ID   NIA2_ARATH              Reviewed;         917 AA.
AC   P11035; Q7Y260;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   16-JUN-2009, entry version 102.
DE   RecName: Full=Nitrate reductase [NADH] 2;
DE            Short=NR2;
DE            EC=1.7.1.1;
GN   Name=NIA2; Synonyms=CHL3; OrderedLocusNames=At1g37130;
GN   ORFNames=F28L22.2;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=88276888; PubMed=3393528; DOI=10.1073/pnas.85.14.5006;
RA   Crawford N.M., Smith M., Bellissimo D.B., Davis R.W.;
RT   "Sequence and nitrate regulation of the Arabidopsis thaliana mRNA
RT   encoding nitrate reductase, a metalloflavoprotein with three
RT   functional domains.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:5006-5010(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 350-422.
RX   MEDLINE=93005711; PubMed=1840922; DOI=10.1105/tpc.3.5.461;
RA   Wilkinson J.Q., Crawford N.M.;
RT   "Identification of the Arabidopsis CHL3 gene as the nitrate reductase
RT   structural gene NIA2.";
RL   Plant Cell 3:461-471(1991).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 522-917.
RX   MEDLINE=89091069; PubMed=2905260;
RA   Cheng C., Dewdney J., Nam H., den Boer B.G.W., Goodman H.M.;
RT   "A new locus (NIA 1) in Arabidopsis thaliana encoding nitrate
RT   reductase.";
RL   EMBO J. 7:3309-3314(1988).
RN   [6]
RP   HERBICIDE RESISTANCE.
RX   MEDLINE=93287999; PubMed=8510658;
RA   Wilkinson J.Q., Crawford N.M.;
RT   "Identification and characterization of a chlorate-resistant mutant of
RT   Arabidopsis thaliana with mutations in both nitrate reductase
RT   structural genes NIA1 and NIA2.";
RL   Mol. Gen. Genet. 239:289-297(1993).
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.
CC   -!- TISSUE SPECIFICITY: Root, leaf, and shoot.
CC   -!- MISCELLANEOUS: When mutated confers resistance to the herbicide
CC       chlorate.
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; J03240; AAA32830.1; -; mRNA.
DR   EMBL; AC007505; AAF19225.1; -; Genomic_DNA.
DR   EMBL; AF367272; AAK56261.1; -; mRNA.
DR   EMBL; AF436835; AAL32017.1; -; mRNA.
DR   EMBL; AY037183; AAK59768.1; -; mRNA.
DR   EMBL; AY039914; AAK64018.1; -; mRNA.
DR   EMBL; AY133530; AAM91360.1; -; mRNA.
DR   EMBL; AY142568; AAN13137.1; -; mRNA.
DR   EMBL; S45385; AAL32273.1; -; Genomic_DNA.
DR   EMBL; X13435; CAA31787.1; -; mRNA.
DR   IPI; IPI00544857; -.
DR   PIR; A31821; RDMUNH.
DR   RefSeq; NP_174901.1; -.
DR   UniGene; At.23731; -.
DR   UniGene; At.72953; -.
DR   HSSP; P17571; 2CND.
DR   PRIDE; P11035; -.
DR   ProMEX; P11035; -.
DR   GeneID; 840630; -.
DR   GenomeReviews; CT485782_GR; AT1G37130.
DR   KEGG; ath:AT1G37130; -.
DR   TAIR; At1g37130; -.
DR   OMA; P11035; CHEEILP.
DR   BRENDA; 1.7.1.1; 302.
DR   GermOnline; AT1G37130; Arabidopsis thaliana.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0005773; C:vacuole; IDA:TAIR.
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:0030151; F:molybdenum ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009703; F:nitrate reductase (NADH) activity; IDA:TAIR.
DR   GO; GO:0042128; P:nitrate assimilation; IMP:TAIR.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; IMP:TAIR.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR   GO; GO:0009416; P:response to light stimulus; IMP:TAIR.
DR   GO; GO:0009610; P:response to symbiotic fungus; IEP:TAIR.
DR   InterPro; IPR001199; Cyt_B5.
DR   InterPro; IPR018506; Cyt_B5_heme-BS.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR005066; MoCF_OxRdtse_dimer.
DR   InterPro; IPR008335; Mopterin_OxRdtase_euk.
DR   InterPro; IPR001834; NADH-Cyt_B5_reductase.
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   1: Evidence at protein level;
KW   Complete proteome; Disulfide bond; FAD; Flavoprotein; Heme;
KW   Herbicide resistance; Iron; Metal-binding; Molybdenum; NAD;
KW   Nitrate assimilation; Oxidoreductase.
FT   CHAIN         1    917       Nitrate reductase [NADH] 2.
FT                                /FTId=PRO_0000166050.
FT   DOMAIN      542    617       Cytochrome b5 heme-binding.
FT   DOMAIN      660    772       FAD-binding FR-type.
FT   METAL       191    191       Molybdenum-pterin (Potential).
FT   METAL       245    245       Molybdenum-pterin (Potential).
FT   METAL       577    577       Iron (heme axial ligand) (By similarity).
FT   METAL       600    600       Iron (heme axial ligand) (By similarity).
FT   DISULFID    433    433       Interchain (Potential).
SQ   SEQUENCE   917 AA;  102844 MW;  B8909A318C04C39A CRC64;
     MAASVDNRQY ARLEPGLNGV VRSYKPPVPG RSDSPKAHQN QTTNQTVFLK PAKVHDDDED
     VSSEDENETH NSNAVYYKEM IRKSNAELEP SVLDPRDEYT ADSWIERNPS MVRLTGKHPF
     NSEAPLNRLM HHGFITPVPL HYVRNHGHVP KAQWAEWTVE VTGFVKRPMK FTMDQLVSEF
     AYREFAATLV CAGNRRKEQN MVKKSKGFNW GSAGVSTSVW RGVPLCDVLR RCGIFSRKGG
     ALNVCFEGSE DLPGGAGTAG SKYGTSIKKE YAMDPSRDII LAYMQNGEYL TPDHGFPVRI
     IIPGFIGGRM VKWLKRIIVT TKESDNFYHF KDNRVLPSLV DAELADEEGW WYKPEYIINE
     LNINSVITTP CHEEILPINA FTTQRPYTLK GYAYSGGGKK VTRVEVTVDG GETWNVCALD
     HQEKPNKYGK FWCWCFWSLE VEVLDLLSAK EIAVRAWDET LNTQPEKMIW NLMGMMNNCW
     FRVKTNVCKP HKGEIGIVFE HPTLPGNESG GWMAKERHLE KSADAPPSLK KSVSTPFMNT
     TAKMYSMSEV KKHNSADSCW IIVHGHIYDC TRFLMDHPGG SDSILINAGT DCTEEFEAIH
     SDKAKKMLED YRIGELITTG YSSDSSSPNN SVHGSSAVFS LLAPIGEATP VRNLALVNPR
     AKVPVQLVEK TSISHDVRKF RFALPVEDMV LGLPVGKHIF LCATINDKLC LRAYTPSSTV
     DVVGYFELVV KIYFGGVHPR FPNGGLMSQY LDSLPIGSTL EIKGPLGHVE YLGKGSFTVH
     GKPKFADKLA MLAGGTGITP VYQIIQAILK DPEDETEMYV IYANRTEEDI LLREELDGWA
     EQYPDRLKVW YVVESAKEGW AYSTGFISEA IMREHIPDGL DGSALAMACG PPPMIQFAVQ
     PNLEKMQYNI KEDFLIF
//