ID A0A3B6QAN7_WHEAT Unreviewed; 914 AA.
AC A0A3B6QAN7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Nitrate reductase {ECO:0000256|PIRNR:PIRNR000233};
GN ORFNames=CFC21_090865 {ECO:0000313|EMBL:KAF7087702.1}, CFC21_090871
GN {ECO:0000313|EMBL:KAF7087707.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS6D02G020700.1};
RN [1] {ECO:0000313|EMBL:KAF7087702.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7087702.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS6D02G020700.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS6D02G020700.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS6D02G020700.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7087702.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7087702.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) 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, 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}.
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DR EMBL; CM022228; KAF7087702.1; -; Genomic_DNA.
DR EMBL; CM022228; KAF7087707.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6QAN7; -.
DR SMR; A0A3B6QAN7; -.
DR STRING; 4565.A0A3B6QAN7; -.
DR PaxDb; 4565-Traes_6DS_69570DBE2-1; -.
DR EnsemblPlants; TraesCS6D02G020700.1; TraesCS6D02G020700.1; TraesCS6D02G020700.
DR Gramene; TraesCAD_scaffold_044875_01G000100.1; TraesCAD_scaffold_044875_01G000100.1; TraesCAD_scaffold_044875_01G000100.
DR Gramene; TraesCLE_scaffold_032368_01G000100.1; TraesCLE_scaffold_032368_01G000100.1; TraesCLE_scaffold_032368_01G000100.
DR Gramene; TraesCS6D02G020700.1; TraesCS6D02G020700.1; TraesCS6D02G020700.
DR Gramene; TraesCS6D03G0042700.1; TraesCS6D03G0042700.1.CDS; TraesCS6D03G0042700.
DR Gramene; TraesKAR6D01G0006120.1; cds.TraesKAR6D01G0006120.1; TraesKAR6D01G0006120.
DR Gramene; TraesPAR_scaffold_103124_01G000100.1; TraesPAR_scaffold_103124_01G000100.1; TraesPAR_scaffold_103124_01G000100.
DR Gramene; TraesROB_scaffold_101117_01G000300.1; TraesROB_scaffold_101117_01G000300.1; TraesROB_scaffold_101117_01G000300.
DR Gramene; TraesWEE_scaffold_098685_01G000100.1; TraesWEE_scaffold_098685_01G000100.1; TraesWEE_scaffold_098685_01G000100.
DR OMA; MNNCWYT; -.
DR OrthoDB; 1239at2759; -.
DR Proteomes; UP000019116; Chromosome 6D.
DR Proteomes; UP000815260; Chromosome 6D.
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:UP000019116}.
FT DOMAIN 538..613
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 654..766
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..72
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 187
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 914 AA; 101768 MW; 32D71E9265E07B65 CRC64;
MAASVEPRQS FGRLDAPATA PPARNGASNG IRRRADSPVR GCGFPPLISP PRKALVEEDE
DEDDDEEPEE DWREAYGSQL QLEVEPSTRD PRDEGTADAW IDRNPSLIRL TGKHPLNCEP
PLARLMHHGF ITPAPLHYVR NHGAVPRGDW STWTVEVTGL VRRPARLTMD ELANGFAAAE
LPATLVCAGN RRKEQNMVQQ TVGFNWGAAG VSTSVWRGAR LRDVLLRCGI MSSSKKGQAL
NVCFEGAEDL PGGGGSKYGT SVTREWALDP SRDILLAYAQ NGEPLLPDHG YPVRVLIPGC
IGGRMVKWLR RIVVTTAESD NYYHFKDNRV LPSHVDAELA NSEAWWYRPE YIINELNTNS
VITTPGHDEI LPINAFTTQR AYTMKGYAYS GGGKKITRVE VTLDGGESWM LCTLDIPEKP
NKYGRYWCWC FWSVEIEVLD LLGAKEVSVR AWDQTHNTQP EKLIWNLMGM MNNCWFKVKV
NVCRPHKGEI GLVFEHPTQP GNQTGGWMAR QKHLETAEAA APGLKRSTST PFMNTVADKQ
FTMSEVRKHG SKESAWIVVH GHVYDCTAFL KDHPGGADSI LINAGSDCTE EFDAIHSDKA
KALLDTYRIG ELITTGTGYN SDNSVHGGSS LSHLAPIREA TKVAGAPIAL SSPREKVPCR
LVDKKELSHD VRLFRFALPS SDQVLGLPVG KHIFVCATID GKLCMRAYTP TSMVDEIGQF
ELLVKVYFRD EHPKFPNGGL MTQYLESLQL GSCIDVKGPL GHVEYTGRGN FVINGKQRRA
RRLAMICGGS GITPMYQVIQ AVLRDQPEDE TEMHLVYANR SEDDILLRDE LDRWAAEYPE
RLKVWYVIDQ VKRPEDGWRF SVGFVTEDIL RAHVPEGGDE TLALACGPPP MIKFAISPNL
EKMKYDMANS FISF
//
