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Database: UniProt
Entry: A0A3M9Y322_9PEZI
LinkDB: A0A3M9Y322_9PEZI
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ID   A0A3M9Y322_9PEZI        Unreviewed;      1060 AA.
AC   A0A3M9Y322;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Nitrate reductase [NADPH] {ECO:0000256|ARBA:ARBA00015499};
DE            EC=1.7.1.3 {ECO:0000256|ARBA:ARBA00012673};
GN   ORFNames=D7B24_009348 {ECO:0000313|EMBL:RNJ54883.1};
OS   Verticillium nonalfalfae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=1051616 {ECO:0000313|EMBL:RNJ54883.1, ECO:0000313|Proteomes:UP000267145};
RN   [1] {ECO:0000313|EMBL:RNJ54883.1, ECO:0000313|Proteomes:UP000267145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VnAa140 {ECO:0000313|EMBL:RNJ54883.1,
RC   ECO:0000313|Proteomes:UP000267145};
RA   Stajich J.E., Kasson M.T.;
RT   "Genome sequence of Verticillium nonalfalfae VnAa140.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RNJ54883.1}.
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DR   EMBL; RBVV01000091; RNJ54883.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M9Y322; -.
DR   STRING; 1051616.A0A3M9Y322; -.
DR   OrthoDB; 1239at2759; -.
DR   Proteomes; UP000267145; 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; 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}.
FT   DOMAIN          661..743
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          767..916
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          829..855
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..140
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..184
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1060 AA;  119210 MW;  D3A3B2711E56CCD8 CRC64;
     MGGTSHFVVE KRDHPGSSEQ AIENEPDWGA GHNHRVGFKN VDGRVPGYSG EPGGPKYWEK
     AMKKYEALLD RKRKGELINF RDVIDGEDDL RLIHPQDRAV GVRFALDCTE DWVKYGQKWP
     INEAKKKKVE EKKKKSEEGQ DSQQNGASQP AKPAHDDKTS HGDLKDERKN DVGEGETLED
     KYTDEERALL RALQHEKDYM ANLRTNDGNQ ESPQKHNRCD VSIDEADQFT PDNWFPRSAE
     LIRLTGKHPL NAEAPLTGLL AAGLITPNEL HYVRNHGAVP RLMWEYHTVD INDGKLTLTM
     DELKHGYRSI NIPVFMACDG NRRKELNMMR RTQGFNWGAG GGGCAYWKGA LLRDVLLAAG
     VPDDLGNDGP RRWVNFEGSE DLSAGKYATC IPLAYAMDPR NDVMLAYEMN DLPLPPDHGY
     PVRVIIPGHV GGRCVKWLKR VWISEKENDS YYHIWDNRVL PSFVTDNESP FAETMFRHPG
     TACMEQNLNS VIVHPQQGEK ILLKDAGKGK GTEYRIQGFA YDGGGHEVQR VEVSLDDGET
     WLYCIRKFPD LPIRHGKKFW TWCHWHVDVP LHRMVQARSI IVKCWNVFKN SQPRDPAWNL
     KGMMNNCWYT VKSEIAPDDE TDGAYVLFRH PTEPANGDGG WMQPSVVNQI ELAKREAGTP
     QKQFTREEIE KHDSEDDCWI VVDGKVYDAT SVMSWHPGGK APIMVHAGRV HAETTEEFGS
     IHDGFAYEKL KGTVTDKAAN FIKENAKKQA VEKAKSKDDN KATLQKHRWV PTKLIARKAI
     SEDTRAYTFQ LPDHKAILGL GTCQHILIGF HLKDKMLVRS YTPTRPILPA LNDTPDRLPS
     PSQNGIPNGK GAEERSKAIN EQHHDLRDGD GTFELVVKTY FPTDQQPGGA MSNILDCMPL
     GEEVEIRGPT GEIVYLGNGT FLIDGEERKY RRVSLVLGGS GVTPGFSLLS RVIMSGDDET
     EIRVVDANNT EADILLREEM EELVKKSKGQ LKVVHVLSRP SDAWKGLTGY VTGEILKDNL
     FAPGEGAATF VCGPPVMMQK AVLPAMKEWG YEEDKDLFGF
//
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