NIA_PETHY
ID NIA_PETHY Reviewed; 909 AA.
AC P36859;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Nitrate reductase [NADH];
DE Short=NR;
DE EC=1.7.1.1;
GN Name=NIA;
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. TLRL13; TISSUE=Leaf;
RX PubMed=8514183; DOI=10.1016/0378-1119(93)90557-j;
RA Salanoubat M., Ha D.B.D.;
RT "Analysis of the petunia nitrate reductase apoenzyme-encoding gene: a first
RT step for sequence modification analysis.";
RL Gene 128:147-154(1993).
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 -!- ACTIVITY REGULATION: Regulated by the nitrogen source and controlled by
CC the circadian rhythm.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Maximum expression 2 hours after sunrise. Low
CC expression found 2 hours before and 8 hours after sunrise.
CC -!- SIMILARITY: Belongs to the nitrate reductase family. {ECO:0000305}.
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DR EMBL; L13691; AAA33713.1; -; Genomic_DNA.
DR AlphaFoldDB; P36859; -.
DR SMR; P36859; -.
DR PRIDE; P36859; -.
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..909
FT /note="Nitrate reductase [NADH]"
FT /id="PRO_0000166066"
FT DOMAIN 535..610
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT DOMAIN 652..764
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 187
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 570
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 593
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 704..707
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 721..725
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 726
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17571"
FT BINDING 733
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 738..740
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 791
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT DISULFID 426
FT /note="Interchain"
FT /evidence="ECO:0000255"
SQ SEQUENCE 909 AA; 102376 MW; 502C706F6E63E706 CRC64;
MAASVENRQF SHLEPGLSGV VRSFKPRSDS PVRGCNFPLN NELTNFQKKP NTTIYLDCSS
SEDDDDDDDK NEYLQMIRKG KLEVEPSVHD IRDEGTADNW IERNNSMIRL TGKHPFNSEP
PLARLMHHGF ITPVPLHYVR NHGPVPKGMW DDWTVEVTGL VKRPMKFTME QLVNEFPSRE
LPVTLVCAGN RRKEQNMVKQ TIGFNWGAAA VSTTVWRGVP LRAILKRCGI YSRTKGALNI
CFEGADVLPG GGGSKYGTSI KKEFAMDPSR DIIIAYMQNG EKLTPDHGFP LRMIIPGFIG
GRMVKWLKRI IVTTQESESY YHYKDNRVLP PHVDAELANA EAWWYKPEYI INELNINSVI
TTPCHEEILP INSWTTQRPY TLRGYSYSGG GKKVTRVEVT MDGGETWNVC TVDHPEKPNK
YGKYWCWCFW SLEVEVLDLL SAKEIAVRAW DETLNTQPEK LIWNVMGMMN NCWFRVKTNV
CKPHKGEIGI VFEHPTQPGN LSGGWMAKER HLEISAEAPP TLKKSISTPF MNTASKMYSM
SEVKKHNSAD SAWIIVHGHV YDATRFLKDH PGGIDSILIN AGTDCTEEFD AIHSDKAKKL
LEDFRIGELI TTGYTSDSSP NNSVHGSSSF SGFLAPIKEL APAVRSVALI PREKIPCKLV
DKKSISHDVR KFRFALPSED QVLGLPVGKH IFLCAIIDDK LCMRAYTPTS TVDEVGYFEL
VVKIYFKGIV PKFPNGGQMS QYLDSLPLGA FVDVKGPLGH IEYQGRGNFL VHGKRKFAKK
LAMLAGGTGI TPVYQVMQAI LKDPEDETEM HVVYANRTED DILLKDELDS WAVKLPERVK
VWYVVQDSIK EGWKYSTGFI TEAVLREHIP LPSQTTLALA CGPPPMIQFA VNPNLEKMGY
DIKDSLLVF
