NIA_CUCMA
ID NIA_CUCMA Reviewed; 918 AA.
AC P17569;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Nitrate reductase [NADH];
DE Short=NR;
DE EC=1.7.1.1;
OS Cucurbita maxima (Pumpkin) (Winter squash).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX NCBI_TaxID=3661;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16593773; DOI=10.1073/pnas.83.21.8073;
RA Crawford N.M., Campbell W.H., Davis R.;
RT "Nitrate reductase from squash: cDNA cloning and nitrate regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:8073-8076(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Seedling;
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).
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 -!- INDUCTION: By nitrate.
CC -!- SIMILARITY: Belongs to the nitrate reductase family. {ECO:0000305}.
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DR EMBL; M33154; AAA33114.1; -; mRNA.
DR PIR; A41667; A41667.
DR AlphaFoldDB; P17569; -.
DR SMR; P17569; -.
DR Proteomes; UP000504608; Unplaced.
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; Reference proteome.
FT CHAIN 1..918
FT /note="Nitrate reductase [NADH]"
FT /id="PRO_0000166055"
FT DOMAIN 543..618
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT DOMAIN 661..774
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 25..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 195
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 578
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 601
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 714..717
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 731..735
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 736
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P17571"
FT BINDING 743
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 748..750
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT BINDING 801
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A286R227"
FT DISULFID 434
FT /note="Interchain"
FT /evidence="ECO:0000255"
SQ SEQUENCE 918 AA; 103384 MW; A2CAFDDADEA1B2D1 CRC64;
MAASVDNRQY GPLQPPLSGV VRSFKNGPNH RADSPVRGCN FPNSNVDYNN NRPLKSSVKI
QEAAAEEMED SCSEDENENE FRDLIVKGNR ELEPSILDHR DEGTADNWIE RNASMVRLTG
KHPFNSEPPL NRLMHHGFIT PVPLHYVRNH GVVPKAKWAD WTVEVCGLVK RPAKFTMDQL
LNEFRFREFP ATLVCAGNRR KEQNMVKQSI GFNWGAAGVS TSVWRRVPLC DLLKRCGILS
RKKGALNVCF EGAEDLPGGG GSKYGTSIKK ELAMDPARDI ILAYMQNGEQ LAPDHGFPVR
MIIPGFIGGR MVKWLKRIIV TTKESENYYH FKDNRVLPSH VDADVANAEA WWYKPEHIIN
ELNINSVITT PCHEEILPIN AWTTQRPYTL RGYSYSGGGK KVTRVEVTMD SGETWQVCTL
DHPEKANKYG KYWCWCFWSL EVEVLDLLSA KEIAVRAWDE THNTQPEKLI WNLMGMMNNC
WFRVKTNMCK PHKGEIGIVF EHPTQPGNQS GGWMDRERHL EISTESNQTL KKSVSTPFMN
TASNTYTLSE VKKHNSPQSA WIIVHGHVYD CTRFLKDHPG GSDSILINAG TDCTEEFDAI
HSDKAKKMLE DYRIGELITT GYASDSSSNS PNNSTHGASN FSHLAPIREA PVSRRVALAP
NEKIPCKLIS KTSISHDVRV FRFALPGGQD QALGLPVGKH IFICATVDGK LCMRAYTPTS
SIDEMGFFEL VVKVYFKGVH PKFPNGGIMS QYLDSMEVGS TLDVKGPLGH IEYTGRGNFM
VHGKPRFARR LAMLAGGTGI TPIYQVVQAI LKDPEDETEM YVVYANRTED DILLRDELDT
WAKKNQRLKV WYVVQESIRE GWEYSVGFIT ENILREHIPA AAEDTLALAC GPPAMIQFAV
QPNLEKMNYD TKNSLLVF
