NIA1_ORYSJ
ID NIA1_ORYSJ Reviewed; 916 AA.
AC P16081; A0A0P0XHA0; Q0J545; Q6ZC37;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Nitrate reductase [NADH] 1;
DE Short=NR1;
DE EC=1.7.1.1;
GN Name=NIA1;
GN OrderedLocusNames=Os08g0468100 {ECO:0000312|EMBL:BAF23920.1},
GN LOC_Os08g36480 {ECO:0000305};
GN ORFNames=OsJ_27622 {ECO:0000312|EMBL:EAZ43035.1}, P0470B03.25;
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 [GENOMIC DNA].
RC STRAIN=cv. Biggs M-201;
RX PubMed=2491689; DOI=10.1007/bf00016030;
RA Cheng C., Dewdney J., Nam H., den Boer B.G.W., Goodman H.M., Choi H.K.,
RA Kleinhofs A., An G.;
RT "Nucleotide sequence of rice nitrate reductase genes.";
RL Plant Mol. Biol. 13:731-733(1989).
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).
CC -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first step
CC of nitrate assimilation in plants, fungi and bacteria.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + nitrite = H(+) + NADH + nitrate;
CC Xref=Rhea:RHEA:17913, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.7.1.1;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=Binds 1 heme group per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000250};
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the nitrate reductase family. {ECO:0000305}.
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DR EMBL; X15819; CAA33817.2; -; Genomic_DNA.
DR EMBL; X15820; CAA33817.2; JOINED; Genomic_DNA.
DR EMBL; AP004585; BAD09558.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF23920.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT05814.1; -; Genomic_DNA.
DR EMBL; CM000145; EAZ43035.1; -; Genomic_DNA.
DR EMBL; AK121810; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S07554; S07554.
DR RefSeq; XP_015650300.1; XM_015794814.1.
DR AlphaFoldDB; P16081; -.
DR SMR; P16081; -.
DR STRING; 4530.OS08T0468100-01; -.
DR iPTMnet; P16081; -.
DR PaxDb; P16081; -.
DR PRIDE; P16081; -.
DR EnsemblPlants; Os08t0468100-01; Os08t0468100-01; Os08g0468100.
DR GeneID; 4345795; -.
DR Gramene; Os08t0468100-01; Os08t0468100-01; Os08g0468100.
DR KEGG; osa:4345795; -.
DR eggNOG; KOG0534; Eukaryota.
DR eggNOG; KOG0535; Eukaryota.
DR eggNOG; KOG0537; Eukaryota.
DR InParanoid; P16081; -.
DR OMA; ITPGYQL; -.
DR OrthoDB; 166846at2759; -.
DR PlantReactome; R-OSA-1119291; Nitrate assimilation.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000007752; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR ExpressionAtlas; P16081; baseline and differential.
DR Genevisible; P16081; OS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR GO; GO:0031984; C:organelle subcompartment; IEA:UniProt.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; ISS:UniProtKB.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0009703; F:nitrate reductase (NADH) activity; IBA:GO_Central.
DR GO; GO:0050464; F:nitrate reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0042128; P:nitrate assimilation; IBA:GO_Central.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.10.120.10; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR Gene3D; 3.90.420.10; -; 1.
DR InterPro; IPR001834; CBR-like.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR005066; MoCF_OxRdtse_dimer.
DR InterPro; IPR008335; Mopterin_OxRdtase_euk.
DR InterPro; IPR012137; Nitr_rd_NADH.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
DR InterPro; IPR036374; OxRdtase_Mopterin-bd_sf.
DR InterPro; IPR022407; OxRdtase_Mopterin_BS.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19370; PTHR19370; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF03404; Mo-co_dimer; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF00174; Oxidored_molyb; 1.
DR PIRSF; PIRSF000233; Nitr_rd_NADH; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR PRINTS; PR00407; EUMOPTERIN.
DR PRINTS; PR00371; FPNCR.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR SUPFAM; SSF56524; SSF56524; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; FAD; Flavoprotein; Heme; Iron; Metal-binding; Molybdenum;
KW NAD; Nitrate assimilation; Oxidoreductase; Reference proteome.
FT CHAIN 1..916
FT /note="Nitrate reductase [NADH] 1"
FT /id="PRO_0000166065"
FT DOMAIN 541..616
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT DOMAIN 656..768
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 192
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250|UniProtKB:P49050"
FT BINDING 576
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 599
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 708..711
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 725..729
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 730
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17571"
FT BINDING 737
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 742..744
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 792
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17571"
FT BINDING 795
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT DISULFID 431
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT CONFLICT 98
FT /note="D -> N (in Ref. 1; CAA33817)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="I -> T (in Ref. 1; CAA33817)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="R -> E (in Ref. 1; CAA33817)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="R -> A (in Ref. 1; CAA33817)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="R -> G (in Ref. 6; AK121810)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="H -> Y (in Ref. 1; CAA33817)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="C -> R (in Ref. 1; CAA33817)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="S -> P (in Ref. 1; CAA33817)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="L -> F (in Ref. 1; CAA33817)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="V -> A (in Ref. 1; CAA33817)"
FT /evidence="ECO:0000305"
FT CONFLICT 581
FT /note="D -> N (in Ref. 6; AK121810)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 916 AA; 101513 MW; 844D2A0D537E629D CRC64;
MAASVQPRQF GHLEPGSAPV RGAASSNGAK AYPPANGIPR RADSPVRGCG FPPLVSPPPR
KPPSDGSDDE EEEQEDWREL YGSHLQLEVE PPVRDARDEG TADAWIERNP SLIRLTGKHP
LNCEPPLARL MHHGFITPAA LHYVRNHGAV PRGDWSTWTV DVTGLVKRPM RLTMDELVNG
FPAVEIPVTL VCAGNRRKEQ NMVQQTVGFN WGAAGVSTSV WRGARLRDVL RRCGIMPSKG
GALNVCFEGA EDLPGGGGSK YGTSITRQWA LDPSRDIMLA YMQNGEPLLP DHGFPVRAII
PGCIGGRMVK WVKRIIVTTA ESDNYYHYKD NRVLPSHVDA ELANADAWWY KPEYIINELN
VNSVITTPGH DEILPINGIT TQRGYTMKGY AYSGGGKRIT RVEVTLDGGE TWLVCVLDLP
EKPTKYGKHW CWCFWSVEVE VLDLLGAKEI AVRAWDQSHN TQPEKLIWNL MGMMNNCWFK
VKVNVCRPHK GEIGLVFEHP TQPGNQTGGW MARQKHLETA EAAAPGLKRS TSTPFMNTTD
GKQFTMSEVR KHSSQDSAWI VVHGHVYDCT AFLKDHPGGA DSILINAGTD CTEEFDAIHS
DKAKALLDTY RIGELITTGA GYSSDNSVHG ASNLSQLAPI REAIKAPAPV ALSSPRDKVP
CQLVDKKELS RDVRLFRFAL PSSDQVLGLP VGKHIFVCAS IEGKLCMRAY TPTSMVDEVG
HFDLLIKVYF KNEHPKFPDG GLMTQYLDSL PVGAYIDVKG PLGHVEYTGR GEFVINGKPR
NARRLAMIAG GSGITPMYQV IQSVLRDQPE DTTEMHLVYA NRTEDDILLR DELDRWAAEY
PDRLKVWYVI DQVKRPEEGW KYGVGFVTEE VLREHVPEGG DDTLALACGP PPMIKFAVSP
NLEKMKYDMA NSFIVF
