ID A0A1H1BWQ1_9BURK Unreviewed; 849 AA.
AC A0A1H1BWQ1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Nitrite reductase (NADH) large subunit {ECO:0000313|EMBL:SDQ56365.1};
GN ORFNames=SAMN05443245_1855 {ECO:0000313|EMBL:SDQ56365.1};
OS Paraburkholderia fungorum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=134537 {ECO:0000313|EMBL:SDQ56365.1, ECO:0000313|Proteomes:UP000183487};
RN [1] {ECO:0000313|Proteomes:UP000183487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS106B {ECO:0000313|Proteomes:UP000183487};
RA Varghese N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNKP01000001; SDQ56365.1; -; Genomic_DNA.
DR RefSeq; WP_074764013.1; NZ_FNKP01000001.1.
DR AlphaFoldDB; A0A1H1BWQ1; -.
DR OrthoDB; 9768666at2; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000183487; 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; 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 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; 1.
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}.
FT DOMAIN 1..282
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 315..384
FT /note="NADH-rubredoxin oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18267"
FT DOMAIN 419..466
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT DOMAIN 554..617
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 627..750
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
SQ SEQUENCE 849 AA; 92012 MW; EF8AE7E5DC12657B CRC64;
MKIIVIGHGM VGHKLIESLA QDAAHGLDIT VLCEESRPAY DRVHLSEFFA GKTADDLSLV
EPGFFERQNV LLKLNAKAVA IDRDARTVTV STGETLPYDK LVFATGSYPF VPPVQGRERK
DCFVYRTIDD LEAMQECGAR SKTGTVVGGG LLGLECAKAL RDMGLQTHVV EFAPRLMAVQ
VDDGGGRVLR TKIEELGVTV HTQKNTTAIV DGEAGTHRMQ FADGTHLDTD MIVFSAGIRP
RDDLARECGL TLGARGGIVI DNACRTSDPH IYAIGECALW NGQLFGLVAP GYEMARAVAK
QLLGDSAEFA GADMSTKLKL MGVDVASIGD AHGSTPGSRA YQFSDERKQV YKKLVVSECG
KYLLGGVMVG DASEYGTLLQ MMLNRIELPA SPEFLILPQA DGNAKPALGV EALPAAAQIC
SCNNVSKGDL CAAVCAGATD IGALKCATSA GTSCGGCVPL VTQVMKAEMK KQGLAVNNHV
CEHFAYSRQE LYHIVRVEGV RSFGELIAKH GHGLGCDICK PVVASVLASC WNEFVLKKEH
ASLQDTNDYY LANIQRDGTY SVVPRMAGGE VTPDGLIAVG QVAKKYGLYT KITGGQRVDL
FGARVEQLPL IWEELIAAGF ESGHAYGKSL RTVKSCVGST WCRYGVGDSV GLAVEIENRY
KGLRTPHKIK FGVSGCTREC AEAQGKDVGI IATEKGWNLY VCGNGGMKPR HAELLASDLD
KETLVRYIDR FLMFYVRTAD RLQRTSVWRD NLEGGLEYLI DVVVNDRLGV ADELEAEMQQ
VVDTYECEWK KAVTDPETRK RFRHFVNSGE SDSNVTFVEE RGQIRPATPA ERESKQSALA
AIPVVVEMV
//
