ID A0A1X6NHP9_9APHY Unreviewed; 828 AA.
AC A0A1X6NHP9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 08-NOV-2023, entry version 24.
DE RecName: Full=Nitrate reductase [NADPH] {ECO:0000256|ARBA:ARBA00015499};
DE EC=1.7.1.3 {ECO:0000256|ARBA:ARBA00012673};
DE Flags: Fragment;
GN ORFNames=POSPLADRAFT_1127961 {ECO:0000313|EMBL:OSX68145.1};
OS Postia placenta MAD-698-R-SB12.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Postiaceae; Postia.
OX NCBI_TaxID=670580 {ECO:0000313|EMBL:OSX68145.1, ECO:0000313|Proteomes:UP000194127};
RN [1] {ECO:0000313|EMBL:OSX68145.1, ECO:0000313|Proteomes:UP000194127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAD-698-R-SB12 {ECO:0000313|EMBL:OSX68145.1,
RC ECO:0000313|Proteomes:UP000194127};
RG DOE Joint Genome Institute;
RA Gaskell J., Kersten P., Larrondo L.F., Canessa P., Martinez D., Hibbett D.,
RA Schmoll M., Kubicek C.P., Martinez A.T., Yadav J., Master E.,
RA Magnuson J.K., James T., Yaver D., Berka R., Labutti K., Lipzen A.,
RA Aerts A., Barry K., Henrissat B., Blanchette R., Grigoriev I., Cullen D.;
RT "Genome Sequence of the Model Brown-Rot Fungus Postia placenta SB12.";
RL Submitted (APR-2017) 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}.
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DR EMBL; KZ110591; OSX68145.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6NHP9; -.
DR STRING; 670580.A0A1X6NHP9; -.
DR OrthoDB; 1239at2759; -.
DR Proteomes; UP000194127; 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:UP000194127}.
FT DOMAIN 452..530
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 563..682
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OSX68145.1"
SQ SEQUENCE 828 AA; 93118 MW; 114A92C931A5FA0C CRC64;
TPDSWIPRSQ QLLRLTGRHP LNAEPSLTAL FDAGMITPTK LHYVRSHGPV PALDWDSHKL
SEGDRDNVHF GVADDGEPTA TRLWTMDEIA EGPFPLCELP VTIACDGNRR KEVNMVKRSA
GYNWSAAGVS TCVWRGIFIR DLLLATGLRT GPEHEEWFLN LEGADQCSEG TYATSIPLAH
AMDPANDVLL VFGQNDRVLH PDHGYPLRIV IPGFVGGRQV KWLKNIWISK EANSSHYHIW
DNKVVPSVID SKEHPLADAF FHSEDNACYE QILQSVICKP AHDERLPLPT EKGGLDQLYK
VEGYAYDGSG TKVHRVELSL DEGTTWKYCS RRFMDRPTRH GTKHWAWVFW SCEVRISDLA
NAKEILVRAF DTKKNTQPEH EFNIHQHLWR LVKPMISSNS WYRVRPSLVI DPETKQPVIH
FRHPVAPGQE EGGWMKPNIE DVMADQSGGS SGKTFSIEEV EKHNKRDDAW LILDGKVYDV
TSVLDWHPGG ANAIIGYVGK ATVDATNQYK GIHDGYANSK RDECLIGELT KEAMKVIEKD
AERAAKLLAE MKEKRKDFAL QPDVFVAAKL LKREEKTSDT RLYTFELPKR KDGSHGRMGL
PVGKHVQIAI HFADQAVMRS YTPVSPVLPH EEDGTFQLLV KTYLPSDGGP FPPGGTASNY
LDLMQEGEEI DILGPNGEIE YKGNGEFEIE GKTYHFTKVS LVTGGSGLTP HWQVIHAILS
NKNDKTKIAL VDSNKTFDDI LMREQLQEYA DKEQERFKLW HCLSKPPKDR EWKVVVCSIC
VIVREEHLYP AGDDTVALVC GPPSLIEKAA VPGLKELGFV EGKNLFGW
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