NIA_ASPNG
ID NIA_ASPNG Reviewed; 867 AA.
AC P36858;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Nitrate reductase [NADPH];
DE Short=NR;
DE EC=1.7.1.3;
GN Name=niaD;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1541396; DOI=10.1016/0378-1119(92)90682-f;
RA Unkles S.E., Campbell E.I., Punt P.J., Hawker K.L., Contreras R.,
RA Hawkins A.R., van den Hondel C.A.M.J.J., Kinghorn J.R.;
RT "The Aspergillus niger niaD gene encoding nitrate reductase: upstream
RT nucleotide and amino acid sequence comparisons.";
RL Gene 111:149-155(1992).
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; M77022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JQ1525; JQ1525.
DR AlphaFoldDB; P36858; -.
DR SMR; P36858; -.
DR STRING; 5061.CADANGAP00006756; -.
DR PRIDE; P36858; -.
DR VEuPathDB; FungiDB:An08g05610; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1129386; -.
DR VEuPathDB; FungiDB:ATCC64974_101980; -.
DR VEuPathDB; FungiDB:M747DRAFT_296682; -.
DR eggNOG; KOG0534; Eukaryota.
DR eggNOG; KOG0535; Eukaryota.
DR eggNOG; KOG0537; Eukaryota.
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..867
FT /note="Nitrate reductase [NADPH]"
FT /id="PRO_0000166040"
FT DOMAIN 514..589
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT DOMAIN 615..726
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 38..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 152
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 549
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 572
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 669..672
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 686..690
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 691
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17571"
FT BINDING 700..702
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 753
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 837..846
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT DISULFID 399
FT /note="Interchain"
FT /evidence="ECO:0000255"
SQ SEQUENCE 867 AA; 97189 MW; BE40335DCBE12E42 CRC64;
MATVTEVLTE PFTAQGVTLK SGPIKVHQEE LPAVELSDIP LPPPSKEPTE VLSIDKPTPD
YHVPRDPRLI RLTGVHPFNV EPPLTALYDE GFLTSPELFY VRNHGPVPLV KDEDIPNWEI
SIEGLVEKPL VLNFRDILQQ YDQITAPITL VCAGNRRKEQ NVVRKTKGFS WGSAGLSTAL
WTGPMMADIL RSAKPLRKAK YVCMEGADKL PNGYYGTSIK LNWAMDPNRG IMLAHKMNGE
DLRPDHGRPL RAVVPGQIGG RSVKWLKKLI LTDAPSDNWY HIYDNRVLPT MVSPEMSSSD
PNWWRDDRYA IYDLNVNSSV VYPEHKEVLD LASAGPSYNV KGYAYAGGGR RITRVEISLD
KGKSWRLANI SYAEDKYRDF EGDLFGGRVH MSWRETCFCW CFWSLDIAIP ELENTDAILV
RAMDEALALQ PRDMYWSVLG MMNNPWFRVT ITKENGTLRF EHPTDPTGPG GWMERVKKAG
GDLVNGYWGE RQAGEEPTEP EPEKEINMKK EGVNRIIDLQ EFKKNSSDEK PWFIVNGEVY
DGTAFLEGHP GGAQSIISSA GIDVSEEFLA IHTQTAKAMM PDYHIGTMDK ASLEALKNDN
APQSDEPRAT FLQSKSWTKA TLVKRTDVSW DTRIFTFQLQ HDKQTLGLPI GQHLMIKVAD
PTSKEAIIRS YTPISDTNQE GTMDLLVKIY FDTPTVKGGK MTMALEKLAL GSEIDCKGPT
GRFEYLGNGK ILVSGKERHV SSFKMICGGT GITPIFQVLR AVMQDKQDPT SCVVLDGNRQ
EEDILCRADL DAYEALDSKK CKVVHTLTKA PDSWTGRRGR ISEDLLKEHA IPDGKSMVLI
CGPEAMEKSA RKILLEQGWA ESDLHFF
