ID C1G7W4_PARBD Unreviewed; 1049 AA.
AC C1G7W4;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Nitrate reductase [NADPH] {ECO:0000256|ARBA:ARBA00015499};
DE EC=1.7.1.3 {ECO:0000256|ARBA:ARBA00012673};
GN ORFNames=PADG_03269 {ECO:0000313|EMBL:EEH47171.1};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH47171.1, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH47171.1, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH47171.1,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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; KN275959; EEH47171.1; -; Genomic_DNA.
DR RefSeq; XP_010758803.1; XM_010760501.1.
DR AlphaFoldDB; C1G7W4; -.
DR STRING; 502780.C1G7W4; -.
DR GeneID; 22582606; -.
DR KEGG; pbn:PADG_03269; -.
DR VEuPathDB; FungiDB:PADG_03269; -.
DR eggNOG; KOG0534; Eukaryota.
DR eggNOG; KOG0535; Eukaryota.
DR eggNOG; KOG0537; Eukaryota.
DR HOGENOM; CLU_003827_4_2_1; -.
DR InParanoid; C1G7W4; -.
DR OMA; MNNCWYT; -.
DR OrthoDB; 1239at2759; -.
DR Proteomes; UP000001628; 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:UP000001628}.
FT DOMAIN 674..752
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 785..897
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1049 AA; 119297 MW; 6BC50D9DAC2F0E75 CRC64;
MASGAHITCP RYHPGSTKKE IEEEPNWRTA GLPRIGLRNR ENHFPGLTQR GDEWLKEELE
FEEHAIENEA ELFKKMERGD LLTVRDIMTK QEDFHLRRPE VFSEGWRYVL HTTEDFLKFQ
QNWPVNVQKR QKEEEEKKRK EEVEEAQGHL KQENERRREC GENAINGEDA SPPENGTGAE
GKPLTKTADR SKQTYSAQEI ALLRTLQTEK EYIKSLKQDD GMGQSPLAGD QNTKPMRIDE
ADQFSPDNWI PRNDALIRLT GKHPLNCEPP LSTLYDAGLI TPNKLHFVRN HGPVPHLRWQ
THRLDVESGK LVLSMDELKD RFQTINIPVL IACDGNRRKE VNMVKRSKGF NWGPGACGCA
YWKGPLLRDV LLAAGVPDEP PPHRTWVNFE GADDPSDGKY ATCIPLEYAM DPNNDVILAY
EMNDKVLPPD HGYPLRIVIP GYVGGRCVKW LSRIWTSDKE NDTYYHVFDN RVLPGFVVDM
DSEFAKAMFE LPSTACIEQT LNSVIVKPAN GEALNLLTGD NKRRKEYRIE GIAYTGGGHE
VQRVEVSLDC GENWLYCTRR FPKAPIRHGK KFWIWVHWYV DVDIVHLARA TGITVRCFDA
FKNCQPERLN WNLLGMMNNC WYTVRTNISQ HPKSGDLLIT FQHPTEPGSG KGGWMKPSME
EQREEIRQEA TAPPKQFTRQ EVEKHDSASN CWIVINNKVY DATNVLSWHP GGASAILAHA
GWVHLETTEE FESIHDDYAQ QKLNECLLGV VTEKAREYIK KEAEENVKAR TKGGADKPES
GIQRHKWTQV RFRKKKQLSA DTRLYTFALP PDTKSLGLGT CEHIQLGFHF ADKLIIRPYT
PVRPVFESEA DGTFTLAVKT YFPSSTQPGG TISNVLDCLR DNEEVEIKGP SGMIRYEGNG
QFVIDGKIRK FNNVTLILGG SGITPGYQLI ARILRSDAVP GGSKDSTAIR VIDANKTEDD
ILLMDELDEF TKQHPQQFRI IHVIASPKQE LMEGRIEGLV NRDVIRQYGF EPQGDNVALL
CGPPGLIKMA ALPNLKDWGY KEDENLFGF
//
