NIA_LEPMC
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 03-AUG-2022, entry version 119.
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 Leptosphaeria; 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}.
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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 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 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
