ID K6EDN3_9BACI Unreviewed; 808 AA.
AC K6EDN3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Nitrite reductase [NAD(P)H] large subunit {ECO:0000313|EMBL:EKN71551.1};
DE EC=1.7.1.4 {ECO:0000313|EMBL:EKN71551.1};
GN Name=nasB {ECO:0000313|EMBL:EKN71551.1};
GN ORFNames=BABA_00915 {ECO:0000313|EMBL:EKN71551.1};
OS Neobacillus bataviensis LMG 21833.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN71551.1, ECO:0000313|Proteomes:UP000006316};
RN [1] {ECO:0000313|EMBL:EKN71551.1, ECO:0000313|Proteomes:UP000006316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX PubMed=23087684;
RA Heylen K., Keltjens J.;
RT "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT reduction in Bacillus.";
RL Front. Microbiol. 3:371-371(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRNR:PIRNR037149};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- COFACTOR:
CC Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC Evidence={ECO:0000256|ARBA:ARBA00001929};
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC {ECO:0000256|ARBA:ARBA00005096}.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000256|ARBA:ARBA00010429}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKN71551.1}.
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DR EMBL; AJLS01000005; EKN71551.1; -; Genomic_DNA.
DR RefSeq; WP_007083226.1; NZ_AJLS01000005.1.
DR AlphaFoldDB; K6EDN3; -.
DR STRING; 1117379.BABA_00915; -.
DR PATRIC; fig|1117379.3.peg.190; -.
DR eggNOG; COG1251; Bacteria.
DR OrthoDB; 9792592at2; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000006316; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniRule.
DR CDD; cd19943; NirB_Fer2_BFD-like_1; 1.
DR CDD; cd19944; NirB_Fer2_BFD-like_2; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.90.480.20; -; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 1.
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; IPR017121; Nitrite_Rdtase_lsu.
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; IPR041575; Rubredoxin_C.
DR NCBIfam; TIGR02374; nitri_red_nirB; 1.
DR PANTHER; PTHR43809; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 1.
DR PANTHER; PTHR43809:SF1; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 1.
DR Pfam; PF04324; Fer2_BFD; 2.
DR Pfam; PF01077; NIR_SIR; 1.
DR Pfam; PF03460; NIR_SIR_ferr; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF18267; Rubredoxin_C; 1.
DR PIRSF; PIRSF037149; NirB; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 1.
DR SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR037149};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR037149}; Heme {ECO:0000256|ARBA:ARBA00022617};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063,
KW ECO:0000256|PIRNR:PIRNR037149};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EKN71551.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006316}.
FT DOMAIN 4..280
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 317..383
FT /note="NADH-rubredoxin oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18267"
FT DOMAIN 413..462
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT DOMAIN 479..528
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT DOMAIN 554..616
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 624..763
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
SQ SEQUENCE 808 AA; 89359 MW; C757DB7BE51A4C3F CRC64;
MMKKLVMIGN GMAGVRTIEE ILKQAPEQFD ITIFGQEPHP NYNRIKLSNI LQGDTNFDEI
IINPLDWYKE NNIQLFSGEA VVKIDVDRKR VISDQGREVE YDELIIATGS NSFILPIPGA
DKIGVTGFRD IQDCEMMIKS AEEYKKAVVI GGGLLGLEAA RGLLNLGMSV DVVHLMPHLM
ERQLDPIASS LLRSELEAQG MNFLMEKETV EILGDERVTG LRFKDGSEAE ADLVVMSIGI
KSNTTVAKNS GIYVNRGIVV NDFMETSVPH VYAVGECAEH REIVYGLVAP LYEQGKVLAN
RICGMDGEPY EGSVTGTQLK VAGVDLYSAG EIFEDESTKS IMIYNEYEGI YKRVLTRNNM
IVGIVLYGDT KDSTRLFRML TKKEDISGGS IFQTECTGSG TSDSIAAMPD DELVCGCNGV
TKGAIVEAIQ TQGLTTLDQV SHCTNAGRSC GRCKPMVSSI LAHTLGDQFD ATAAQKVSIC
GCTTISREEL VAEIKEKGLT SVKEVMNVLE WNNEEGCTKC RPAINYYLGM ILMDEYKDDR
DSRLVNEKIH ANIQKDGTYS VVPRMYGGVT TAADLKKIAE VAERYHVPLV KLTGGQGIGL
FGVKKEDLPS MWEDLDMPSG YAYGKTLRTV KTCVGAQFCR YGTQDSMALG IELEKKFERL
DTPHKVKMGV SACPRNCSEA GIKDIGFVGI DGGWEIYVAG NGGVDLRPGD LLCTVKTQVE
VMEMTGAYLQ YYRETANYLE RTSKWVERMG LDHVKEVLAD EETRKALNER MDQTLKKYIE
PWNEAIQSEE IQDKYYTKHT VAVGSESK
//
