NIA_LOTJA
ID NIA_LOTJA Reviewed; 900 AA.
AC P39869;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Nitrate reductase [NADH];
DE Short=NR;
DE EC=1.7.1.1;
GN Name=NIA;
OS Lotus japonicus (Lotus corniculatus var. japonicus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX NCBI_TaxID=34305;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Gifu / B-129;
RA Waterhouse R.N., Smyth A.J., Prosser I.M., Forde B.G., Clarkson D.T.;
RL Submitted (JUL-1994) 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 -!- 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. {ECO:0000250};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=Binds 1 heme group. The heme group is called cytochrome b-557.
CC {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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nitrate reductase family. {ECO:0000305}.
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DR EMBL; X80670; CAA56696.1; -; Genomic_DNA.
DR PIR; S47029; S47029.
DR AlphaFoldDB; P39869; -.
DR SMR; P39869; -.
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 3: Inferred from homology;
KW Disulfide bond; FAD; Flavoprotein; Heme; Iron; Metal-binding; Molybdenum;
KW NAD; Nitrate assimilation; Oxidoreductase.
FT CHAIN 1..900
FT /note="Nitrate reductase [NADH]"
FT /id="PRO_0000166059"
FT DOMAIN 521..596
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT DOMAIN 644..756
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 172
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 556
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 579
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 696..699
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 713..717
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 718
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17571"
FT BINDING 725
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 730..732
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 783
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT DISULFID 411
FT /note="Interchain"
FT /evidence="ECO:0000255"
SQ SEQUENCE 900 AA; 101420 MW; 547C25388DD13535 CRC64;
MAASVDNRQY STLNGVVRSF TPNNTYLHDP KPSFPAVNLD LDASSSDDDD EKDDASILKD
LIRKGNAEIE SSVLDPRDQG TADNWISRNS SMVRLTGKHP FNSEPPLPRL MHHGFITPVP
LHYVRNHGPV PKARWDDWTV EVTGLVKTPT RFSMDRLVRD FPSRELPVTL VCAGNRRKEQ
NMVRQSIGFN WGSAGVSTSV WRGVSLRHIL RRCRIQTRSR GALHVCFEGD EDLPGGGGSK
YSTSIRREVA MDPSRDVILA YMQNGEVLAP DHGFPVRVII PGFIGGRMVK WLKRIVVTEE
ECDGHYHYKD NRVLPSHVDA ELANEEGWWY KPEYIINELN INSVITTPCH DEILPINAWT
TQRPYTLRGY SYSGGGRKVT RVEVTLDGGE TWFVCALDQQ EKPNKYGKYW CWCFWSLEVE
VLDLLGTKEI AVRAWDEALN TQPENLIWNV MGMMNNCWFR VKTNVCKPHK GEIGIVFEHP
TQPGNQPGGW MAKEKHLEIS QQDSRPILKK SVSSPFMNTF TKMYSLSEVK KHNSPDSAWI
IVHGHVYDCT RFLKDHPGGA DSILINAGTD CTEEFEAIHS DKAKKMLEDY RVGELITTGY
TSDSSSPNNS LHGNSEFKHL APIKEITTMS LPPLPRRKVA LIPREKIPCK LISRTSISHD
VRVFRFALPS EDQQLGLPVG KHIFLCATVD GKLCMRAYTP TSGVDEVGYF ELVVKVYFKG
VHPKFPNGGA MSQHLDSLPI GSDLDVKGPL GHIEYTGRGN FLVHGKHRFA KKLAMLAGGT
GITPIYQVAQ AILKDPEDHT KMYVVYANRT EDDILLREEL DTWAKKYEDR FKVWYVVETA
KEGWGYSVGF VTEGVMREHL PEAGDDALAL ACGPPPMIQF AVNPNLEKMG YDVKNDLLVF
