ID A0A094B8P1_9PEZI Unreviewed; 1028 AA.
AC A0A094B8P1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Nitrate reductase [NADPH] {ECO:0000256|ARBA:ARBA00015499};
DE EC=1.7.1.3 {ECO:0000256|ARBA:ARBA00012673};
GN ORFNames=V492_07847 {ECO:0000313|EMBL:KFY06682.1};
OS Pseudogymnoascus sp. VKM F-4246.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY06682.1, ECO:0000313|Proteomes:UP000029299};
RN [1] {ECO:0000313|EMBL:KFY06682.1, ECO:0000313|Proteomes:UP000029299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY06682.1,
RC ECO:0000313|Proteomes:UP000029299};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFY06682.1}.
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DR EMBL; JPJU01002709; KFY06682.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094B8P1; -.
DR STRING; 1420902.A0A094B8P1; -.
DR HOGENOM; CLU_003827_4_2_1; -.
DR Proteomes; UP000029299; 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; 1.
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:UP000029299}.
FT DOMAIN 661..739
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 772..884
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1028 AA; 116356 MW; 5FFF467C7AEBEFBA CRC64;
MAPRPHLVRV TPHPGSSQKA IEEEPDWGGI HQNRIGFLNR QERPTGHTHS GDDKNVEGGL
DKETAGEVKG LDYHLIRPDV HSAGWRYVLH SSEDWIKNTQ DWPANLEKRK EDEKTAKLKE
EEQRKTNGEK GQSNEVKQED DWRREAGQNK HHDAYASNVG SDGDQQGKKD SESKQNAGSK
DESAQQKYSP QELALLHNLQ QEKDYVFNLK QNDGKKRSPA ADGRQLISID EVDQFTPDNW
IPRSDKLVRL TGQHPMNAEP QLTSLFDAGL ITPNDLHYVR NHGPVPHLLW ETHTLEIEGS
SLVLTMDEIK ENFDPINIPV ALACDGNRRK ELNQIKRSKG FNWASGAVSC AYWKGPLLRD
ILRKAGVPEA FPEGKRYWVN FEGADELSEG KYATCIPFEY AMDSNNDVIL AYEMNDVPLP
PDHGHPIRLI IPGYVGGRCV KWLNKIWLSD RENESHYHIW DNRVLPSFIT EMDGEFSKTM
FSHPDTKCNE QNLNSVIVKP AQGERISLAE ARRGNTYRIM GYAYDGGGHE VQRVEVSLDE
GETWLYCFPD GPIRHGNKYW TWLHWYLDVE ITHLLQAKSV TVRCHNVFKN TQPEKPSWNI
MGMMNNCWYV IKPAIVQGHD NVIPEIVFTH PVEPGTGDGG WLKESTEIQI SNAKQAAGGP
QKQFTREEIE KHNKDNDCWI VVNDNVYDAT SVLEWHPGGK AAIMGHAGKV HEETSSDFNS
VHDGYAFEKL KECVLGMVTE KAKSFIKANA QKVAEEKAKS AKGNSKIALQ KHRWIPARLK
KREAISEDTR KYTFKLPDNK NELGLATCQH VQLGFHFKDK MVIRSYTPIR PILPTEEDGT
FQLAVKTYFP SDSQPGGAIS NILDCMPLGE EIEIRGPVGD IIYEGNGKFN IEGENMNFRR
VTLILGGSGI TPGYQLICRI LMLEGDNTEI RVVDANRSES DILLRDEMED LQKKHPRQFK
ITHVLSRPSD DWKGLKGYVN PDIIREHAFA PTDGSVALLC GPPAMIQKAA LPALKDWGYE
EEKNCFGF
//
