ID   NIR_PINSY               Reviewed;         105 AA.
AC   Q43090;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Ferredoxin--nitrite reductase, chloroplastic;
DE            EC=1.7.7.1;
DE   AltName: Full=PSNiR;
DE            Short=NiR;
DE   Flags: Fragment;
GN   Name=NIR;
OS   Pinus sylvestris (Scotch pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=3349;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Black forest provenance;
RX   PubMed=8049370; DOI=10.1007/bf00043873;
RA   Neininger A., Seith B., Hoch B., Mohr H.;
RT   "Gene expression of nitrite reductase in Scots pine (Pinus sylvestris L.)
RT   as affected by light and nitrate.";
RL   Plant Mol. Biol. 25:449-457(1994).
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; Evidence={ECO:0000250};
CC       Note=Binds 1 siroheme per subunit. {ECO:0000250};
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highest expression in roots and hypocotyls. Some
CC       expression in cotyledonary whorls. {ECO:0000269|PubMed:8049370}.
CC   -!- INDUCTION: Strong induction by nitrate in roots and hypocotyls. Strong
CC       induction by light and weak induction by nitrate in cotyledonary
CC       whorls. {ECO:0000269|PubMed:8049370}.
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X74949; CAA52905.1; -; mRNA.
DR   PIR; S46311; S46311.
DR   AlphaFoldDB; Q43090; -.
DR   SMR; Q43090; -.
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; -; 1.
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; 1.
DR   SUPFAM; SSF56014; SSF56014; 1.
DR   PROSITE; PS00365; NIR_SIR; 1.
PE   2: Evidence at transcript level;
KW   4Fe-4S; Chloroplast; Heme; Iron; Iron-sulfur; Metal-binding;
KW   Nitrate assimilation; Oxidoreductase; Plastid.
FT   CHAIN           <1..105
FT                   /note="Ferredoxin--nitrite reductase, chloroplastic"
FT                   /id="PRO_0000199955"
FT   BINDING         28
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         32
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         32
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"
FT   NON_TER         1
SQ   SEQUENCE   105 AA;  11597 MW;  1A9E45BF8846017E CRC64;
     KARALKITEE LDRTMEVPKP VRMHWTGCPN TCAQVQVADI GFMGCMTRDE NKKVVEGVDI
     FIGGRVGADS HLGDLIHKGV PCKDVVPVVQ ELLIKHFGAI RKTNM