ID NIA_BEABA Reviewed; 894 AA. AC P43100; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 02-SEP-2026, entry version 120. DE RecName: Full=Nitrate reductase [NADPH]; DE Short=NR; DE EC=1.7.1.3; GN Name=NIA; OS Beauveria bassiana (White muscardine disease fungus) (Tritirachium OS shiotae). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria. OX NCBI_TaxID=176275; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=BB147; RA Maurer P.; RL Submitted (FEB-1995) 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 + NADP(+) + H2O = nitrate + NADPH + H(+); 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=1.7.1.3; 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; X84950; CAA59336.1; -; Genomic_DNA. DR PIR; S52857; S52857. DR AlphaFoldDB; P43100; -. DR SMR; P43100; -. DR EnsemblFungi; BB8028_0002g00600.1; BB8028_0002g00600.1; BB8028_0002g00600. 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:0050464; F:nitrate reductase (NADPH) activity; IEA:UniProtKB-EC. DR GO; GO:0008482; F:sulfite oxidase activity; IEA:TreeGrafter. DR GO; GO:0042128; P:nitrate assimilation; IEA:InterPro. DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:InterPro. DR GO; GO:0006790; P:sulfur compound metabolic process; IEA:TreeGrafter. DR CDD; cd06183; cyt_b5_reduct_like; 1. DR FunFam; 2.60.40.650:FF:000001; Nitrate reductase; 1. DR FunFam; 3.10.120.10:FF:000016; Nitrate reductase; 1. DR FunFam; 3.90.420.10:FF:000005; Nitrate reductase; 1. DR Gene3D; 2.60.40.650; -; 1. DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1. DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1. DR Gene3D; 3.90.420.10; Oxidoreductase, molybdopterin-binding domain; 1. DR Gene3D; 2.40.30.10; Translation factors; 1. 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; PTHR19372:SF7; SULFITE OXIDASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR19372; SULFITE REDUCTASE; 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; PR00406; CYTB5RDTASE. DR PRINTS; PR00363; CYTOCHROMEB5. DR PRINTS; PR00407; EUMOPTERIN. DR PRINTS; PR00371; FPNCR. DR SMART; SM01117; Cyt-b5; 1. DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. DR SUPFAM; SSF56524; Oxidoreductase molybdopterin-binding domain; 1. DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 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 3: Inferred from homology; KW Disulfide bond; FAD; Flavoprotein; Heme; Iron; Metal-binding; Molybdenum; KW NADP; Nitrate assimilation; Oxidoreductase. FT CHAIN 1..894 FT /note="Nitrate reductase [NADPH]" FT /id="PRO_0000166041" FT DOMAIN 535..610 FT /note="Cytochrome b5 heme-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279" FT DOMAIN 638..749 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716" FT REGION 1..79 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 7..16 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 69..79 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 169 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 570 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 593 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 692..695 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:A0A286R227" FT BINDING 709..713 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:A0A286R227" FT BINDING 723..725 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:A0A286R227" FT BINDING 773 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P17571" FT BINDING 776 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:A0A286R227" FT DISULFID 418 FT /note="Interchain" FT /evidence="ECO:0000255" SQ SEQUENCE 894 AA; 99934 MW; D0ED234BF1B1322B CRC64; MAVKSQLGVT YTTKTFPPSP PRTVGNSHAG SDDERDEVDA TPTTPPVEKL GQLLKPYSLP PTNTPTHVLP EDLKTPDHRV NRDPRLIRLT GVHPFNVEPP LTDLYDEGFL NSENLHYVRN HGPVPHCPDD ESLNWTFTVD GLVEKPFTIA VRDLIQKYDQ FTYPVTLVCA GNRRKEQNVV RKSKGFSWGA AGLSTALWTG VPIGALLRMA KPKRAAKYVC FEGADKLPNG YYGTSVKLNW CMDENRGIMV AHKMNGQSLH PDHGKPVRII IPGQIGGRSV KWLKKITITS EPSDNWYHIY DNRVLPTTIS PDASANLPDV WKDEKYAIYD LNANSAICYP RHDERLVLAT APDTYKVRGY AYGGGGKRIT RLEVTLNKGK SWLLAGIHYP EDDYRRAPDG DLLYGGSTDM WWRETCFCWC FWEIDIPVAD LSAADDIMIR AMDEGMMVQP RDMYWSVLGM MNNPWFRVVI HKEDGALRFE HPTQPALMPG GWMERVKRRG GNLTNGFWGE KTAAEEEQVL AEPEKEICMT NPKVVRIISL EELKAHEGEM EPWFVVNGHV YNGTPYLDNH PGGATSIINA AAQDATEEFM TIHSENAKAM MPQYHIGTLN DAARKALEGS AEESPASDPT RAVFLQPKYW SKAILETKTD VSSDSKIFSF RLDHAAQSIG LPTGQHLLVR LRDPATREAV IRAYTPLSET HAKGQLDILI KIYRDVPGQP GGKMTQALDS IPLGHFVDIK GPVGKFEYLG KGHCTVSGTS RHVRRFVMIC AGSGVTPIFQ VLRAVTSDAQ DGTECLVLDG NRCEKDILCR EELDAMVARA PARTTLLHKL SRPDASWCGL RGRMDKEYLE EHIGGFRKSD GREMVLVCGP AALEETVRSV LVEMAWKPED MLFF //