ID   NIR_BETPN               Reviewed;         583 AA.
AC   P38500;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Ferredoxin--nitrite reductase, chloroplastic;
DE            EC=1.7.7.1;
DE   Flags: Precursor;
GN   Name=NIR1;
OS   Betula pendula (European white birch) (Betula verrucosa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Betulaceae; Betula.
OX   NCBI_TaxID=3505;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   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 pendula
RT   and identification of conserved protein regions.";
RL   Mol. Gen. Genet. 231:411-416(1992).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O + NH4(+) + 6 oxidized [2Fe-2S]-[ferredoxin] = 8 H(+) +
CC         nitrite + 6 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:18041,
CC         Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.7.7.1;
CC   -!- COFACTOR:
CC       Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC       Note=Binds 1 siroheme per subunit.;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC   -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- INDUCTION: By nitrate.
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC       family. {ECO:0000305}.
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DR   EMBL; X60093; CAA42690.1; -; mRNA.
DR   PIR; S20495; S20495.
DR   AlphaFoldDB; P38500; -.
DR   SMR; P38500; -.
DR   PRIDE; P38500; -.
DR   UniPathway; UPA00653; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0048307; F:ferredoxin-nitrite reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.413.10; -; 2.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR   InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR   InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR   InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR   Pfam; PF01077; NIR_SIR; 2.
DR   Pfam; PF03460; NIR_SIR_ferr; 2.
DR   PRINTS; PR00397; SIROHAEM.
DR   SUPFAM; SSF55124; SSF55124; 2.
DR   SUPFAM; SSF56014; SSF56014; 2.
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
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..583
FT                   /note="Ferredoxin--nitrite reductase, chloroplastic"
FT                   /id="PRO_0000019704"
FT   BINDING         461
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         467
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         502
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         506
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         506
FT                   /ligand="siroheme"
FT                   /ligand_id="ChEBI:CHEBI:60052"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
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