ID   NIA2_PHAVU              Reviewed;         890 AA.
AC   P39866;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-NOV-2008, entry version 60.
DE   RecName: Full=Nitrate reductase [NADH] 2;
DE            Short=NR-2;
DE            EC=1.7.1.1;
GN   Name=NIA2; Synonyms=NR2;
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae;
OC   Phaseolus.
OX   NCBI_TaxID=3885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Saxa;
RA   Jensen P.E., Hoff T., Stummann B.M., Henningsen K.W.;
RL   Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
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.
CC   -!- COFACTOR: Binds 1 heme group. The heme group is called cytochrome
CC       b-557.
CC   -!- COFACTOR: Binds 1 molybdenum ion.
CC   -!- SUBUNIT: Homodimer (By similarity).
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; U01029; AAA95940.1; -; Unassigned_DNA.
DR   PIR; T11805; T11805.
DR   HSSP; P17571; 2CND.
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   3: Inferred from homology;
KW   FAD; Flavoprotein; Heme; Iron; Metal-binding; Molybdenum; NAD;
KW   Nitrate assimilation; Oxidoreductase.
FT   CHAIN         1    890       Nitrate reductase [NADH] 2.
FT                                /FTId=PRO_0000166068.
FT   DOMAIN      513    588       Cytochrome b5 heme-binding.
FT   DOMAIN      634    746       FAD-binding FR-type.
FT   METAL       165    165       Molybdenum-pterin (Potential).
FT   METAL       219    219       Molybdenum-pterin (Potential).
FT   METAL       548    548       Iron (heme axial ligand) (By similarity).
FT   METAL       571    571       Iron (heme axial ligand) (By similarity).
FT   DISULFID    404    404       Interchain (Potential).
SQ   SEQUENCE   890 AA;  99995 MW;  FC03B96F0139DE1E CRC64;
     MAASVGNRQF ATHMNGVVRS CGQDLKPSLP LDFDLDSSSS DDDENDDASY LKELVRKANA
     ETEASVMDPR DEGTADQWVA RNASMVRLTG KHPFNAESPL QRLMHHGFIT PVPLHYVRNH
     GPVPKANWED WTVEITGLVK RPTRFTMDRL VREFPHREFP ATLVCAGNRR KEQNMVKKTI
     GFNWGSAGTS TSVWRGVPVR HVLRRCGILT RGKGALHVSF EGAENLPGGG GSKYGTSISR
     EMAMDPSRDI ILAYMQNGEP LAPDHGFPIR MIIPGFIGGR MVKWLKRIVV TEQECESHYH
     YKDNRVLPSH VDPELANEEG WWFKPEYIIN ELNINSVITT PCHDEILPIN SWTTQRPYVV
     RGYAYSGGGR KVTRVEVTLD GGETWHVCTL DHPEKPNKYG KYWCWCFWSL EVEVLDLLGT
     KEIAVRAWDE GLNTQPENLI WNLMGMMNNC WFRVKTNVCK PHKGEIGIVF EHPTQPGNQP
     GGWMAKEKHL EQSQEAKPSL KKSVSTPFMN TASKMFSVSE VKKHSSPDSA WIIVHGHVYD
     CTRFLKDHPG GTDSILINAG TDCTEEFDAI HSDKAKKMLE DYRIGELITT GYTSADSSPN
     NSVHGNSEFI HLAPINEITT IPPLPPRSVA LNPRQKIPCK LVSKTSISHD VRLFRFEMPS
     KNQLLGLPVG KHIFLCATID GKLCMRAYTP TSSVEEVGFF DLLIKVYFKD VHPKFPNGGL
     MSQYLESLSI GSMLDVKGPL GHIEYTGRGN FTVNGKSRFA KRLAMLAGGT GITPIYQVAQ
     AILKDPEDLT EMHVVYANRT EDDILLREEL DTWAKEHCER FKVWYVVETA KEGWGYGVGF
     ITEAIMREHL PEASSDSLAM TCGPPPMIQF AVQPNLEKMG YDIKNDLLVF
//