ID NIA_LOTTE Reviewed; 160 AA. AC P39882; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 02-SEP-2026, entry version 89. DE RecName: Full=Nitrate reductase [NADH]; DE Short=NR; DE EC=1.7.1.1; DE Flags: Fragment; GN Name=NIA; OS Lotus tetragonolobus (Winged pea) (Tetragonolobus purpureus). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus. OX NCBI_TaxID=3868; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Leaf; RA Wu S., Lu Q., Kriz A.L., Harper J.E.; RT "Molecular cloning and analysis winged bean and soybean bispecific RT constitutive NR and their NiR."; RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases. 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=nitrite + NAD(+) + H2O = nitrate + NADH + H(+); 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. {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}. 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; L16780; AAA80564.1; -; mRNA. DR AlphaFoldDB; P39882; -. DR SMR; P39882; -. DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB. DR GO; GO:0009703; F:nitrate reductase (NADH) activity; IEA:UniProtKB-EC. DR GO; GO:0042128; P:nitrate assimilation; IEA:TreeGrafter. DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:TreeGrafter. DR CDD; cd06183; cyt_b5_reduct_like; 1. DR FunFam; 3.40.50.80:FF:000025; Nitrate reductase [NADH]; 1. DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1. DR InterPro; IPR001834; CBR-like. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR039261; FNR_nucleotide-bd. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR PANTHER; PTHR19370; NADH-CYTOCHROME B5 REDUCTASE; 1. DR PANTHER; PTHR19370:SF185; NADH-CYTOCHROME B5 REDUCTASE; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PRINTS; PR00406; CYTB5RDTASE. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. PE 2: Evidence at transcript level; KW FAD; Flavoprotein; Heme; Iron; Metal-binding; Molybdenum; NAD; KW Nitrate assimilation; Oxidoreductase. FT CHAIN <1..160 FT /note="Nitrate reductase [NADH]" FT /id="PRO_0000166060" FT BINDING 37 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:A0A286R227" FT NON_TER 1 SQ SEQUENCE 160 AA; 17728 MW; D6CFC1447393A932 CRC64; KGPLGHIEYT GKGNFIAHGE PKFARRLAML AGGTGITPIY QVIQAVLKDP DDRTEMFFAV YSNKTESDIL LREELDAWAK KHSDRFKVWY VVDKAGNDWA FSTGRVNESI MRVHLPGPSD ALALACGPPP INSAYGWQPS LENIGYKKDD VPVFMATTQS //