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Database: UniProt
Entry: A0A1B3LRJ3_9PROT
LinkDB: A0A1B3LRJ3_9PROT
Original site: A0A1B3LRJ3_9PROT 
ID   A0A1B3LRJ3_9PROT        Unreviewed;       822 AA.
AC   A0A1B3LRJ3;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Nitrite reductase [NAD(P)H], large subunit {ECO:0000313|EMBL:AOF83456.1};
DE            EC=1.7.1.4 {ECO:0000313|EMBL:AOF83456.1};
GN   Name=nirB {ECO:0000313|EMBL:AOF83456.1};
GN   ORFNames=BSY238_3508 {ECO:0000313|EMBL:AOF83456.1};
OS   Methyloversatilis sp. RAC08.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Sterolibacteriaceae; Methyloversatilis.
OX   NCBI_TaxID=1842540 {ECO:0000313|EMBL:AOF83456.1, ECO:0000313|Proteomes:UP000094168};
RN   [1] {ECO:0000313|Proteomes:UP000094168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RAC08 {ECO:0000313|Proteomes:UP000094168};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-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; CP016448; AOF83456.1; -; Genomic_DNA.
DR   RefSeq; WP_069040247.1; NZ_CP016448.1.
DR   AlphaFoldDB; A0A1B3LRJ3; -.
DR   STRING; 1842540.BSY238_3508; -.
DR   KEGG; metr:BSY238_3508; -.
DR   PATRIC; fig|1842540.3.peg.3552; -.
DR   OrthoDB; 9768666at2; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000094168; Chromosome.
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   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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:AOF83456.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094168}.
FT   DOMAIN          5..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          423..471
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          488..538
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          563..626
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          636..775
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   822 AA;  89280 MW;  944667AE04A4C274 CRC64;
     MEKKRLVMVG NGMAGCRTLE ELIKIAPGMY DITVFGAEPH PNYNRILLSP VLAGEMTVQD
     IILNDWDWYR DNGITLHAGK KVVKIDRIAR KVVAEDGTEA EYDRLLLATG SNPFILPVSG
     KDLPGVIAYR DIADTDAMIE AAANHRHAVV IGAGLLGLEA ANGLALRGMH VTVVHLGAWI
     MERQLDRPSA DMLQASLEKK GLAFLLEKQT ESLIAGPDGR VSAVRFKSGE TIPADLVVMA
     AGIRPNTTLA ESAGIHCNRG IVANDTMQTY DPKIYAVGEC VSHRGIAYGL VAPLFEQAKV
     CANHLAQYGI GTYKGSVTST KLKVTGIDVF SAGNFTGGPG CDDIVLHDPS GGVYKRLVLE
     GERLVGACLY GDTADGAWYF QLIKDGQDIH AVRDHLMFGQ NHLGDVGHKG QTQAASMPDT
     AEVCGCNGVC KGTIVKAIKE KGLFSLDDVR KHTKASSSCG SCTGLVEQIL ASCIGGAYTP
     ASSTSKAMCG CTDMNHGDVR AAIRDRHYID IPTVMRELQW KTPNGCASCR PALNYYVQSS
     WPHEAKDDPQ SRYINERAHA NIQKDGTYSV VPRMWGGLTT PNELRAIADA AEKYKVPTVK
     VTGGQRIDLL GVKKDDLPAM WADLAQAGMV SGHAYGKSLR TVKTCVGAEH CRFGTQLSMG
     LGVKLEKMLF GMYSPHKVKL AVSGCPRNCA EAGIKDVGVI GVESGYEIYV AGNGGIKTEV
     AQYFCKVTSD DEVMEYSGAF LQLYREEGWY LERTVHYIDR VGLDYVKGKV VDDAENRKAL
     YERLLFALQD YKDPWLERAQ ADAKSDLGRE FRTIAIRQAM QA
//
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