ID NIA_LEPMC Reviewed; 893 AA. AC P36842; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 2. DT 28-JUN-2023, entry version 122. DE RecName: Full=Nitrate reductase [NADPH]; DE Short=NR; DE EC=1.7.1.3; GN Name=NIAD; OS Leptosphaeria maculans (Blackleg fungus) (Phoma lingam). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes; OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae; OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex. OX NCBI_TaxID=5022; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Isolate 19; RX PubMed=8041355; DOI=10.1007/bf00280180; RA Williams R.S.B., Davis M.A., Howlett B.J.; RT "Nitrate reductase of the ascomycetous fungus, Leptosphaeria maculans: gene RT sequence and chromosomal location."; RL Mol. Gen. Genet. 244:1-8(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 886-893. RC STRAIN=Isolate 19; RX PubMed=7789806; DOI=10.1016/0378-1119(95)00169-7; RA Williams R.S.B., Davis M.A., Howlett B.J.; RT "The nitrate and nitrite reductase-encoding genes of Leptosphaeria maculans RT are closely linked and transcribed in the same direction."; RL Gene 158:153-154(1995). 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 + 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=1.7.1.3; 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; U04445; AAA50579.1; -; Genomic_DNA. DR EMBL; U18793; AAA82740.1; -; Genomic_DNA. DR PIR; S46442; S46442. DR AlphaFoldDB; P36842; -. DR SMR; P36842; -. 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:0042128; P:nitrate assimilation; IEA:UniProtKB-KW. DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:InterPro. DR CDD; cd06183; cyt_b5_reduct_like; 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..893 FT /note="Nitrate reductase [NADPH]" FT /id="PRO_0000166045" FT DOMAIN 536..611 FT /note="Cytochrome b5 heme-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279" FT DOMAIN 641..752 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716" FT REGION 1..83 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 54..68 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 170 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 571 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 594 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 695..698 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:A0A286R227" FT BINDING 712..716 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:A0A286R227" FT BINDING 726..728 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:A0A286R227" FT BINDING 776 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P17571" FT BINDING 779 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:A0A286R227" FT BINDING 863..872 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT DISULFID 418 FT /note="Interchain" FT /evidence="ECO:0000255" SQ SEQUENCE 893 AA; 99942 MW; 7686E3C9676DD2EF CRC64; MSVTTQQPAV VPLPSSPRLP IESHAGPRST QLPPSPPETV NGDDPKSITS TPAEPDFPLP PPANPKPQVL DIDKPTPDAH VPRDPRLIRL TGVHPFNTEP PLTDLYNEGF LTSPELFYVR NHGAVPEVQD EECLDWEFSI EGMVANPLKI TLRQLLEEYE NVTYPVTLVC AGNRRKEQNV VRKSKGFAWG AAGVSTALFT GVVMKDVIER AKPLRKAKYV CMEGADKLPN GYYGTSVKLN WVMDPNRGIM LAHKMNGENL SLDHGKPLRA VVPGQIGGRS VKWLKKLIVT AEPSDNWYHI YDNRVLPTMV DPDEAAKNPK WWMDERYAIY DLSPNSAIAF PAHEEKVVLA SAENSYNVRG YAYSGGGRRI TRCEVSLNKG KNWRLANIDY AEDKYRDFEG RELFGARLDM DWRETSFCWC FWNLDIATAE LRDANDILVR AMDEAMCIQP RDMYWSVLGM MNNPWYRITI HHEGDVLRFE HPTQPALIPG GWMERVKKAG GNLTNGQWGE QIEGQELENT AVEEVKEIKM TKDGVNRIVE LDELKWHESA EYPWFVVNDE VYDGTSFLEG HPGGAQSIIS AAGLDASDEF MAIHSETAKA MMPAYHIGTL SPTASKQLSL EEPTSKQASS SSLRPTFLDS RTWSKALLSS KTKVSWDTRI FRFKLDHASQ TLGLPTGQHL MIRLRDPVTR EAIIRSYTPI SQISEQGFCD VLIKIYADAP GREGGKMTKA LDSIPCGHWV DMKGPIGKFE YLGKGVCSIN GNERRVRSMK MICGGSGITP IYQVLRAILQ DSADSTHCTV LNGNRLEEDI LCREDLDRFA EENGERCTLV HTLTQAAEGW TGRRGRIGEE LLKEFCGTEE DGLVLVCGPE GLERSVKGLL SGMAWRDDDV IFF //