NIA1_BRANA
ID NIA1_BRANA Reviewed; 911 AA.
AC P39867;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Nitrate reductase [NADH], clone PBNBR1405;
DE Short=NR;
DE EC=1.7.1.1;
GN Name=NIA1;
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Lisandra;
RX PubMed=8685274; DOI=10.1104/pp.111.1.39;
RA Fukuoka H., Ogawa T., Minami H., Yano H., Ohkawa Y.;
RT "Developmental stage-specific and nitrate-independent regulation of nitrate
RT reductase gene expression in rapeseed.";
RL Plant Physiol. 111:39-47(1996).
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; D38219; BAA07394.1; -; mRNA.
DR PIR; T08105; T08105.
DR RefSeq; NP_001302849.1; NM_001315920.1.
DR AlphaFoldDB; P39867; -.
DR SMR; P39867; -.
DR GeneID; 106400358; -.
DR KEGG; bna:106400358; -.
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..911
FT /note="Nitrate reductase [NADH], clone PBNBR1405"
FT /id="PRO_0000166051"
FT DOMAIN 539..614
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT DOMAIN 654..766
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 191
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 574
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 597
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 706..709
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 723..727
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 728
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17571"
FT BINDING 735
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 740..742
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 793
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT DISULFID 430
FT /note="Interchain"
FT /evidence="ECO:0000255"
SQ SEQUENCE 911 AA; 102252 MW; BBA4E19835B03D8C CRC64;
MATSVDNRHY PRLSSALNGG VVHSFKPPLV PSPSLDRDQD QSVNVPTEKS VDKTTKEDRF
DSSDDEDESH NRYVSYYKEM VLKSNSDLEP TALDSRDEST GDKWIHRNSS MVRLTGKHPF
NAEAPLPRLM HHGFITPVPL HYVRNHGGVP KAEWSDWSVE VTGLVKRPAG LTMEQLISEF
PSREFPVTLV CAGNRRKEQN MVKQTIGFNW GSAGVSTSLW RGVALSDVLR RCGVYSKRGG
ALNVCFEGAE DLPGGGGSKY GTSIKKEMAM DPARDIILAY MQNGELLTPD HGFPVRVIIP
GFIGGRMVKW LKRIIVTPQE SDNYYHYKDN RVLPSYVDAE LPNEESWWYR PEYIINELNI
NSVITTPGHE EILPINAFTT QKPYTLKGYA YSGGGKKVTR VEVTLDGGET WSVCELDHQE
KPNKYGKFWC WCFWSLDVEV LDLLSAKEVA VRAWDESLNT QPEKLIWNLM GMMNNCWFRI
KTNVCKPHRG EIGIVFEHPT RPGNQSGGWM AKERQIEKSS ESHPTLKKSV STPFMNTASK
MYSMSEVRKH NSAESAWIIV HGHIYDCTRF LKDHPGGSDS ILINAGTDCT EEFEAIHSDK
AKKLLEDYRI GELITTGYDS SPNVSVHGGS SVMSLLAPIR QLAPTKNIAL VNPREKVPVK
LIEKTSISHD VRRFRFALPS EDQQLGLPVG KHIFLCATIN DKLCLRAYTP TSTVDAVGYI
DLVIKVYFKN VHPRFPNGGL MSQHPDSLPI GAVLDIKGPL GHIEYQGRGK FMVSGKPKFA
NKLAMLAGGT GITPIYQVIQ SILSDPEDET EMFVVYANRT EDDILVREEL EGWASKFPDR
LKIWYVVEIA KEGWEYSTGF ITEAVLREHV PEGLEGESLA LACGPPPMIQ FALQPNLEKM
GYDIKEDLLI F
