ID I0CCB0_CUCSA Unreviewed; 873 AA.
AC I0CCB0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=Nitrate reductase {ECO:0000256|PIRNR:PIRNR000233};
GN Name=NR3 {ECO:0000313|EMBL:AFH74423.1};
GN ORFNames=Csa_5G383350 {ECO:0000313|EMBL:KGN50981.1};
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659 {ECO:0000313|EMBL:AFH74423.1};
RN [1] {ECO:0000313|EMBL:KGN50981.1, ECO:0000313|Proteomes:UP000029981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX PubMed=19881527; DOI=10.1038/ng.475;
RA Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT "The genome of the cucumber, Cucumis sativus L.";
RL Nat. Genet. 41:1275-1281(2009).
RN [2] {ECO:0000313|EMBL:KGN50981.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19495411; DOI=10.1371/journal.pone.0005795;
RA Ren Y., Zhang Z., Liu J., Staub J.E., Han Y., Cheng Z., Li X., Lu J.,
RA Miao H., Kang H., Xie B., Gu X., Wang X., Du Y., Jin W., Huang S.;
RT "An integrated genetic and cytogenetic map of the cucumber genome.";
RL PLoS ONE 4:E5795-E5795(2009).
RN [3] {ECO:0000313|EMBL:KGN50981.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20565788; DOI=10.1186/1471-2164-11-384;
RA Guo S., Zheng Y., Joung J.G., Liu S., Zhang Z., Crasta O.R., Sobral B.W.,
RA Xu Y., Huang S., Fei Z.;
RT "Transcriptome sequencing and comparative analysis of cucumber flowers with
RT different sex types.";
RL BMC Genomics 11:384-384(2010).
RN [4] {ECO:0000313|EMBL:KGN50981.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22047402; DOI=10.1186/1471-2164-12-540;
RA Li Z., Zhang Z., Yan P., Huang S., Fei Z., Lin K.;
RT "RNA-Seq improves annotation of protein-coding genes in the cucumber
RT genome.";
RL BMC Genomics 12:540-540(2011).
RN [5] {ECO:0000313|EMBL:AFH74423.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Root {ECO:0000313|EMBL:AFH74423.1};
RA Reda M., Migocka M., Reder E.;
RT "Activity of nitrate reductase and expression of NR encoded genes in
RT cucumber under different nitrogen conditions.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:KGN50981.1}
RP NUCLEOTIDE SEQUENCE.
RA Huang S., Zhang Z., Lin K., Zhou Q.;
RL Submitted (OCT-2014) 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 {ECO:0000256|ARBA:ARBA00003838, ECO:0000256|PIRNR:PIRNR000233}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000256|PIRSR:PIRSR000233-1};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000256|PIRSR:PIRSR000233-1};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the nitrate reductase family.
CC {ECO:0000256|ARBA:ARBA00006253, ECO:0000256|PIRNR:PIRNR000233}.
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DR EMBL; JQ692875; AFH74423.1; -; mRNA.
DR EMBL; CM002926; KGN50981.1; -; Genomic_DNA.
DR RefSeq; NP_001267688.1; NM_001280759.1.
DR AlphaFoldDB; I0CCB0; -.
DR SMR; I0CCB0; -.
DR STRING; 3659.I0CCB0; -.
DR EnsemblPlants; KGN50981; KGN50981; Csa_5G383350.
DR GeneID; 101219242; -.
DR Gramene; KGN50981; KGN50981; Csa_5G383350.
DR KEGG; csv:101219242; -.
DR eggNOG; KOG0534; Eukaryota.
DR eggNOG; KOG0535; Eukaryota.
DR eggNOG; KOG0537; Eukaryota.
DR OMA; INEMSTN; -.
DR OrthoDB; 1239at2759; -.
DR Proteomes; UP000029981; Chromosome 5.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0009703; F:nitrate reductase (NADH) activity; IBA:GO_Central.
DR GO; GO:0050464; F:nitrate reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0042128; P:nitrate assimilation; IBA:GO_Central.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IBA:GO_Central.
DR CDD; cd06183; cyt_b5_reduct_like; 1.
DR CDD; cd02112; eukary_NR_Moco; 1.
DR Gene3D; 2.60.40.650; -; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 3.90.420.10; Oxidoreductase, molybdopterin-binding domain; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
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; PTHR19372:SF7; SULFITE OXIDASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR19372; SULFITE REDUCTASE; 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; PR00406; CYTB5RDTASE.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR PRINTS; PR00407; EUMOPTERIN.
DR PRINTS; PR00371; FPNCR.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF56524; Oxidoreductase molybdopterin-binding domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 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 {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000233-1};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505, ECO:0000256|PIRSR:PIRSR000233-
KW 1};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063,
KW ECO:0000256|PIRNR:PIRNR000233};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000029981}.
FT DOMAIN 518..593
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 617..729
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 492..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 177
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000256|PIRSR:PIRSR000233-1"
SQ SEQUENCE 873 AA; 98804 MW; FD1196D34484B217 CRC64;
MATAVNHKTL DLEPVSSTGN FPVQRCNSFR SNSFKFKRQA EKPLLIDDDD SSFDRDEENI
DYFRDLIRKG KEEIEPSILD PRDQGTADSG IMRNPCMVRL TGKHPFNSEP PLDHLMRHGF
ITPAPLHYVR NHGPVPKTDW SSWTIDVTGL VENPTSFTLD QLVNNFRSLE FPVTIMCSGN
RRKEQNMVKQ TIGFHWGAAV TSTSLWRGVP LREVLKRCGI FSRQRGALYV WMEGADNLPG
GGGCSYGTSI RREMAMDPSR DIIIAYKQNG DPLPPDHGFP VRMIVPGFTG GRMVKWLKRI
IVTNRESDNY YHFMDNRVLP SHVDSSELAH AEGWWYKPEY VIYEMNINSV ITTPSHNETL
LINSETTLST YTLRGYAYSG GGKKVTRVQV TLDGGETWKI CNLEYHEKPN KYGKYWCWIF
WSVDVEILDL FGSKQIAVRA WDETTNTQPE NLNWNLMGMM NNSWYRIKIN ICKPQKGEIG
IVFRHPTVAG NNAGGWQEKD KPNPTDESPS QQKDNKSTTT FSMSEVKTHN SSESAWIVVQ
NHVYDCTPFL KDHPGGADSI LINAGTDCTE EFEAIHSDKA IKMLEDYKIG DLLILNDNKD
ATSSPKAVTQ HVALIPREKI PVKLISKTTI SHNTRIFRFG LSSEDQRLGL PVGKHIFLCA
NVDGKLCMRA YTPSSAVDQT GYFDLVVKIY FKNVHPDFPN GGLMSQYLDS LPLGSMVEVK
GPLGHIEYMG RGNFRVNGKP RLAKKLAMVA GGTGITPIYQ VVQAILKDPE DETEMFVVYA
NRSEEDILLR EELETWAKEN ERLKIWYVVK DGVQEGWPYS VGYIREDILR EHIPMGSPQT
LALVCGPPPM IELTVKPILK NLEYDLEGSL LVF
//
