NIA_SPIOL
ID NIA_SPIOL Reviewed; 926 AA.
AC P23312; Q41377;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Nitrate reductase [NADH];
DE Short=NR;
DE EC=1.7.1.1;
GN Name=NIA;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2103436; DOI=10.1007/bf00017743;
RA Prosser I.M., Lazarus C.M.;
RT "Nucleotide sequence of a spinach nitrate reductase cDNA.";
RL Plant Mol. Biol. 15:187-190(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Hoyo;
RX PubMed=9128133; DOI=10.1016/s0167-4838(97)00015-0;
RA Tamura N., Takahashi H., Takeba G., Satoi T., Nakagawa H.;
RT "The nitrate reductase gene isolated from DNA of cultured spinach cells.";
RL Biochim. Biophys. Acta 1338:151-155(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 287-926.
RC STRAIN=cv. Hoyo;
RA Shiraishi N., Kubo Y., Takeba K., Kiyota S., Sakano K., Nakagawa H.;
RT "Sequence analysis of cloned cDNA and proteolytic fragments for nitrate
RT reductase from Spinacia oleracea L.";
RL Plant Cell Physiol. 32:1031-1038(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=1.7.1.1;
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 -!- SIMILARITY: Belongs to the nitrate reductase family. {ECO:0000305}.
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DR EMBL; M32600; AAA34033.1; -; mRNA.
DR EMBL; D86226; BAA13047.1; -; Genomic_DNA.
DR EMBL; U08029; AAA18377.1; -; mRNA.
DR PIR; S11868; RDSPNH.
DR AlphaFoldDB; P23312; -.
DR SMR; P23312; -.
DR IntAct; P23312; 1.
DR OrthoDB; 166846at2759; -.
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:UniProtKB-EC.
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; Nitrate assimilation; Oxidoreductase.
FT CHAIN 1..926
FT /note="Nitrate reductase [NADH]"
FT /id="PRO_0000166071"
FT DOMAIN 551..626
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT DOMAIN 670..782
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 204
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 586
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 609
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 722..725
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 739..743
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 744
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17571"
FT BINDING 751
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 756..758
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 809
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT DISULFID 443
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT CONFLICT 303
FT /note="D -> A (in Ref. 2; BAA13047)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 926 AA; 103971 MW; FF21DF01963F1AFC CRC64;
MAASVDRQYH PAPMSGVVRT PFSNHHRSDS PVRNGYTFSN PPSSNGVVKP GEKIKLVDNN
SNSNNGSNNN NNRYDSDSEE DDDENEMNVW NEMIKKGNSE LEPSSVDSRD EGTADQWIER
NPSMIRLTGK HPFNSEPPLT RLMHHGFLTP VPLHYVRNHG PVPNAKWEDW TVEVTGLVKR
PIRFTMDQLV NDFQSREFPV TLVCAGNRRK EQNMTKQSIG FNWGSAAVST SVWRGVPLRD
VLKRCGVMSS LKGALNVCFE GAEDLPGGGG SKYGTSVKRE FAMDPARDII LAYMQNGEKL
SPDHGYPVRM IIPGFIGGRM VKWLKRIIVT TTESDNYYHY KDNRVLPSHV DAELANSEAW
WYKQEYIINE LNVNSVITSP CHEEILPINA WTTQRPYTMR GYAYSGGGRK VTRVEVTMDG
GDTWDICELD HQERGSKYGK FWCWCFWSLE VEVLDLLGAK EIGVRAWDES LNTQPEKLIW
NVMGMMNNCW FRVKTNVCKP HKGEIGIVFE HPTQPGNKSG GWMARERHLE ISDSGPTLKR
TASTPFMNTT SKMYSMSEVK KHNTADSAWI VVHGNVYNAT RFLKDHPGGS DSILINAGTD
CTEEFDAIHS DKAKRLLEDF RIGELISTGY TSDSSSPGNS VHGGSVYSGL AGLAPITEAV
PLRNVALNPR VKIPCKLIEK VSLSHDVRRF RFGLPSEDQV LGLPVGKHIF LCANVDDKLC
MRAYTPSSTI DVVGYFDLVV KVYFKDVHPR FPNGGVMSQH LDSLSLGSIV DVKGPLGHIE
YLGKGNFTVH GKPKFAKKLA MISGGTGITP IYQVMQAILK DPEDKTEMHV VYANRTEEDI
LLREELDKWA DEFRDRVKVW YVVEKAEEGW KYDTGFISEK ILRDHVPAVG DDVLALTCGP
PPMIQFAVQP NLDKMGFDIK EQLLIF
