ID   NIA_CICIN               Reviewed;         920 AA.
AC   P43101;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-NOV-2008, entry version 64.
DE   RecName: Full=Nitrate reductase [NADH];
DE            Short=NR;
DE            EC=1.7.1.1;
GN   Name=NIA;
OS   Cichorium intybus (Chicory).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; campanulids; Asterales; Asteraceae; Cichorioideae;
OC   Cichorieae; Cichorium.
OX   NCBI_TaxID=13427;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=cv. Witloof; TISSUE=Leaf, and Root;
RX   MEDLINE=97141273; PubMed=8987617; DOI=10.1007/BF00196644;
RA   Palms B., Goupil P., de Almeida Engler J., Van der Straeten D.,
RA   Van Montagu M., Rambour S.;
RT   "Evidence for the nitrate-dependent spatial regulation of the nitrate
RT   reductase gene in chicory roots.";
RL   Planta 200:20-27(1996).
CC   -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first
CC       step of nitrate assimilation in plants, fungi and bacteria.
CC   -!- CATALYTIC ACTIVITY: Nitrite + NAD(+) + H(2)O = nitrate + NADH.
CC   -!- COFACTOR: Binds 1 FAD per subunit.
CC   -!- COFACTOR: Binds 1 heme group per subunit.
CC   -!- COFACTOR: Binds 1 molybdenum-pterin group per subunit.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- TISSUE SPECIFICITY: In cortical cells of roots grown at low
CC       nitrate concentrations, in vascular tissues of roots at high
CC       nitrate concentrations and in root apex under both conditions.
CC   -!- SIMILARITY: Belongs to the nitrate reductase family.
CC   -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
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DR   EMBL; X84103; CAA58909.1; -; Genomic_DNA.
DR   EMBL; X84102; CAA58908.1; -; mRNA.
DR   PIR; S52301; S52301.
DR   HSSP; P17571; 2CND.
DR   SMR; P43101; 665-920.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0009703; F:nitrate reductase (NADH) activity; IEA:EC.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001199; Cyt_B5.
DR   InterPro; IPR001834; Cyt_B5_reductase.
DR   InterPro; IPR001709; FPN_cyt_redctse.
DR   InterPro; IPR005066; MoCF_OxRdtse_dimer.
DR   InterPro; IPR008335; Mopterin_OxRdtase_euk.
DR   InterPro; IPR012137; Nitr_rd_NADH.
DR   InterPro; IPR008333; OxRdtase_FAD-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD_bd.
DR   InterPro; IPR000572; OxRdtase_Mopterin-bd.
DR   Gene3D; G3DSA:3.10.120.10; Cyt_B5; 1.
DR   Gene3D; G3DSA:2.60.40.650; MoCF_oxrdtse_dimer; 1.
DR   Gene3D; G3DSA:3.90.420.10; Oxred_molyb_bd; 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   ProDom; PD000612; Cyt_B5; 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   FAD; Flavoprotein; Heme; Iron; Metal-binding; Molybdenum; NAD;
KW   Nitrate assimilation; Oxidoreductase.
FT   CHAIN         1    920       Nitrate reductase [NADH].
FT                                /FTId=PRO_0000166054.
FT   DOMAIN      534    609       Cytochrome b5 heme-binding.
FT   DOMAIN      663    775       FAD-binding FR-type.
FT   METAL       185    185       Molybdenum-pterin (Potential).
FT   METAL       239    239       Molybdenum-pterin (Potential).
FT   METAL       569    569       Iron (heme axial ligand) (By similarity).
FT   METAL       592    592       Iron (heme axial ligand) (By similarity).
FT   DISULFID    424    424       Interchain (Potential).
SQ   SEQUENCE   920 AA;  103520 MW;  FE1E332CCC9A4D58 CRC64;
     MAASVENRQF RHEPGLSAAG VVRSFSPNHR RSDSPIRNCN YPAAAREFMT PKKLPPETYD
     TSDDEEDEAD YRDAIKKSNS ELESSVFDPR DQGTADQWIE RNPSMVRLTG KHPFNSEPPL
     NKLMQHGFIT PDPLHYVRNH GPVPNATWED WTVEICGLVK RPARFSMTQL VNEFPSREFP
     VTLVCAGNRR KEQNLTKQTI GFNWGAAGIS TSVWKGVPLV HILKRCGIYS RKKGALNVCF
     EGAEDLPGGG GSKYGTSIKI EMAMDPARDI ILAYMQNGEK LSPDHGFPVR MIIPGFIGGR
     MVKWLKRIIV TTPESESYYH FKDNRVLPSH VDAELANSEG WWYKPEYIIN ELNINSVITT
     PCHEEILPIN SWTTQRPYTL RGYAYSGGGK KVTRVEVTMD GGETWNVCTL DHKEKPTRYA
     KYWCWCFWSL EVEVLDLLSA KEIAVRAWDE TLNTQPDKLI WNLMGMMNNC WFRVKTNMCK
     PHKGEIGIVF EHPTQPGNQS GGWMAREKHL EISSELAHPT LKKSVSSPFM NTTSLTFTMS
     EVKKHNSADS AWIVVHGHIY DCTSFLKDHP GGSDSILLNA GTDCTEEFDA IHSDKAKKLL
     EEYRVGELIT MGYSSDSAAS SPNNSVHGAT NYLTLHLSLA TIKEIAPTRS VALIPKEIAP
     TRREKIPCKL ISKTSVSHDV RLFRFALPSP DQVLGLPVGK HVFVCATIDD KLCMRAYTPT
     STIDEVGYFE LLVKIYFKGV EPKFPNGGLM SQHLESMELG SSIEIKGPLG HIEYMGRGTF
     SVHGKQKFAR KLAMFAGGTG ITPDLSSDAS YLKDPEDDTE MYVVYANRTE DDILLREELD
     AWADKYSDRV KVWYVVAKSI REGWKYSEGF ITEDIMREHV PEVSEDTLAL ACGPPPMIQF
     AINPNLEKMG YDIKNSLLVF
//