ID N1PX19_DOTSN Unreviewed; 1113 AA.
AC N1PX19;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Nitrate reductase [NADPH] {ECO:0000256|ARBA:ARBA00015499};
DE EC=1.7.1.3 {ECO:0000256|ARBA:ARBA00012673};
GN ORFNames=DOTSEDRAFT_86414 {ECO:0000313|EMBL:EME48076.1};
OS Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight
OS fungus) (Mycosphaerella pini).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX NCBI_TaxID=675120 {ECO:0000313|EMBL:EME48076.1, ECO:0000313|Proteomes:UP000016933};
RN [1] {ECO:0000313|Proteomes:UP000016933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX PubMed=23209441; DOI=10.1371/journal.pgen.1003088;
RA de Wit P.J.G.M., van der Burgt A., Oekmen B., Stergiopoulos I.,
RA Abd-Elsalam K.A., Aerts A.L., Bahkali A.H., Beenen H.G., Chettri P.,
RA Cox M.P., Datema E., de Vries R.P., Dhillon B., Ganley A.R.,
RA Griffiths S.A., Guo Y., Hamelin R.C., Henrissat B., Kabir M.S.,
RA Jashni M.K., Kema G., Klaubauf S., Lapidus A., Levasseur A., Lindquist E.,
RA Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A., Schijlen E.,
RA Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S., Goodwin S.B.,
RA Grigoriev I.V., Collemare J., Bradshaw R.E.;
RT "The genomes of the fungal plant pathogens Cladosporium fulvum and
RT Dothistroma septosporum reveal adaptation to different hosts and lifestyles
RT but also signatures of common ancestry.";
RL PLoS Genet. 8:E1003088-E1003088(2012).
RN [2] {ECO:0000313|EMBL:EME48076.1, ECO:0000313|Proteomes:UP000016933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
CC -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first step
CC of nitrate assimilation in plants, fungi and bacteria.
CC {ECO:0000256|ARBA:ARBA00003838}.
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 Evidence={ECO:0000256|ARBA:ARBA00000195};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000256|ARBA:ARBA00001924};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the nitrate reductase family.
CC {ECO:0000256|ARBA:ARBA00006253}.
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DR EMBL; KB446536; EME48076.1; -; Genomic_DNA.
DR AlphaFoldDB; N1PX19; -.
DR STRING; 675120.N1PX19; -.
DR EnsemblFungi; EME48076; EME48076; DOTSEDRAFT_86414.
DR eggNOG; KOG0534; Eukaryota.
DR eggNOG; KOG0535; Eukaryota.
DR eggNOG; KOG0537; Eukaryota.
DR HOGENOM; CLU_003827_4_2_1; -.
DR OMA; MNNCWYT; -.
DR OrthoDB; 1239at2759; -.
DR Proteomes; UP000016933; Unassembled WGS sequence.
DR GO; GO:0030151; F:molybdenum ion 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 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; 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; 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; 2.
DR Pfam; PF03404; Mo-co_dimer; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF00174; Oxidored_molyb; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
DR PRINTS; PR00407; EUMOPTERIN.
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; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000016933}.
FT DOMAIN 715..793
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 826..969
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1113 AA; 125934 MW; 99C78FAFDA27C4EF CRC64;
MPHHIPWTVN VREHPGSSKD DISNEPDWSN AHQHRVGFRN RQGRMPGVTH QDDEAGDVPG
LIRSSSSSEP DEEEEDFDEQ AKKDYKRLEA KAKKGDLINF RDIITNEKDF HLRYPENRSL
GWRFVLEATE DWVKNEEDWP ANIQKRQKEE AAKKEKETHT SDGVAISGRS KESKEKPSHE
ESGQEENDWK RKDGENSKHN DAYAADDEHS DQSDKDGSDD EEQSEYQKLL DRYSPQEIAL
LRALQHEKDY RYKLTQNDGK RESPQTHNRS TISIDEQDQF SPDNWLPRSE DLIRLTGKHP
MNAEADLTRL FEESQKCELI TPNELHYIRN HGAVPRLLWE FHKLDVENGK LTLCMNDLRD
NFEHINIAVA LACDGNRRKE LNMIRKSKGF NWGAGATGCA YWKGPLLRDV LEAAGVKAGK
YTGEGKLRWV NFQGADDPSE GKYETCITLD YAMDPANDVI LAMYMNDVPL PPDHGYPVRL
LIPGYVGGRC VKWLSKIWIT DYENQSHYHI WDNRVLPSFI TEKDGEFANA MFAHPDTACN
EQNLNSVIVK PAQGEKIPLT KARHGQTYRI EGYAYDGGGH EVQRVEVSLD GGETWLYCIR
KFPEYPIRHG NKFWTWLHWY VDVSVVHMLS AKSIAVRAWS VFKNTQPERA IWNTMGMMNN
CWYQVKPEIQ QSKDEDVPHM FFRHPCEPGT GDGGWMKPSV ENQIASAKQE AGAPQKQFTR
EEIEKHSTEN DCWLVVDQKV YDCTSVLAWH PGGKAAILGH AGKVHAETSD EFASIHDGFA
YQKLKECILG VVTEKAANFI TANAEAAAKE KANSKNDDQD IVLQKHRWVP VELLERKALS
EDTRSYIFGL PDDMKDLGLG TCQHIQLGFH LKDKMLIRSY TPTKPLLPDP KKASKHDPAA
KPSKSTASSP SPSSDIQSMQ DGHGTFELVI KTYFPTSSQP GGAMSNILDC MPIGEEIEIR
GPTGEIVYNG NGSFTIEDKE MKFKKISLVL GGSGITPGYA LIARALLGAG EDVEVRVVDA
NKSEKDILLR EELDHFVKES KGRLKVTHVL SHPSEEWKGL KGHVNADIIK KSLFPPEEGS
VTFLCGPPAM IQKAALPALR EWGYKEDVNV FGF
//
