ID A0A165VN99_9AGAM Unreviewed; 870 AA.
AC A0A165VN99;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 08-NOV-2023, entry version 30.
DE RecName: Full=Nitrate reductase [NADPH] {ECO:0000256|ARBA:ARBA00015499};
DE EC=1.7.1.3 {ECO:0000256|ARBA:ARBA00012673};
GN ORFNames=NEOLEDRAFT_1153772 {ECO:0000313|EMBL:KZT29931.1};
OS Neolentinus lepideus HHB14362 ss-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT29931.1, ECO:0000313|Proteomes:UP000076761};
RN [1] {ECO:0000313|EMBL:KZT29931.1, ECO:0000313|Proteomes:UP000076761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT29931.1,
RC ECO:0000313|Proteomes:UP000076761};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV425553; KZT29931.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165VN99; -.
DR STRING; 1314782.A0A165VN99; -.
DR InParanoid; A0A165VN99; -.
DR OrthoDB; 1239at2759; -.
DR Proteomes; UP000076761; 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:UP000076761}.
FT DOMAIN 488..566
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 604..722
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 870 AA; 98700 MW; 0E9E317607118865 CRC64;
MTRKNKSRKA KKKDPSLSAC TKDEEEEEFI RHIIEEQKHL SQLKNHDGKT VAPLLENNLE
MYIAEDDQFS PENWIPRSSA LTRLAGKSPL NAEPPLSELF DVGMITPTRL HYVRNHGEVP
RLNWETHTLD VYSDPADILP NAKCFSMDEL AAMDSICMPV NIACDNNRRG EYNLFRGVLA
RDLLLACGAP EDPPPGKKWF LHYEGADICS GGTYATSIPY LYAMDPMNDV MIAYEMNGRA
LHPDHGYPIR SIIPGFVGGR LVKWLKKLWV SEEESTNWYH VSLTRDSRVI PSFVTEQDSL
LAKVFYHHPS TACYEQVLNS AICHPSHREE LPTDQKKYRI QGYAYAGGGA EVTKVEVSLD
EGKTWKYCFR RWPDAPLRHG RKFWTWLHWY CDVKVEEILD AKEIRCRAWD SQKNTQPDNF
TWNILGTLNN SIYRIRSTTV IDEKTGTVSV QWLHPVVPGS DDGWMKPSPE EQVKMKVEEL
TAGAGDRDNQ FTIEEVAKHA STDDCWIVIN NKVYDVTSAL SWHPGGANAI MPHAGKCHME
TTLEYASIHD DYANKKRDEC YIGVLTKKGI ELMNTDSGKD DAKHAHEARA KEAKEREGYP
LKKHSWCPAT LVKKTELSHD TRRYTFVLPA EEGEKVKVGL PIGNHLAIGV HFKDRMVVRP
YTPTRPIFAS EDDGTFDLVV KSYFPDEKGK FPPGGTVGNY LDCLEEGEQI DVKGPMGEII
YYGKGKFTSD GKEFQFSKIN LLAGGSGITP HYQLIHAIIL DETDDTKLRL VYCNNSEDDI
LLFEDLNGLA ERSKGQLEIW HILSHPRNEE DWKKTGGTGH FDENVMKERM FEPADDCCVF
VCGPPGLVEK AGKPSLEKWG FKDAESMFGW
//
