ID A0A0Q3FHC7_BRADI Unreviewed; 908 AA.
AC A0A0Q3FHC7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Nitrate reductase {ECO:0000256|PIRNR:PIRNR000233};
GN Name=100829419 {ECO:0000313|EnsemblPlants:KQJ98598};
GN ORFNames=BRADI_3g37940v3 {ECO:0000313|EMBL:KQJ98598.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:KQJ98598.1};
RN [1] {ECO:0000313|EMBL:KQJ98598.1, ECO:0000313|EnsemblPlants:KQJ98598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ98598.1,
RC ECO:0000313|EnsemblPlants:KQJ98598};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQJ98598.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ98598.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQJ98598}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ98598};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
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, ECO:0000256|PIRNR:PIRNR000233}.
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|PIRSR:PIRSR000233-1};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000256|PIRSR:PIRSR000233-1};
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, ECO:0000256|PIRNR:PIRNR000233}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000882; KQJ98598.1; -; Genomic_DNA.
DR RefSeq; XP_003574607.1; XM_003574559.2.
DR AlphaFoldDB; A0A0Q3FHC7; -.
DR STRING; 15368.A0A0Q3FHC7; -.
DR EnsemblPlants; KQJ98598; KQJ98598; BRADI_3g37940v3.
DR GeneID; 100829419; -.
DR Gramene; KQJ98598; KQJ98598; BRADI_3g37940v3.
DR KEGG; bdi:100829419; -.
DR InParanoid; A0A0Q3FHC7; -.
DR OrthoDB; 1239at2759; -.
DR Proteomes; UP000008810; Chromosome 3.
DR ExpressionAtlas; A0A0Q3FHC7; baseline and differential.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0009703; F:nitrate reductase (NADH) activity; IBA:GO_Central.
DR GO; GO:0050464; F:nitrate reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0042128; P:nitrate assimilation; IBA:GO_Central.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IBA:GO_Central.
DR CDD; cd06183; cyt_b5_reduct_like; 1.
DR CDD; cd02112; eukary_NR_Moco; 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; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
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; IPR012137; Nitr_rd_NADH.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
DR InterPro; IPR036374; OxRdtase_Mopterin-bd_sf.
DR InterPro; IPR022407; OxRdtase_Mopterin_BS.
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 PIRSF; PIRSF000233; Nitr_rd_NADH; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR PRINTS; PR00407; EUMOPTERIN.
DR PRINTS; PR00371; FPNCR.
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; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000233-1};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505, ECO:0000256|PIRSR:PIRSR000233-
KW 1};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063,
KW ECO:0000256|PIRNR:PIRNR000233};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810}.
FT DOMAIN 533..608
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 648..760
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 182
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000256|PIRSR:PIRSR000233-1"
SQ SEQUENCE 908 AA; 101248 MW; C61C37CBBD8BCDB8 CRC64;
MAASVEPRQF GRLETPVRAG AGTNGIRRRA DSPVRGCGFS PLISPPRKSC VHEEASSDEE
EEEQQDWREL YGSHLQSEVE PSVRDPRDEG TADAWIDRNP SLVRLTGKHP LNCEPPLSRL
MHHGFITPAP LHYVRNHGAV PRADWATWTV EVTGLVRRPA RFTMDELVHE FPAVEIPATL
VCAGNRRKEQ NMVQQTVGFN WGAAGVSTSV WRGARLRDVL RRCGVMGARQ GQGALNVCFE
GAEDLPGGGG SKYGTSVTRE WALDPSRDIM LAYMQNGEPL LPDHGFPVRV IIPGCIGGRM
VKWVKRIIVT TAESDNYYHF KDNRVLPSHV DAELANAEGW WYKPEHIINE LNTNSVITTP
GHDEILPINA FTTQRAYTMK GYAYSGGGKK ITRVEVTLDG GETWQVCTLD IPEKPNKYGR
YWCWCFWSVE VEVLDLLGAK EVAVRAWDQT HNTQPEKLIW NLMGMMNNCW FKVKVNVCRP
HKGEIGLVFE HPTQPGNQTG GWMARQKHLE TAEAAAPGLK RSTSTPFMNT TGDKQFTMSE
VRKHGSQESA WIVVHGHVYD CTAFLKDHPG GADSILINAG TDCTEEFDAI HSDKAKALLD
TYRVGELITT GTGYNSDNSV HGGSNLSHLA PIREATKALA PIALSSPREK VPCRLVDKKE
LSHDVRLFRF ALPSSDQVLG LPVGKHIFVC ANIEGKLCMR AYTPTSMVDE IGQFELLVKI
YFKDEHPKFP NGGLMTQHLE SLQIGASIDV KGPLGHVEYT GRGNFTINGK ARHARRLAMI
CGGSGITPMY QVIQAVLRDQ PEDETEMHLV YANRTEDDIL LRDELDRWAA DYPDRLKVWY
VIDQVKRPEE GWKFSVGFVT EAILREHVPE GGDDTLALAC GPPPMIKFAI SPNLEKMKYD
MANSFISF
//
