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Database: UniProt
Entry: A0A2N5NBS6_9BACL
LinkDB: A0A2N5NBS6_9BACL
Original site: A0A2N5NBS6_9BACL 
ID   A0A2N5NBS6_9BACL        Unreviewed;       814 AA.
AC   A0A2N5NBS6;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Nitrite reductase [NAD(P)H] large subunit {ECO:0000313|EMBL:PLT47796.1};
DE            EC=1.7.1.4 {ECO:0000313|EMBL:PLT47796.1};
GN   ORFNames=B8V81_0703 {ECO:0000313|EMBL:PLT47796.1};
OS   Paenibacillus pasadenensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=217090 {ECO:0000313|EMBL:PLT47796.1, ECO:0000313|Proteomes:UP000234789};
RN   [1] {ECO:0000313|EMBL:PLT47796.1, ECO:0000313|Proteomes:UP000234789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R16 {ECO:0000313|EMBL:PLT47796.1,
RC   ECO:0000313|Proteomes:UP000234789};
RA   Passera A., Marcolungo L., Casati P., Brasca M., Quaglino F.,
RA   Delledonne M.;
RT   "Functional genome analysis of Paenibacillus pasadenensis strain R16:
RT   insights on endophytic life style and antifungal activity.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:PLT47796.1}.
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DR   EMBL; NFEZ01000002; PLT47796.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5NBS6; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000234789; 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; 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   Gene3D; 3.90.480.10; Sulfite Reductase Hemoprotein;Domain 2; 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.
DR   PROSITE; PS00365; NIR_SIR; 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:PLT47796.1}.
FT   DOMAIN          6..283
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          319..386
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
FT   DOMAIN          424..473
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          487..536
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          562..624
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          632..767
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   814 AA;  86630 MW;  BB597B9C4336869E CRC64;
     MTIPKKLVLV GNGMAGIRCI EHLLKLAPDA YSITIFGAEP HPNYNRIQLS SVLADGGAGL
     QDIVLNDWSW YEDNGITLHA GHAVTAIDTA SRTVTSDQGV SASYDALLLA TGSRAYILPV
     PGADKEGVIG FRDIRDCQTM LEASRTYRRA AVIGGGLLGL EAARGLLNLG MDVTVVHNSA
     LLMNRQLDPA ASLMLQQELE RQGMTFRLNA QTAEITGRKR AAGLKFKDGS SLDADLVVMA
     VGIVPNAELA ASAGIETRRG IIVGDELATS APGIYALGEC AEHDGIAYGL VAPLYEQGAV
     LAKHLAGVPT EGYRGSVTST KLKVSGVDVF SAGDYMGGAG ARSLRWQDEM DGVYKKLVVR
     GDRLAGAVLF GDTSDGAMLF NLIKSGEPIA GREKELLLGY APGSGGAAAS SLLERLAAMP
     SDEIVCGCNG VSKEAVIQAI VSGGCTSLGA IKACTKASAS CGGCKPLVEG LLELTAGDAV
     VQVREGICGC TSLGREEIVE AISSMGLSGV RETMHVLGWS QPEGCSKCRP ALNYYLGMLQ
     PGSHRDEKES RFANERYHAN IQKDGTFSVV PRIYGGVTSP AELKHIADVA ERFQVPLVKF
     TGGQRLDLLG VRKEDLPRMW EELGMASGSA YGKALRTVKT CVGDTFCRFG TQDAMGMGIR
     LEKAYERIST PAKFKMAVSG CPRNCAEATI KDFGVVAIDG GWELHAGGNG GVKVRATDLI
     GVVRTEEEVM EWSGAFLQYY RETAAWGERT AHWVERVGIG SIREALASAE ERIALNERLQ
     EALATLEDPW QEIVDDPELR KNFEPLAVAG REQP
//
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