NIA_FUSOX
ID NIA_FUSOX Reviewed; 905 AA.
AC P39863;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Nitrate reductase [NADPH];
DE Short=NR;
DE EC=1.7.1.3;
GN Name=NIA;
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FOM24;
RX PubMed=8370541; DOI=10.1016/0378-1119(93)90669-t;
RA Diolez A., Langin T., Gerlinger C., Brygoo Y., Daboussi M.-J.;
RT "The nia gene of Fusarium oxysporum: isolation, sequence and development of
RT a homologous transformation system.";
RL Gene 131:61-67(1993).
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; Z22549; CAA80270.1; -; Genomic_DNA.
DR PIR; JN0803; JN0803.
DR AlphaFoldDB; P39863; -.
DR SMR; P39863; -.
DR PRIDE; P39863; -.
DR VEuPathDB; FungiDB:FOC1_g10006706; -.
DR VEuPathDB; FungiDB:FOC4_g10006835; -.
DR VEuPathDB; FungiDB:FOIG_06720; -.
DR VEuPathDB; FungiDB:FOMG_03004; -.
DR VEuPathDB; FungiDB:FOXG_04181; -.
DR VEuPathDB; FungiDB:FOZG_02928; -.
DR VEuPathDB; FungiDB:HZS61_014296; -.
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..905
FT /note="Nitrate reductase [NADPH]"
FT /id="PRO_0000166043"
FT DOMAIN 546..621
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT DOMAIN 648..759
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 179
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 581
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 604
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 702..705
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 719..723
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 733..735
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 783
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17571"
FT BINDING 786
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 875..884
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT DISULFID 428
FT /note="Interchain"
FT /evidence="ECO:0000255"
SQ SEQUENCE 905 AA; 101899 MW; D5D8E23F7971ACDA CRC64;
METSTTTTLL QQERIPENSE PISTHIHTHS LPPTPPGTAK PSRIGSFHDL QELSSVESPR
LDHIKPYPLP PKFSPKSVLK EDLKTPDNFV ERDPRLIRLT GVHPFNVEAP LSDLYDEGFL
TSENLHYVRN HGHVPRCEDD DILDWEFEIS GLVENPIKMN VRDLINDYQQ LTYPVTFVCA
GNRRKEQNIV RKTKGFSWGP AGLSTALWTG VAIGDLLSAA KPKRGARYVC FEGADKLPNG
YYGTSIKLNW CMDPNRGVMV AHKMNGNPLP PDHGKPVRIV IPGQIGGRSI KWLKKITITQ
EPSDNWYHIY DNRVLPTMIS PEESANLPEV WKDEKYAIYD LSTNSAICYP AHEEKVPFTD
APASYKVRGY AYSGGGRRIT RVEVTLDKGK SWRLANIRYP EDDYRNAPEG DTLYGGRVDM
WWRETSFCWC FWDLDIPLDE LKSADDIMMR AMDESMNVQP RDMYWSVLGM MNNPWFRIVI
HKEDHALRFE HPTHATLKIK GWMERVKEAG GDLTNGYWGE KAPGEVQEVV VKEPEKQICM
TNPQINRKIT IEELKAHSGE EEPWFVVKGE VYDGTPYLSG HPGGAASIFG AAGQDATEEF
MAIHSENAKA MLPTYHIGTL DEESRAILSG DATKTNDDAD REVFLQAKTW SKAILDKKTS
ISPDTKIFSF KLNHEAQKIG LPTGQHLMMR LRDPATREAI IRSYTPYSDG SDCGRLDILI
KIYYDTPQRK GGVMTQALDA LPIGHWVDFK GPTGKFVYHG NGLCTINEKE RRVRRFIMVC
GGSGITPIRQ VLRAVIDNPK DTTPCLVFNG NRSVNDILCM EELEELEAAN PSRCRVVNAL
SNPPPEWNGL KGFVNQALVP EYMDLPKASG EGDELLLVCG PPPMVKAVEA SFLGMGFKSD
DFVFF
