ID NIR_BETVE Reviewed; 583 AA. AC P38500; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 25-NOV-2008, entry version 64. DE RecName: Full=Ferredoxin--nitrite reductase, chloroplastic; DE EC=1.7.7.1; DE Flags: Precursor; GN Name=NIR1; OS Betula verrucosa (White birch) (Betula pendula). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Fagales; Betulaceae; Betula. OX NCBI_TaxID=3505; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Leaf; RX MEDLINE=92167960; PubMed=1347145; DOI=10.1007/BF00292710; RA Friemann A., Brinkmann K., Hachtel W.; RT "Sequence of a cDNA encoding nitrite reductase from the tree Betula RT pendula and identification of conserved protein regions."; RL Mol. Gen. Genet. 231:411-416(1992). CC -!- CATALYTIC ACTIVITY: NH(3) + 2 H(2)O + 6 oxidized ferredoxin = CC nitrite + 6 reduced ferredoxin + 7 H(+). CC -!- COFACTOR: Binds 1 siroheme per subunit. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity). CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation). CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast (By similarity). CC -!- INDUCTION: By nitrate. CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S CC domain family. 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; X60093; CAA42690.1; -; mRNA. DR PIR; S20495; S20495. DR SMR; P38500; 42-576. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0048307; F:ferredoxin-nitrite reductase activity; IEA:EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR006066; Nir_Si_BS. DR InterPro; IPR006067; Nir_Sir_4Fe4S. DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer. DR Pfam; PF01077; NIR_SIR; 1. DR Pfam; PF03460; NIR_SIR_ferr; 2. DR PRINTS; PR00397; SIROHAEM. DR PROSITE; PS00365; NIR_SIR; 1. PE 2: Evidence at transcript level; KW 4Fe-4S; Chloroplast; Electron transport; Heme; Iron; Iron-sulfur; KW Metal-binding; Nitrate assimilation; Oxidoreductase; Plastid; KW Transit peptide; Transport. FT TRANSIT 1 22 Chloroplast (Potential). FT CHAIN 23 583 Ferredoxin--nitrite reductase, FT chloroplastic. FT /FTId=PRO_0000019704. FT METAL 461 461 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 467 467 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 502 502 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 506 506 Iron (siroheme axial ligand) (By FT similarity). FT METAL 506 506 Iron-sulfur (4Fe-4S) (By similarity). SQ SEQUENCE 583 AA; 65229 MW; 482111EF7E66991F CRC64; MSSLSVRFLS PPLFSSTPAW PRTGLAATQA VPPVVAEVDA GRLEPRVEER EGYWVLKEKF REGINPQEKL KLEREPMKLF MEGGIEDLAK MSLEEIDKDK ISKSDIDVRL KWLGLFHRRK HHYGRFMMRL KLPNGVTTSA QTRYLASVIR KYGKDGCADV TTRQNWQIRG VVLSDVPEIL KGLDEVGLTS LQSGMDNVRN PVGNPLAGID IHEIVATRPY NNLLSQFITA NSRGNLAFTN LPRKWNVCVV GSHDLFEHPH INDLAYMPAI KDGRFGFNLL VGGFFSPRRC AEAVPLDAWV SADDIILVCK AILEAYRDLG TRGNRQKTRM MWLIDELGIE GFRSEVVKRM PNQELERAAP EDLIEKQWER RELIGVHPQK QEGLSYVGLH IPVGRVQADD MDELARLADT YGCGELRLTV EQNIIIPNIE NSKLEALLGE PLLKDRFSPE PPILMKGLVA CTGNQFCGQA IIETKARALK VTEEVQRQVA VTRPVRMHWT GCPNSCGQVQ VADIGFMGCM ARDENGKPCE GAAVFLGGRI GSDSHLGNLY KKGVPCKNLV PLVVDILVKH FGAVPREREE SED //