NIR_ORYSJ
ID NIR_ORYSJ Reviewed; 596 AA.
AC Q42997; Q5ZBK4; Q7F475;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Ferredoxin--nitrite reductase, chloroplastic;
DE EC=1.7.7.1;
DE Flags: Precursor;
GN OrderedLocusNames=Os01g0357100, LOC_Os01g25484;
GN ORFNames=P0025H06.19-1, P0025H06.19-2;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Kinmaze; TISSUE=Leaf;
RX PubMed=8541663; DOI=10.1271/bbb.59.2183;
RA Terada Y., Aoki H., Tanaka T., Morikawa H., Ida S.;
RT "Cloning and nucleotide sequence of a leaf ferredoxin-nitrite reductase
RT cDNA of rice.";
RL Biosci. Biotechnol. Biochem. 59:2183-2185(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
CC -!- FUNCTION: Catalyzes the six-electron reduction of nitrite to ammonium.
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:0000305}.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD53072.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D50556; BAA09122.1; -; mRNA.
DR EMBL; AP003312; BAC10721.1; -; Genomic_DNA.
DR EMBL; AP003312; BAD53072.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JC4395; JC4395.
DR RefSeq; XP_015641702.1; XM_015786216.1.
DR AlphaFoldDB; Q42997; -.
DR SMR; Q42997; -.
DR STRING; 4530.OS01T0357100-02; -.
DR PaxDb; Q42997; -.
DR PRIDE; Q42997; -.
DR EnsemblPlants; Os01t0357100-01; Os01t0357100-01; Os01g0357100.
DR GeneID; 4326014; -.
DR Gramene; Os01t0357100-01; Os01t0357100-01; Os01g0357100.
DR KEGG; osa:4326014; -.
DR eggNOG; KOG0560; Eukaryota.
DR InParanoid; Q42997; -.
DR OrthoDB; 333458at2759; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR ExpressionAtlas; Q42997; baseline and differential.
DR Genevisible; Q42997; OS.
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 Reference proteome; Repeat; Transit peptide; Transport.
FT TRANSIT 1..28
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 29..596
FT /note="Ferredoxin--nitrite reductase, chloroplastic"
FT /id="PRO_0000247480"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 474
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 480
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 515
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 519
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 519
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 596 AA; 66143 MW; B69BC7FCD11390F5 CRC64;
MASSASLQRF LPPYPHAAAS RCRPPGVRAR PVQSSTVSAP SSSTPAADEA VSAERLEPRV
EQREGRYWVL KEKYRTGLNP QEKVKLGKEP MSLFMEGGIK ELAKMPMEEI EADKLSKEDI
DVRLKWLGLF HRRKHQYGRF MMRLKLPNGV TTSEQTRYLA SVIEAYGKEG CADVTTRQNW
QIRGVTLPDV PAILDGLNAV GLTSLQSGMD NVRNPVGNPL AGIDPDEIVD TRSYTNLLSS
YITSNFQGNP TITNLPRKWN VCVIGSHDLY EHPHINDLAY MPAVKGGKFG FNLLVGGFIS
PKRWEEALPL DAWVPGDDII PVCKAVLEAY RDLGTRGNRQ KTRMMWLIDE LGMEAFRSEV
EKRMPNGVLE RAAPEDLIDK KWQRRDYLGV HPQKQEGMSY VGLHVPVGRV QAADMFELAR
LADEYGSGEL RLTVEQNIVI PNVKNEKVEA LLSEPLLQKF SPQPSLLLKG LVACTGNQFC
GQAIIETKQR ALLVTSQVEK LVSVPRAVRM HWTGCPNSCG QVQVADIGFM GCLTKDSAGK
IVEAADIFVG GRVGSDSHLA GAYKKSVPCD ELAPIVADIL VERFGAVRRE REEDEE
