ID   NIR_MAIZE               Reviewed;         569 AA.
AC   P17847;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   04-NOV-2026, entry version 145.
DE   RecName: Full=Ferredoxin--nitrite reductase, chloroplastic;
DE            EC=1.7.7.1;
DE   Flags: Precursor; Fragment;
GN   Name=NIR;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16666376; DOI=10.1104/pp.88.3.741;
RA   Lahners K., Kramer V., Back E., Privalle L., Rothstein S.;
RT   "Molecular cloning of complementary DNA encoding maize nitrite reductase:
RT   molecular analysis and nitrate induction.";
RL   Plant Physiol. 88:741-746(1988).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6 oxidized [2Fe-2S]-[ferredoxin] + NH4(+) + 2 H2O = nitrite +
CC         6 reduced [2Fe-2S]-[ferredoxin] + 8 H(+); 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.
CC   -!- INDUCTION: By nitrate.
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA60450.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M23456; AAA60450.1; ALT_INIT; mRNA.
DR   PIR; JA0172; JA0172.
DR   AlphaFoldDB; P17847; -.
DR   SMR; P17847; -.
DR   FunCoup; P17847; 161.
DR   STRING; 4577.P17847; -.
DR   PaxDb; 4577-P17847; -.
DR   MaizeGDB; 69266; -.
DR   eggNOG; KOG0560; Eukaryota.
DR   InParanoid; P17847; -.
DR   OMA; AADITAC; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000007305; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0048307; F:ferredoxin-nitrite reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0010167; P:response to nitrate; IBA:GO_Central.
DR   Gene3D; 3.90.480.20; -; 1.
DR   Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 2.
DR   InterPro; IPR051329; NIR_SIR_4Fe-4S.
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   NCBIfam; NF007125; PRK09566.1; 1.
DR   PANTHER; PTHR32439; FERREDOXIN--NITRITE REDUCTASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR32439:SF0; FERREDOXIN--NITRITE REDUCTASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01077; NIR_SIR; 2.
DR   Pfam; PF03460; NIR_SIR_ferr; 2.
DR   PRINTS; PR00397; SIROHAEM.
DR   SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 2.
DR   SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 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   Reference proteome; Transit peptide; Transport.
FT   TRANSIT         <1..4
FT                   /note="Chloroplast"
FT   CHAIN           5..569
FT                   /note="Ferredoxin--nitrite reductase, chloroplastic"
FT                   /id="PRO_0000019705"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         447
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         453
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         488
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         492
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         492
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   569 AA;  63342 MW;  AA31738F2944CCE3 CRC64;
     IPGRTGRARA AVSVPPPAGE QVPTERLEPR VEERAGGYWV LKEKYRAGLN PQEKVKLEKE
     PMALFMEGGI QDLARVPMEQ IDAAKLTKDD VDVRLKWLGL FHRRKHQYGR FMMRLKLPNG
     VTTSEQTRYL ASVIEAYGAD GCADVTTRQN WQIRGVTLPD VPAILDGLRA VGLTSLQSGM
     DNVRNPVGNP LAGVDPHEIV DTRPYTNLLS SYVTNNSQGN PTITNLPRKW NVCVIGSHDL
     YEHPHINDLA YMPAVKDGEF GFNLLVGGFI SPKRWAEALP LDAWVAGDDV VPVCKAILEA
     YRDLGSRGNR QKTRMMWLID ELGMEVFRSE VEKRMPNGVL ERAAPEDLVD KRWERRDYLG
     VHPQKQEGLS YVGLHVPVGR LQAADMFELA RLADEYGTGE LRLTVEQNIV LPNVSNERLD
     ALLAEPLLQE QRLSPRPSML LRGLVACTGN QFCGQAIIET KARALQVARE VEKRVAVPRP
     VRMHWTGCPN SCGQVQVADI GFMGCLTKDS DGKIVEAADI FVGGRVGSDS HLADVYRKSV
     PCKDLVPIVA DLLVERFGAV PREREEDEE
//