ID   NIA2_MAIZE              Reviewed;         231 AA.
AC   P39871;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Nitrate reductase [NAD(P)H];
DE            Short=NR;
DE            EC=1.7.1.2;
DE   Flags: Fragment;
GN   Name=NAR;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. W64A X WI82E; TISSUE=Root;
RA   Long D.M., Oaks A., Rothstein S.J.;
RT   "Regulation of maize root nitrate reductase mRNA levels.";
RL   Physiol. Plantarum 85:561-566(1992).
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=1.7.1.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NADP(+) + nitrite = H(+) + NADPH + nitrate;
CC         Xref=Rhea:RHEA:19061, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.7.1.2;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC       Note=Binds 1 heme group. The heme group is called cytochrome b-557.
CC       {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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the nitrate reductase family. {ECO:0000305}.
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DR   EMBL; X64446; CAA45776.1; -; mRNA.
DR   PIR; S24544; S24544.
DR   AlphaFoldDB; P39871; -.
DR   SMR; P39871; -.
DR   PRIDE; P39871; -.
DR   MaizeGDB; 25891; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P39871; baseline and differential.
DR   GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009703; F:nitrate reductase (NADH) activity; IBA:GO_Central.
DR   GO; GO:0050464; F:nitrate reductase (NADPH) activity; IEA:RHEA.
DR   GO; GO:0042128; P:nitrate assimilation; IBA:GO_Central.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.80; -; 1.
DR   InterPro; IPR001834; CBR-like.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR19370; PTHR19370; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Heme; Iron; Metal-binding; Molybdenum; NAD; NADP;
KW   Nitrate assimilation; Oxidoreductase; Reference proteome.
FT   CHAIN           <1..231
FT                   /note="Nitrate reductase [NAD(P)H]"
FT                   /id="PRO_0000166063"
FT   DOMAIN          <1..85
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         25..28
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT   BINDING         42..46
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT   BINDING         47
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P17571"
FT   BINDING         59..61
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT   BINDING         112
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT   NON_TER         1
SQ   SEQUENCE   231 AA;  26254 MW;  9864B425C0ED45F4 CRC64;
     PQKLGLPVGR HVYVCASIGG KLCMRAYTPT SPVDEVGHFD LLIKIYFKDE DPKYPNGGLM
     SQYLDSLPLG ATIDIKGPHR HIEYTGRRRF VVNGKQRHAR RLAMIQAGRG TTPDDDTEQA
     VLRDQPDDDT EMHLVYANRT DHDMLLREEI DRAWLPRTRR LKVWYVVSKV PEDGWEYGVG
     RVDEHVMREH LPLGDSETIA LVCGPPAMIE CTVRPGLEKM GYDLDKACLV F