NIA_NEUCR
ID NIA_NEUCR Reviewed; 982 AA.
AC P08619; Q7RVF6;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Nitrate reductase [NADPH];
DE Short=NR;
DE EC=1.7.1.3;
GN Name=nit-3; ORFNames=NCU05298;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=1829499; DOI=10.1007/bf00259673;
RA Okamoto P.M., Fu Y.-H., Marzluf G.A.;
RT "Nit-3, the structural gene of nitrate reductase in Neurospora crassa:
RT nucleotide sequence and regulation of mRNA synthesis and turnover.";
RL Mol. Gen. Genet. 227:213-223(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [3]
RP PRELIMINARY PARTIAL PROTEIN SEQUENCE.
RX PubMed=16453480; DOI=10.1002/j.1460-2075.1983.tb01678.x;
RA Le K.H.D., Lederer F.;
RT "On the presence of a heme-binding domain homologous to cytochrome b5 in
RT Neurospora crassa assimilatory nitrate reductase.";
RL EMBO J. 2:1909-1914(1983).
RN [4]
RP MUTANTS.
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=8479443; DOI=10.1007/bf00279534;
RA Okamoto P.M., Garrett R.H., Marzluf G.A.;
RT "Molecular characterization of conventional and new repeat-induced mutants
RT of nit-3, the structural gene that encodes nitrate reductase in Neurospora
RT crassa.";
RL Mol. Gen. Genet. 238:81-90(1993).
RN [5]
RP MUTAGENESIS.
RX PubMed=8355655; DOI=10.1007/bf00277060;
RA Okamoto P.M., Marzluf G.A.;
RT "Nitrate reductase of Neurospora crassa: the functional role of individual
RT amino acids in the heme domain as examined by site-directed mutagenesis.";
RL Mol. Gen. Genet. 240:221-230(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 per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=Binds 1 heme group per subunit. The heme group is called
CC cytochrome b-557. {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 -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC -!- SUBUNIT: Homodimer.
CC -!- INDUCTION: Its expression is highly regulated and responds rapidly to
CC nitrate induction and to nitrogen repression.
CC -!- SIMILARITY: Belongs to the nitrate reductase family. {ECO:0000305}.
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DR EMBL; X61303; CAA43600.1; -; Genomic_DNA.
DR EMBL; CM002239; EAA32833.1; -; Genomic_DNA.
DR PIR; S16292; S16292.
DR RefSeq; XP_962069.1; XM_956976.2.
DR AlphaFoldDB; P08619; -.
DR SMR; P08619; -.
DR STRING; 5141.EFNCRP00000005051; -.
DR PRIDE; P08619; -.
DR EnsemblFungi; EAA32833; EAA32833; NCU05298.
DR GeneID; 3878217; -.
DR KEGG; ncr:NCU05298; -.
DR HOGENOM; CLU_003827_4_0_1; -.
DR InParanoid; P08619; -.
DR BioCyc; MetaCyc:MON-13438; -.
DR BRENDA; 1.7.1.3; 3627.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
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-UniPathway.
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; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR005066; MoCF_OxRdtse_dimer.
DR InterPro; IPR008335; Mopterin_OxRdtase_euk.
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 PRINTS; PR00363; CYTOCHROMEB5.
DR PRINTS; PR00407; EUMOPTERIN.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; Heme; Iron;
KW Metal-binding; Molybdenum; NADP; Nitrate assimilation; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..982
FT /note="Nitrate reductase [NADPH]"
FT /id="PRO_0000166046"
FT DOMAIN 617..692
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT DOMAIN 721..836
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 240
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 652
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 675
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 776..779
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 794..798
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 810..812
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 860
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17571"
FT BINDING 863
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 952..961
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT DISULFID 499
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT MUTAGEN 652
FT /note="H->A: Little loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:8355655"
FT MUTAGEN 675
FT /note="H->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:8355655"
FT CONFLICT 31..49
FT /note="VGCSSREEPQGSGGLLVPH -> AAAAAAEKNPRGAADYCPSD (in Ref.
FT 2; EAA32833)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="I -> IP (in Ref. 2; EAA32833)"
FT /evidence="ECO:0000305"
FT CONFLICT 696
FT /note="P -> L (in Ref. 2; EAA32833)"
FT /evidence="ECO:0000305"
FT CONFLICT 869..870
FT /note="AE -> LR (in Ref. 2; EAA32833)"
FT /evidence="ECO:0000305"
FT CONFLICT 910
FT /note="M -> E (in Ref. 2; EAA32833)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 982 AA; 108433 MW; B7838C031B19687F CRC64;
MEAPALEQRQ SLHDSSERQQ RFTSLILPNG VGCSSREEPQ GSGGLLVPHN DNDIDNDLAS
TRTASPTTTD FSSSSSDDNS TTLETSVNYS HSSNTNTNTS CPPSPITSSS LKPAYPLPPP
STRLTTILPT DLKTPDHLIR DPRLIRLTGS HPFNVEPPLT ALFEHGFLTP QNLHYVRNHG
PIPSSVATPP ATINKEEDDS LLNWEFTVEG LVEHPLKISV RELMDASKWD NVTYPVTLVC
AGNRRKEQNV LRKSKGFSWG AGGLSTALWT GVGLSEILAR AKPLTKKGGG ARYVCFEGAD
QLPNGTYGTS VKLAWAMDPN KGIMVAHKMN GENLHPDHGR PVRVVVPGQI GGRSVKWLKR
IVVTKGPSEN WYHVFDNRVL PTTVGPEESG EKTEEMERVW RDERYAIYDL NVNSVICEPG
HGEVVSLRGD EGAGTYRLRG YAYAGGGRRV TRLEVTLDQG KSWRLAGIEY PEDRYREAQD
GEELFGGRLD VSWRESCFCW CFWDLEIPLS ELRKAKDVCI RAMDESLALQ PKEMYWSVLG
MMNNPWFRVV IHHEGDTLRF EHPTQPMLTS DGWMDRVKKE GGNLANGFWG EKVPGAEENV
VKEEPVKEIS MVDEKVTRLI TLEELRQHDG EEEPWFVVNG QVYNGTPFLE GHPGGAASIT
GAAGQDVTDE FLAIHSENAK AMMPTYHIGT LTPSAPAALK SSSTSDPALS DPSRPIFLQS
KTWNSAILTF KESVSPDTKI FHFALSHPAQ SIGLPVGQHL MMRLPDPAKP TESIIRAYTP
ISDGTLERGT LRVLVKIYYA SPTEDIKGGQ MTQALDALAL GKAVEFKGPV GKFVYQGRGV
CSVNGRERKV KRFVMVCGGS GVTPIYQVAE AVAVDDQDGT ECLVLDGNRV EGDILMKSEL
DELVERAKPM GRCRVKYTLS RPGAEWEGLR GRLDKTMLER EVGEGDLRGE TMVLLCGPEG
MQNMVREVLK GMGWKDEDVL VF
