NIA7_HORVU
ID NIA7_HORVU Reviewed; 891 AA.
AC P27968;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Nitrate reductase [NAD(P)H];
DE EC=1.7.1.2;
GN Name=NAR-7;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Himalaya;
RX PubMed=1896007; DOI=10.1007/bf00260624;
RA Miyazaki J., Juricek M., Angelis K., Schnorr K.M., Kleinhofs A.,
RA Warner R.L.;
RT "Characterization and sequence of a novel nitrate reductase from barley.";
RL Mol. Gen. Genet. 228:329-334(1991).
CC -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first step
CC of nitrate assimilation in plants, fungi and bacteria.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + nitrite = H(+) + NADH + nitrate;
CC Xref=Rhea:RHEA:17913, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.7.1.2;
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=1.7.1.2;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=Binds 1 heme group per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000250};
CC -!- SUBUNIT: Homodimer.
CC -!- INDUCTION: By nitrate.
CC -!- SIMILARITY: Belongs to the nitrate reductase family. {ECO:0000305}.
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DR EMBL; X60173; CAA42739.1; -; Genomic_DNA.
DR PIR; S16895; RDBHNP.
DR AlphaFoldDB; P27968; -.
DR SMR; P27968; -.
DR IntAct; P27968; 1.
DR ExpressionAtlas; P27968; baseline and differential.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR GO; GO:0031984; C:organelle subcompartment; IEA:UniProt.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; ISS:UniProtKB.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0009703; F:nitrate reductase (NADH) activity; IEA:RHEA.
DR GO; GO:0050464; F:nitrate reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:InterPro.
DR Gene3D; 3.10.120.10; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR Gene3D; 3.90.420.10; -; 1.
DR InterPro; IPR001834; CBR-like.
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; PTHR19370; PTHR19370; 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; PR00363; CYTOCHROMEB5.
DR PRINTS; PR00407; EUMOPTERIN.
DR PRINTS; PR00371; FPNCR.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR SUPFAM; SSF56524; SSF56524; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR SUPFAM; SSF81296; SSF81296; 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 2: Evidence at transcript level;
KW Disulfide bond; FAD; Flavoprotein; Heme; Iron; Metal-binding; Molybdenum;
KW NAD; NADP; Nitrate assimilation; Oxidoreductase.
FT CHAIN 1..891
FT /note="Nitrate reductase [NAD(P)H]"
FT /id="PRO_0000166058"
FT DOMAIN 515..590
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT DOMAIN 630..742
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 168
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250|UniProtKB:P49050"
FT BINDING 550
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 573
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 682..685
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 699..703
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 704
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17571"
FT BINDING 711
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 716..718
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 769
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT DISULFID 406
FT /note="Interchain"
FT /evidence="ECO:0000255"
SQ SEQUENCE 891 AA; 98630 MW; AA47EC52FC1EFD13 CRC64;
MAASVEYNRQ VSAHPWPTNA QPKAAFDLFS SSGGGRRRSG ADSDSDDEDS VPPDWRSLYS
PRLDVEPSVK DPRDEATSDA WVKRHPALVR LTGKHPFNSE PPLPRLMSHG FITPVPLHYV
RNHGAVPKAD WSTWTVEVTG LVKRPVKFTM EELVTGFQAV EFPVTLVCAG NRRKEQNMVR
QSSGFNWGPG AISTTVWRGV RLRDVLRRCG VMGAGAASNV CFEGAEDLPG GGGCKYGTSL
RRSVAMDPAR DVILAYMQNG EPLAPDHGFP VRVIVPGFIG GRMVKWLKRI VVACNESESY
YHYRDNRVLP SHVDAELANA EAWWYKPECM INELNINSVI TTPGHDEVLP INALTTQKPY
TMKGYAYSGG GRKVTRVEVT LDGGETWQVC DLEHPERPTK YGKYWCWCFW SVEVEVLELL
GAKEMAVRAW DEALNTQPER LIWNLMGMMN NCWFRVKINV CRPHKGEIGL VFDHPTQPGN
QSGGWMARQK HIETSETTQG TLKRSTSTPF MSTASAQFTM SEVRRHASKD SAWIVVHGHV
YDCTAFLKDH PGGADSILIN AGSDCTEEFD AIHSAKARGL LEMYRVGELI VTGNDYSPQS
SNADLAAIVE APAVVVPRLP ASAVALANPR EKVRCRLVDK KSMSHNVRLF RFALPSPDQK
LGLPVGKHVY VCASTGGKLC MRAYTPTSSV EEVGHVELLI KIYFKDEDPK FPAGGLMSQY
LDALPLGAPV DIKGPVGHIE YAGRGAFTVG GERRFARRLA MVAGGTGITP VYQVIQAVLR
DQPDDTTEMH LVYANRTEDD MLLREEIDRW AAANPARLKV WYVVSKVGRP EDAWEYGVGR
VDEQVLREHL PLGGDGETLA LVCGPPAMLE CTVRPGLEKM GYDLDKDCLV F
