NIR_SPIOL
ID NIR_SPIOL Reviewed; 594 AA.
AC P05314;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Ferredoxin--nitrite reductase, chloroplastic;
DE EC=1.7.7.1;
DE Flags: Precursor;
GN Name=NIR;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3163766; DOI=10.1007/bf00322440;
RA Back E., Burkhart W., Moyer M., Privalle L., Rothstein S.;
RT "Isolation of cDNA clones coding for spinach nitrite reductase: complete
RT sequence and nitrate induction.";
RL Mol. Gen. Genet. 212:20-26(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Dark green Bloomsdale; TISSUE=Leaf;
RX PubMed=1868226; DOI=10.1007/bf00036801;
RA Back E., Dunne W., Schneiderbauer A., de Framond A., Rastogi R.,
RA Rothstein S.J.;
RT "Isolation of the spinach nitrite reductase gene promoter which confers
RT nitrate inducibility on GUS gene expression in transgenic tobacco.";
RL Plant Mol. Biol. 17:9-18(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), IRON-CLUSTER BINDING AT CYS-473;
RP CYS-479; CYS-514 AND CYS-518, AND HEME BINDING AT CYS-518.
RX PubMed=16331965; DOI=10.1021/bi050981y;
RA Swamy U., Wang M., Tripathy J.N., Kim S.K., Hirasawa M., Knaff D.B.,
RA Allen J.P.;
RT "Structure of spinach nitrite reductase: implications for multi-electron
RT reactions by the iron-sulfur:siroheme cofactor.";
RL Biochemistry 44:16054-16063(2005).
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.
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; X07568; CAA30453.1; -; mRNA.
DR EMBL; X17031; CAA34893.1; -; Genomic_DNA.
DR PIR; S16603; S16603.
DR PDB; 2AKJ; X-ray; 2.80 A; A=33-594.
DR PDBsum; 2AKJ; -.
DR AlphaFoldDB; P05314; -.
DR SMR; P05314; -.
DR PRIDE; P05314; -.
DR OrthoDB; 333458at2759; -.
DR BRENDA; 1.7.7.1; 5812.
DR UniPathway; UPA00653; -.
DR EvolutionaryTrace; P05314; -.
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 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Chloroplast; Direct protein sequencing;
KW Electron transport; Heme; Iron; Iron-sulfur; Metal-binding;
KW Nitrate assimilation; Oxidoreductase; Plastid; Transit peptide; Transport.
FT TRANSIT 1..32
FT /note="Chloroplast"
FT CHAIN 33..594
FT /note="Ferredoxin--nitrite reductase, chloroplastic"
FT /id="PRO_0000019706"
FT REGION 13..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 473
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 479
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 514
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 518
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 518
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 VARIANT 221
FT /note="I -> V (probable allelic variation)"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:2AKJ"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 78..85
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:2AKJ"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:2AKJ"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:2AKJ"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:2AKJ"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:2AKJ"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:2AKJ"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:2AKJ"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:2AKJ"
FT TURN 217..221
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 230..240
FT /evidence="ECO:0007829|PDB:2AKJ"
FT TURN 241..245
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:2AKJ"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:2AKJ"
FT STRAND 274..293
FT /evidence="ECO:0007829|PDB:2AKJ"
FT STRAND 306..313
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 317..331
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 342..349
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 351..359
FT /evidence="ECO:0007829|PDB:2AKJ"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:2AKJ"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 410..423
FT /evidence="ECO:0007829|PDB:2AKJ"
FT STRAND 424..431
FT /evidence="ECO:0007829|PDB:2AKJ"
FT TURN 432..434
FT /evidence="ECO:0007829|PDB:2AKJ"
FT STRAND 435..442
FT /evidence="ECO:0007829|PDB:2AKJ"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 446..449
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 453..456
FT /evidence="ECO:0007829|PDB:2AKJ"
FT TURN 465..468
FT /evidence="ECO:0007829|PDB:2AKJ"
FT STRAND 469..472
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 475..477
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 487..500
FT /evidence="ECO:0007829|PDB:2AKJ"
FT STRAND 508..514
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:2AKJ"
FT STRAND 524..534
FT /evidence="ECO:0007829|PDB:2AKJ"
FT STRAND 540..548
FT /evidence="ECO:0007829|PDB:2AKJ"
FT STRAND 560..567
FT /evidence="ECO:0007829|PDB:2AKJ"
FT TURN 568..570
FT /evidence="ECO:0007829|PDB:2AKJ"
FT HELIX 571..582
FT /evidence="ECO:0007829|PDB:2AKJ"
SQ SEQUENCE 594 AA; 66394 MW; 2B3DCAAC16DE06A3 CRC64;
MASLPVNKII PSSTTLLSSS NNNRRRNNSS IRCQKAVSPA AETAAVSPSV DAARLEPRVE
ERDGFWVLKE EFRSGINPAE KVKIEKDPMK LFIEDGISDL ATLSMEEVDK SKHNKDDIDV
RLKWLGLFHR RKHHYGRFMM RLKLPNGVTT SEQTRYLASV IKKYGKDGCA DVTTRQNWQI
RGVVLPDVPE IIKGLESVGL TSLQSGMDNV RNPVGNPLAG IDPHEIVDTR PFTNLISQFV
TANSRGNLSI TNLPRKWNPC VIGSHDLYEH PHINDLAYMP ATKNGKFGFN LLVGGFFSIK
RCEEAIPLDA WVSAEDVVPV CKAMLEAFRD LGFRGNRQKC RMMWLIDELG MEAFRGEVEK
RMPEQVLERA SSEELVQKDW ERREYLGVHP QKQQGLSFVG LHIPVGRLQA DEMEELARIA
DVYGSGELRL TVEQNIIIPN VENSKIDSLL NEPLLKERYS PEPPILMKGL VACTGSQFCG
QAIIETKARA LKVTEEVQRL VSVTRPVRMH WTGCPNSCGQ VQVADIGFMG CMTRDENGKP
CEGADVFVGG RIGSDSHLGD IYKKAVPCKD LVPVVAEILI NQFGAVPRER EEAE
