ID NIA1_SOYBN Reviewed; 886 AA. AC P54233; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 16-JUN-2009, entry version 68. DE RecName: Full=Inducible nitrate reductase [NADH] 1; DE Short=NR; DE EC=1.7.1.1; GN Name=INR1; OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; OC Glycine. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Williams; TISSUE=Leaf; RX MEDLINE=96123229; PubMed=8534848; DOI=10.1007/BF00020980; RA Wu S., Lu Q., Kriz A.L., Harper J.E.; RT "Identification of cDNA clones corresponding to two inducible nitrate RT reductase genes in soybean: analysis in wild-type and nr1 mutant."; RL Plant Mol. Biol. 29:491-506(1995). 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L23854; AAA96727.1; -; mRNA. DR PIR; A59223; A59223. DR UniGene; Gma.1221; -. DR HSSP; P17571; 2CND. DR SMR; P54233; 632-886. DR BRENDA; 1.7.1.1; 299. 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; IEA:EC. DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. 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 2: Evidence at transcript level; KW Disulfide bond; FAD; Flavoprotein; Heme; Iron; Metal-binding; KW Molybdenum; NAD; Nitrate assimilation; Oxidoreductase. FT CHAIN 1 886 Inducible nitrate reductase [NADH] 1. FT /FTId=PRO_0000166069. FT DOMAIN 513 588 Cytochrome b5 heme-binding. FT DOMAIN 630 742 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 886 AA; 99799 MW; C18C73BDE3DE0614 CRC64; MAASVDNRQY GTHINAVVRA CGPDFNTPLP SDFDLDSSSD DEDQNDDASF LKELIQKANA ETEASLLDPR DEGTADQWIP RNASMVRFTG KHPFNGEGPL PRLMHHGFIT PSPLRYVRNH GPVPKIKWDE WTVEVTGLVK RSTHFTMEKL MREFPHREFP ATLVCAGNRR KEHNMVKQSI GFNWGAAGGS TSVWRGVPLR HVLKRCGILA RMKGAMYVSF EGAEDLPGGG GSKYGTSVKR EMAMDPSRDI ILAFMQNGEP LAPDHGFPVR MIIPGFIGGR MVKWLKRIVV TEHECDSHYH YKDNRVLPSH VDAELANDEG WWYKPEYIIN ELNINSVITT PCHEEILPIN SWTTQMPYFI RGYAYSGGGR KVTRVEVTLD GGGTWQVCTL DCPEKPNKYG KYWCWCFWSV EVEVLDLLGA REIAVRAWDE ALNTQPEKLI WNVMGMMNNC WFRVKTNVCR PHKGEIGIVF EHPTQPGNQS GGWMAKEKHL EKSSESNPTL KKSVSSPFMN TTSKTYTMSE VRRHNNADSA WIIVHGHVYD WTRFLKDHPG GTDRILINAG TDCTEEFEAI HSDKAKQMLE DYRIGELTTT CYNSDSSSSN PSVHGRSDTI PLTPIKEVIT PMRSVALIPR EKIPCKLISK TSISHDVRLF RFGLPSDGLL MGLAVGKHIF LCVTVDEKLC MRAYTPTSSV HEVGYFDLVV KVYFKGVHPK FPNGGIMSQH LDSLPIGSVL DVKGPLGHIE YTGRGNFLVH GKPRFATRLA MLAGGTGITP IYQVVQAILK DPEDCTEMHV VYANRTEDDI LLKEELDEWA KKYDRLKVWY VIQESIREGW EYSVGFITES ILTEHIPNAS PDTLALTCGP PPMIQFAVQP NLEKLGYDTQ NNLLVF //