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Database: UniProt
Entry: A0A3B6NJU6_WHEAT
LinkDB: A0A3B6NJU6_WHEAT
Original site: A0A3B6NJU6_WHEAT 
ID   A0A3B6NJU6_WHEAT        Unreviewed;       914 AA.
AC   A0A3B6NJU6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Nitrate reductase {ECO:0000256|PIRNR:PIRNR000233};
GN   ORFNames=CFC21_081507 {ECO:0000313|EMBL:KAF7076905.1};
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:TraesCS6A02G017500.2};
RN   [1] {ECO:0000313|EMBL:KAF7076905.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7076905.1};
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:TraesCS6A02G017500.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS6A02G017500.2};
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:TraesCS6A02G017500.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:KAF7076905.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7076905.1};
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; CM022226; KAF7076905.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B6NJU6; -.
DR   SMR; A0A3B6NJU6; -.
DR   STRING; 4565.A0A3B6NJU6; -.
DR   EnsemblPlants; TraesCS6A02G017500.2; TraesCS6A02G017500.2; TraesCS6A02G017500.
DR   Gramene; TraesCS6A02G017500.2; TraesCS6A02G017500.2; TraesCS6A02G017500.
DR   Gramene; TraesCS6A03G0038200.1; TraesCS6A03G0038200.1.CDS; TraesCS6A03G0038200.
DR   Gramene; TraesKAR6A01G0008860.1; cds.TraesKAR6A01G0008860.1; TraesKAR6A01G0008860.
DR   OrthoDB; 1239at2759; -.
DR   Proteomes; UP000019116; Chromosome 6A.
DR   Proteomes; UP000815260; Chromosome 6A.
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..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..73
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         188
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;  101846 MW;  32C0A2A122F84DC3 CRC64;
     MAASVEPRQS SFGRLDAPAT SPPARSGASN GIRRRADSPV RGCGFPPLIS PPRKTLVEEE
     EEDEDDEEPE EDWREAYGSQ LQLEVEPSTR DPRDEGTADA WIDRNPSLIR LTGKHPLNCE
     PPLARLMHHG FITPAPLHYV RNHGAVPRGD WATWTVEVTG LVRRPARLTM DELSTAFPAA
     ELPATLVCAG NRRKEQNMVQ QTVGFNWGAA GVSTSVWRGA RLRDVLLRCG IMSSKKGQAL
     NVCFEGAEDL PGGGGSKYGT SVTWEWALDP SRDILLAYAQ NGEPLLPDHG YPVRVLIPGC
     IGGRMVKWLR RIVVTPAESD NYYHFRDNRV LPSHVDAELA NAEAWWYRPE YIINELNTNS
     VITTPGHDEI LPINAFTTQR AYTIKGYAYS GGGKKVTRVE VTLDGGESWM LCTLDIPEKP
     NKYGRYWCWC FWSVEIEVLD LLGAKEVAVR AWDQTHNTQP EKLIWNLMGM MNNCWFKVKI
     NVCRPHKGEI GLVFEHPTQP GNQTGGWMAR QKHLETAEAA APGLKRSTST PFMNTVADKQ
     FTMSEVRKHG SKESAWIVVH GHVYDCTAFL KDHPGGADSI LINAGSDCTE EFDAIHSDKA
     KALLDTYRIG ELITTGTGYN SDNSVHGGSS LSHLAPIREA TKVAGAPIAL SSPREKVPCR
     LVEKKELSHD VRLFRFALPS SDQVLGLPVG KHIFVCATID GKLCMRAYTP TSMVDEIGQF
     ELLVKVYFRD EHPKFPNGGL MTQYLESLQL GSCIDVKGPL GHVEYTGRGN FVINGKQRRA
     RRLAMICGGS GITPMYQVIQ AVLRDQPEDE TEMHLVYANR SEDDILLRDE LDRWAAEYPE
     RLKVWYVIDQ VKRPEDGWRF SVGFVTEDIL RAHVPEGGDD TLALACGPPP MIKFAISPNL
     EKMKYDMANS FISF
//
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