NIRB_KLEOX
ID NIRB_KLEOX Reviewed; 957 AA.
AC Q06458;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Nitrite reductase [NAD(P)H] large subunit;
DE EC=1.7.1.4;
GN Name=nasB;
OS Klebsiella oxytoca.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=571;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M5a1;
RX PubMed=8468296; DOI=10.1128/jb.175.8.2370-2378.1993;
RA Lin J.T., Goldman B.S., Stewart V.;
RT "Structures of genes nasA and nasB, encoding assimilatory nitrate and
RT nitrite reductases in Klebsiella pneumoniae M5al.";
RL J. Bacteriol. 175:2370-2378(1993).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O + 3 NADP(+) + NH4(+) = 5 H(+) + 3 NADPH + nitrite;
CC Xref=Rhea:RHEA:24632, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16301, ChEBI:CHEBI:28938, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.7.1.4;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O + 3 NAD(+) + NH4(+) = 5 H(+) + 3 NADH + nitrite;
CC Xref=Rhea:RHEA:24628, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16301, ChEBI:CHEBI:28938, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.7.1.4;
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC -!- SUBUNIT: Homodimer which associates with NirD. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000305}.
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DR EMBL; L06800; AAA25099.1; -; Genomic_DNA.
DR AlphaFoldDB; Q06458; -.
DR SMR; Q06458; -.
DR STRING; 571.MC52_25295; -.
DR eggNOG; COG1251; Bacteria.
DR eggNOG; COG2146; Bacteria.
DR UniPathway; UPA00653; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0106316; F:nitrite reductase NADH activity; IEA:RHEA.
DR GO; GO:0106314; F:nitrite reductase NADPH activity; IEA:RHEA.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway.
DR CDD; cd03529; Rieske_NirD; 1.
DR Gene3D; 1.10.10.1100; -; 1.
DR Gene3D; 2.102.10.10; -; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.30.413.10; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR InterPro; IPR012744; Nitri_red_NirB.
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 InterPro; IPR012748; Rieske-like_NirD.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR041575; Rubredoxin_C.
DR Pfam; PF04324; Fer2_BFD; 1.
DR Pfam; PF01077; NIR_SIR; 1.
DR Pfam; PF03460; NIR_SIR_ferr; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF13806; Rieske_2; 1.
DR Pfam; PF18267; Rubredoxin_C; 1.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF50022; SSF50022; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
DR SUPFAM; SSF55124; SSF55124; 1.
DR SUPFAM; SSF56014; SSF56014; 1.
DR TIGRFAMs; TIGR02378; nirD_assim_sml; 1.
DR TIGRFAMs; TIGR02374; nitri_red_nirB; 1.
DR PROSITE; PS00365; NIR_SIR; 1.
DR PROSITE; PS51300; NIRD; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; FAD; Flavoprotein; Heme; Iron; Iron-sulfur; Metal-binding; NADP;
KW Nitrate assimilation; Oxidoreductase.
FT CHAIN 1..957
FT /note="Nitrite reductase [NAD(P)H] large subunit"
FT /id="PRO_0000199963"
FT BINDING 44..79
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 193..225
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 639
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 645
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 679
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 683
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 683
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 957 AA; 104227 MW; A136CC7FA28C6631 CRC64;
MTKPVLVLVG HGMVGHHFLE QCVSRDLHQQ YRIVVFCEER YAAYDRVHLT EYFAGRSAES
LSLVEGDFFT QHGIELRLSE SVASIDREAR VVRDAFGHET HWDKLVLATG SYPFVPPVPG
HNLEGCFVYR TLDDLDQIAA RAATARRGVV IGGGLLGLEA ANALKQLGLE THVVEFAPNL
MAVQLDNGGA AMLREKISEL GVGVHTSKAT TEIVRNEQGL QLNFRDGSSL ATDMLVFSAG
IRPQDALARS GGLSVGERGG ICIDNQCRTS DPDVLAIGEC ALWENKIYGL VAPGYQMAAR
RAATLAGEAG SFSGADMSTK LKLLGVDVAS FGDAQGRTPG CQSYQWTHGP QQVYKKIVVS
ADGKNLLGGV LVGDAGDYAT LLQMMLNGMA LPKHPESLIL PALEGSRPKA LGVAALPDGA
QICSCHNVSK GDICQAVSGG AGDMAAIKSR TKAATGCGGC SALVKQVMEY QLAEQGVEVK
KDICEHFPWS RQEIYHLVRV NHIRTFEQLI ARYGQGHGCE VCKPLVASVL ASCWNEYLLK
PAHLPLQDTN DRYFANIQKD GTYSVVPRMA AGEVTPDGLI AIGQIAKRYQ LYSKVTGGQR
IDLFGARLEQ LPAIWRELAE AGFETGHAYG KSLRTVKSCV GSTWCRYGVQ DSTGLAVTLE
HRYKGLRAPH KIKMAVSGCT RECAEAQGKD IGVIATEKGW NLYVCGNGGM KPRHADLFAS
DLDEATLIRS IDRLLMFYIR TADRLQRTST WMDNLEGGVD YLREMILEDS LGIGEELEQE
MARVVESYQC EWQTTLNDPQ RLALFRSYVN SDEPDETVQR QTLRGQPQLA PFAAQGEPAL
PSRPWQAICD LDAIPQQAGI GARLGERQIA LFRFGDQVYA LDNLEPGSEA NVLSRGLLGD
AGGEPIVISP LYKQRIRLRD GRQCDGGEQA VRAWPVKVEN GKVWVGNQQL LARAEAS
