NADO1_ORYSJ
ID NADO1_ORYSJ Reviewed; 321 AA.
AC Q7G764; Q0IZA8; Q94LH9;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Probable NAD(P)H-dependent oxidoreductase 1;
DE EC=1.1.1.-;
GN OrderedLocusNames=Os10g0113000, LOC_Os10g02380;
GN ORFNames=OJ1014H12.13, OSJNBb0012A20.18;
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=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
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 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 [6]
RP PROTEIN SEQUENCE OF 12-21; 68-76; 153-162 AND 237-256, FUNCTION, INDUCTION,
RP AND TISSUE SPECIFICITY.
RX PubMed=15086826; DOI=10.1111/j.0031-9317.2004.00299.x;
RA Oguchi K., Tanaka N., Komatsu S., Akao S.;
RT "Characterization of NADPH-dependent oxidoreductase induced by auxin in
RT rice.";
RL Physiol. Plantarum 121:124-131(2004).
CC -!- FUNCTION: May play a role in auxin-induced cell growth by generating
CC hydroxyl radicals, which tends to increase cell wall loosening.
CC {ECO:0000269|PubMed:15086826}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and leaf sheaths.
CC {ECO:0000269|PubMed:15086826}.
CC -!- INDUCTION: By auxin and gibberellic acid.
CC {ECO:0000269|PubMed:15086826}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; AC079685; AAK52587.1; -; Genomic_DNA.
DR EMBL; AC098694; AAM44874.1; -; Genomic_DNA.
DR EMBL; DP000086; AAP51850.1; -; Genomic_DNA.
DR EMBL; AP008216; BAF25957.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT09643.1; -; Genomic_DNA.
DR EMBL; AK061106; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK102609; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015613878.1; XM_015758392.1.
DR AlphaFoldDB; Q7G764; -.
DR SMR; Q7G764; -.
DR STRING; 4530.OS10T0113000-01; -.
DR PaxDb; Q7G764; -.
DR PRIDE; Q7G764; -.
DR EnsemblPlants; Os10t0113000-01; Os10t0113000-01; Os10g0113000.
DR GeneID; 4347977; -.
DR Gramene; Os10t0113000-01; Os10t0113000-01; Os10g0113000.
DR KEGG; osa:4347977; -.
DR eggNOG; KOG1577; Eukaryota.
DR HOGENOM; CLU_023205_0_0_1; -.
DR OMA; IYAPVCW; -.
DR OrthoDB; 1016440at2759; -.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR ExpressionAtlas; Q7G764; baseline and differential.
DR Genevisible; Q7G764; OS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR CDD; cd19124; AKR_AKR4A_4B; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044497; AKR4A/B.
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 PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..321
FT /note="Probable NAD(P)H-dependent oxidoreductase 1"
FT /id="PRO_0000124655"
FT ACT_SITE 55
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 214..273
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 85
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
SQ SEQUENCE 321 AA; 35713 MW; 2B7906FED1FFCC34 CRC64;
MATIPEVPAS ELIQTMPRVG MGTAAFPFTS SEDTTAAMLR AIELGYRHFD TARIYATEGC
VGEAVAEAVR RGLIASRADV FVTSKIWCSD LHAGRVVPAA RETLRNLGMD YVDLLLVHWP
VSLTPGNYDF PFPKEVILPS FDMEGVWRGM EECHRLGLAR AIGVSNFSAK KLEQLLSLAA
VRPAVNQVEV NPMWQQRTLR EVCRREGVQL CGYSPLGAKG TPWGSAAVMD SGVLQEIAGA
KGKTLAQICL RWLYEQGDVL LVKTYNEKRM KENLDIFNWE LTDEERERIS QLPQLRGLPG
LEFISDHGPY KSVEDLWDGD V