NIR_PHOLA
ID NIR_PHOLA Reviewed; 510 AA.
AC Q51879;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Ferredoxin--nitrite reductase;
DE EC=1.7.7.1;
GN Name=nirA; Synonyms=nir;
OS Phormidium laminosum.
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Oscillatoriaceae; Phormidium.
OX NCBI_TaxID=32059;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=OH-1-P-CL1;
RX PubMed=7766873; DOI=10.1007/bf00037030;
RA Merchan F., Prieto R., Kindle K.L., Llama M.J., Serra J.L., Fernandez E.;
RT "Isolation, sequence and expression in Escherichia coli of the nitrite
RT reductase gene from the filamentous, thermophilic cyanobacterium Phormidium
RT laminosum.";
RL Plant Mol. Biol. 27:1037-1042(1995).
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 -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000305}.
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DR EMBL; Z19598; CAA79655.1; -; Genomic_DNA.
DR PIR; S56640; S56640.
DR AlphaFoldDB; Q51879; -.
DR SMR; Q51879; -.
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-KW.
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 3: Inferred from homology;
KW 4Fe-4S; Electron transport; Heme; Iron; Iron-sulfur; Metal-binding;
KW Nitrate assimilation; Oxidoreductase; Transport.
FT CHAIN 1..510
FT /note="Ferredoxin--nitrite reductase"
FT /id="PRO_0000199956"
FT BINDING 396
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 437
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 441
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 441
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 510 AA; 56709 MW; D4BB0816EABD9C80 CRC64;
MTSTVPAETS LNKFEKLKSE KDGLAVKSEL EDFARLGWEA MDETDRDHRL RWMGVFFRPV
SQGKFMLRMR IPNGILTSGQ IRVLAEVVER YGEDGNADIT TRPNLQLRGI RLEDIPDIFR
RFEQAGLTSI QSGMDNVRNI TGSPVAGIDA DELIDTRGLV RKVQDMITNN GEGNPSFSNL
PRKFNIAIAG CRDNSVHAEI NDIAFVPAYK DGKLGFNVLV GGFFSAKRCE AAVPLNAWVD
PRDVVALCEA ILIVYRITGC GANRQKSRLM WLIDEWGMDK FRAEVEQQLG HPLQTAAPKD
EILWDKRDHI GIHAQKKPGL NYVGLLVPVG RLYAPMFDLA RIAEVYGDGE MRLTVERKRD
HSRTCPMSSV ASLLKEPLLE KFSVSPGLLV RSLVSCTGAQ FCNFALIETK NRAMALIREL
ESELELARPV RIHWTGCPNS CGQPQVADIG LMGTKVRKDG KATEGVDLYM GGKVGKHAEL
GTCVQKGIPC DDLKPILRNL LIEHFGARPK
