CC pH dependence:
CC Optimum pH is 7.5, with half-maximal activity at pH 6.0 and 8.3.
CC {ECO:0000269|PubMed:17550420};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17550420}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:17550420}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in seeds, and, to a lower extent,
CC in roots, leaves, flowers and siliques. {ECO:0000269|PubMed:17550420}.
CC -!- DISRUPTION PHENOTYPE: Slight reduction in seed pterin aldehyde
CC reductase activity, especially at low temperature.
CC {ECO:0000269|PubMed:17550420}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM65520.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC005489; AAD32881.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28564.1; -; Genomic_DNA.
DR EMBL; AK176670; BAD44433.1; -; mRNA.
DR EMBL; BT025789; ABF83679.1; -; mRNA.
DR EMBL; AY087973; AAM65520.1; ALT_INIT; mRNA.
DR PIR; C86237; C86237.
DR RefSeq; NP_563866.1; NM_100905.4.
DR AlphaFoldDB; Q9SY73; -.
DR SMR; Q9SY73; -.
DR STRING; 3702.AT1G10310.1; -.
DR iPTMnet; Q9SY73; -.
DR PaxDb; Q9SY73; -.
DR PRIDE; Q9SY73; -.
DR ProteomicsDB; 248845; -.
DR EnsemblPlants; AT1G10310.1; AT1G10310.1; AT1G10310.
DR GeneID; 837570; -.
DR Gramene; AT1G10310.1; AT1G10310.1; AT1G10310.
DR KEGG; ath:AT1G10310; -.
DR Araport; AT1G10310; -.
DR TAIR; locus:2012793; AT1G10310.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_2_10_1; -.
DR InParanoid; Q9SY73; -.
DR OMA; MAVTSMG; -.
DR OrthoDB; 1190834at2759; -.
DR PhylomeDB; Q9SY73; -.
DR BioCyc; ARA:AT1G10310-MON; -.
DR PRO; PR:Q9SY73; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SY73; baseline and differential.
DR Genevisible; Q9SY73; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:TAIR.
DR GO; GO:0006760; P:folic acid-containing compound metabolic process; IDA:TAIR.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; NADP; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..242
FT /note="NADPH-dependent pterin aldehyde reductase"
FT /id="PRO_0000431387"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 21..50
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4W1"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4W1"
FT BINDING 170
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4W1"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 242 AA; 25318 MW; BF48F371610040F1 CRC64;
MTMATPFSGA ANSIVAARTV LITGVSKGLG RALALELAKR GHTVIGCARS QEKLTALQSE
LSSSTNHLLL TADVKSNSSV EEMAHTIVEK KGVPDIIVNN AGTINKNSKI WEVSAEDFDN
VMDTNVKGVA NVLRHFIPLM LPRKQGIIVN MSSGWGRSGA ALVAPYCASK WAIEGLSRAV
AKEVVEGMAV VALNPGVINT ELLTSCFGNS ASLYQAPDAW AVKAATMILN LTAGDNGGSL
TV
