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Database: UniProt
Entry: A0A158GDQ6_9BURK
LinkDB: A0A158GDQ6_9BURK
Original site: A0A158GDQ6_9BURK 
ID   A0A158GDQ6_9BURK        Unreviewed;       846 AA.
AC   A0A158GDQ6;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Nitrite reductase [NAD(P)H] large subunit {ECO:0000313|EMBL:SAL29769.1};
GN   ORFNames=AWB66_01780 {ECO:0000313|EMBL:SAL29769.1};
OS   Caballeronia telluris.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=326475 {ECO:0000313|EMBL:SAL29769.1, ECO:0000313|Proteomes:UP000054717};
RN   [1] {ECO:0000313|EMBL:SAL29769.1, ECO:0000313|Proteomes:UP000054717}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 22936 {ECO:0000313|EMBL:SAL29769.1};
RA   Oliw E.H.;
RL   Submitted (JAN-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; FCNZ02000005; SAL29769.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158GDQ6; -.
DR   STRING; 326475.AWB66_01780; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000054717; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054717}.
FT   DOMAIN          1..298
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..746
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   846 AA;  92065 MW;  F7260F38DA0982AC CRC64;
     MKIIVIGHGM VGHKFLECLA ESPVEGLDIT VLCEEPRPAY DRVHLSEFFA GKTAEDLSLV
     APGFFERENF VLRLNAKAAS IDRAARTVTV STGETLAYDK LVIATGSYSF VPPLAGRDRA
     DCFVYRTIED LEAMRECGAR SKTGTVIGGG LLGLECAKAL RDLGLETHVV EFAPRLMAVQ
     VDEGGGRALR TKIEELGVTV HTERNTKEIV DGETGRNRMQ FADGTHLDTD MIVFSAGIRP
     RDEIARAARL DVGPRGGIVI DDACRTSDEH IYAIGECALW KGMVFGLVAP GYDMARVAAK
     HLLGDAAEFG GADMSTKLKL MGVDVASIGD AHGKTPGSRS YQYHDERKQV YKKLVVSDCG
     KFLLGGVMVG DATEYGTLLQ MMLNRIELPE APEFLILPQS DGKAKPALGV EALPAAAQIC
     SCNNVTKAQI CEAVCAGATS IGSLKTACKA GSSCGGCVPL VTQVMKAEMK KQGMSVNNHV
     CEHFPYSRQE LYHIVRVEGV KSFGELLAKH GRGHGCDICK PAVANILASC WNEFVLKMEH
     ASLQDSNDYY LANIQRDGTY SVVPRMPGGE VTPEGLIAVG QVAKKYGLYT KITGGQRVDL
     FGARVEQLPF IWEELIAAGF ESGHAYGKAL RTVKSCVGST WCRYGVGDSV GLAVEVENRY
     KGLRAPHKIK FGVSGCTREC AEAQGKDVGI IATEKGWNLF VCGNGGMKPR HAELLASDLD
     HATLIRYIDR FLMFYVRTAD RLQRTSVWRD NLEGGLDYLI DVVVNDKLGL GADLEAEMAH
     VIDTYECEWK KAVTDPETRK RFRHFVNSDL GDANVTFVEE RGQIRPATVE EKTKTFPVPV
     VAVETV
//
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