NIA1_MAIZE
ID NIA1_MAIZE Reviewed; 621 AA.
AC P17571;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Nitrate reductase [NADH] 1 {ECO:0000303|PubMed:2189408};
DE Short=NR {ECO:0000303|PubMed:2189408};
DE EC=1.7.1.1 {ECO:0000269|PubMed:2189408, ECO:0000269|PubMed:8188655};
DE Flags: Fragment;
GN Name=NNR1 {ECO:0000303|PubMed:16666879};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. W64 X W128E; TISSUE=Leaf;
RX PubMed=16666879; DOI=10.1104/pp.90.3.792;
RA Gowri G., Campbell W.H.;
RT "cDNA clones for corn leaf NADH: nitrate reductase and chloroplast
RT NAD(P)(+): glyceraldehyde-3-phosphate dehydrogenase.";
RL Plant Physiol. 90:792-798(1989).
RN [2]
RP SEQUENCE REVISION TO 389-390; 405-406 AND 414-417, CHARACTERIZATION,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. W64 X W128E; TISSUE=Leaf;
RX PubMed=2189408; DOI=10.1016/0006-291x(90)91168-r;
RA Hyde G.E., Campbell W.H.;
RT "High-level expression in Escherichia coli of the catalytically active
RT flavin domain of corn leaf NADH:nitrate reductase and its comparison to
RT human NADH:cytochrome B5 reductase.";
RL Biochem. Biophys. Res. Commun. 168:1285-1291(1990).
RN [3]
RP SECONDARY STRUCTURE OF FAD DOMAIN.
RX PubMed=1748631; DOI=10.1016/s0021-9258(18)54316-7;
RA Hyde G.E., Crawford N.M., Campbell W.H.;
RT "The sequence of squash NADH:nitrate reductase and its relationship to the
RT sequences of other flavoprotein oxidoreductases. A family of flavoprotein
RT pyridine nucleotide cytochrome reductases.";
RL J. Biol. Chem. 266:23542-23547(1991).
RN [4]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-593.
RX PubMed=8188655; DOI=10.1016/s0021-9258(17)36716-9;
RA Dwivedi U.N., Shiraishi N., Campbell W.H.;
RT "Identification of an 'essential' cysteine of nitrate reductase via
RT mutagenesis of its recombinant cytochrome b reductase domain.";
RL J. Biol. Chem. 269:13785-13791(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 352-621 IN COMPLEX WITH FAD, AND
RP COFACTOR.
RX PubMed=7812715; DOI=10.1016/s0969-2126(94)00082-4;
RA Lu G., Campbell W.H., Schneider G., Lindqvist Y.;
RT "Crystal structure of the FAD-containing fragment of corn nitrate reductase
RT at 2.5-A resolution: relationship to other flavoprotein reductases.";
RL Structure 2:809-821(1994).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 232-501, AND MUTAGENESIS OF
RP CYS-593.
RX PubMed=7760334; DOI=10.1006/jmbi.1995.0273;
RA Lu G., Lindqvist Y., Schneider G., Dwivedi U., Campbell W.H.;
RT "Structural studies on corn nitrate reductase: refined structure of the
RT cytochrome b reductase fragment at 2.5 A, its ADP complex and an active-
RT site mutant and modeling of the cytochrome b domain.";
RL J. Mol. Biol. 248:931-948(1995).
CC -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first step
CC of nitrate assimilation in plants, fungi and bacteria.
CC {ECO:0000269|PubMed:2189408}.
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; Evidence={ECO:0000269|PubMed:2189408,
CC ECO:0000269|PubMed:8188655};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:7812715};
CC Note=Binds 1 FAD. {ECO:0000269|PubMed:7812715};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 1 heme group. The heme group is called cytochrome b-557.;
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; M27821; AAA03202.1; -; mRNA.
DR PIR; S19254; S19254.
DR PDB; 1CNE; X-ray; 3.00 A; A=352-621.
DR PDB; 1CNF; X-ray; 2.70 A; A=352-621.
DR PDB; 2CND; X-ray; 2.50 A; A=352-621.
DR PDBsum; 1CNE; -.
DR PDBsum; 1CNF; -.
DR PDBsum; 2CND; -.
DR AlphaFoldDB; P17571; -.
DR SMR; P17571; -.
DR STRING; 4577.GRMZM2G568636_P01; -.
DR iPTMnet; P17571; -.
DR PaxDb; P17571; -.
DR PRIDE; P17571; -.
DR MaizeGDB; 25899; -.
DR eggNOG; KOG0534; Eukaryota.
DR eggNOG; KOG0535; Eukaryota.
DR eggNOG; KOG0537; Eukaryota.
DR BRENDA; 1.7.1.1; 6752.
DR EvolutionaryTrace; P17571; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P17571; baseline and differential.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0009703; F:nitrate reductase (NADH) activity; IDA:UniProtKB.
DR GO; GO:0042128; P:nitrate assimilation; IDA:UniProtKB.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IBA:GO_Central.
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; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
DR InterPro; IPR036374; OxRdtase_Mopterin-bd_sf.
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 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.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; FAD; Flavoprotein; Heme; Iron; Metal-binding;
KW Molybdenum; NAD; Nitrate assimilation; Oxidoreductase; Reference proteome.
FT CHAIN <1..621
FT /note="Nitrate reductase [NADH] 1"
FT /id="PRO_0000166062"
FT DOMAIN 249..324
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT DOMAIN 361..473
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 284
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 307
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 413..416
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:7812715,
FT ECO:0007744|PDB:2CND"
FT BINDING 430..432
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:7812715,
FT ECO:0007744|PDB:2CND"
FT BINDING 435
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:7812715,
FT ECO:0007744|PDB:2CND"
FT BINDING 447..449
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:7812715,
FT ECO:0007744|PDB:2CND"
FT BINDING 497
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:7812715,
FT ECO:0007744|PDB:2CND"
FT BINDING 500
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:7812715,
FT ECO:0007744|PDB:2CND"
FT SITE 593
FT /note="Necessary for efficient electron Transfer"
FT /evidence="ECO:0000269|PubMed:8188655"
FT DISULFID 138
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT MUTAGEN 593
FT /note="C->S: Reduction of activity."
FT /evidence="ECO:0000269|PubMed:7760334,
FT ECO:0000269|PubMed:8188655"
FT CONFLICT 459
FT /note="S -> G (in Ref. 1; AAA03202)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="L -> V (in Ref. 1; AAA03202)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="D -> Y (in Ref. 1; AAA03202)"
FT /evidence="ECO:0000305"
FT CONFLICT 560..562
FT /note="Missing (in Ref. 1; AAA03202)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT STRAND 364..375
FT /evidence="ECO:0007829|PDB:2CND"
FT STRAND 378..384
FT /evidence="ECO:0007829|PDB:2CND"
FT STRAND 399..406
FT /evidence="ECO:0007829|PDB:2CND"
FT STRAND 409..415
FT /evidence="ECO:0007829|PDB:2CND"
FT STRAND 425..432
FT /evidence="ECO:0007829|PDB:2CND"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:1CNF"
FT HELIX 447..454
FT /evidence="ECO:0007829|PDB:2CND"
FT STRAND 460..467
FT /evidence="ECO:0007829|PDB:2CND"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:2CND"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:2CND"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:2CND"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:2CND"
FT STRAND 488..495
FT /evidence="ECO:0007829|PDB:2CND"
FT HELIX 496..498
FT /evidence="ECO:0007829|PDB:2CND"
FT HELIX 499..511
FT /evidence="ECO:0007829|PDB:2CND"
FT TURN 512..515
FT /evidence="ECO:0007829|PDB:2CND"
FT STRAND 519..527
FT /evidence="ECO:0007829|PDB:2CND"
FT HELIX 529..531
FT /evidence="ECO:0007829|PDB:2CND"
FT HELIX 535..544
FT /evidence="ECO:0007829|PDB:2CND"
FT TURN 546..548
FT /evidence="ECO:0007829|PDB:2CND"
FT STRAND 549..556
FT /evidence="ECO:0007829|PDB:2CND"
FT HELIX 561..563
FT /evidence="ECO:0007829|PDB:2CND"
FT STRAND 567..571
FT /evidence="ECO:0007829|PDB:2CND"
FT HELIX 574..580
FT /evidence="ECO:0007829|PDB:2CND"
FT STRAND 585..593
FT /evidence="ECO:0007829|PDB:2CND"
FT HELIX 596..600
FT /evidence="ECO:0007829|PDB:2CND"
FT TURN 601..603
FT /evidence="ECO:0007829|PDB:2CND"
FT HELIX 604..608
FT /evidence="ECO:0007829|PDB:2CND"
FT TURN 609..611
FT /evidence="ECO:0007829|PDB:2CND"
FT HELIX 614..617
FT /evidence="ECO:0007829|PDB:2CND"
FT STRAND 618..620
FT /evidence="ECO:0007829|PDB:2CND"
SQ SEQUENCE 621 AA; 69773 MW; ACC276E4ED0FF5D3 CRC64;
GFPVRVIIPG CIGGRMVKWL KRIIVTPAES DNYYHFKDNR VLPSHVDAEL ANAEAWWYKP
EYIINELNIN SVITTPCHDE ILPINAFTTQ RPYTLKGYAY SGGGKKVTRV EVTLDGGETW
LVCTDHPEKP TKYGKYWCWC FWSLEVEVLD LLSAKEIAVR AWDESLNTQP EKLIWNVMGM
MNNCWFRVKT NVCKPHKGEI GIVFDHPTLP GNESGGWMAK EKHLETAEAA APGLKRSTST
PFMNTTDVGK EFTMSEVRKH ASQESAWIVV HGHVYDCTKF LKDHPGGADS ILINAGTDCT
EEFDAIHSDK AKALLDTYRI GELITTGTGY SSDNSVHGGS VLSHLAPIRR AVRAPALSNP
REKIHCRLVG KKELSRDVRL FRFSLPSPDQ VLGLPIGKHI FVCASIEGKL CMRAYTPTSM
VDEIGHFDLL VKVYFKNEHP KFPNGGLMTQ YLDSLPVGSY IDVKGPLGHV EYTGRGSFVI
NGKQRHASRL AMICGGSGIT PMYQIIQAVL RDQPEDHTEM HLVYANRTED DILLRDELDR
WAAEYPDRLK VWYVIDQVKR PEEGWKYSVG FVTEAVLREH VPEGGDDTLA LACGPPPMIQ
FAISPNLEKM KYDMANSFVV F
