ID A0A132MN24_9ACTN Unreviewed; 484 AA.
AC A0A132MN24;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Nitrite reductase (NAD(P)H) large subunit {ECO:0000313|EMBL:KWW99193.1};
DE EC=1.7.1.4 {ECO:0000313|EMBL:KWW99193.1};
GN ORFNames=LI90_827 {ECO:0000313|EMBL:KWW99193.1};
OS Carbonactinospora thermoautotrophica.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Carbonactinosporaceae; Carbonactinospora.
OX NCBI_TaxID=1469144 {ECO:0000313|EMBL:KWW99193.1, ECO:0000313|Proteomes:UP000070188};
RN [1] {ECO:0000313|Proteomes:UP000070188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H1 {ECO:0000313|Proteomes:UP000070188};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Chang R., Ford T., Nguyen P.Q., Woodward J., Permingeat H., Joshi N.S.,
RA Silver P.A., Usadel B., Rutherford A.W., Friesen M., Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KWW99193.1}.
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DR EMBL; LAXD01000001; KWW99193.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A132MN24; -.
DR STRING; 1469144.LI90_827; -.
DR PATRIC; fig|1469144.10.peg.942; -.
DR OrthoDB; 9768666at2; -.
DR Proteomes; UP000070188; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:UniProtKB-EC.
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 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; IPR041575; Rubredoxin_C.
DR PANTHER; PTHR43429:SF3; NADH OXIDASE-RELATED; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF18267; Rubredoxin_C; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:KWW99193.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070188}.
FT DOMAIN 6..297
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 319..377
FT /note="NADH-rubredoxin oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18267"
FT DOMAIN 422..470
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
SQ SEQUENCE 484 AA; 51414 MW; D7E1B4885F525A8B CRC64;
MTAVNRVVVV GYGMAGARLA RELRARARDL RIIVFGAERY PAYNRVLLSS VLAGKADEGD
IALAEPTSRV ELRTGVTVTA IDPADRTVTT DDGTVTRYDA LVLATGSRAW IPPVDGLDPA
ALPEGVAVFR TLEDCRRILR AAEGARRAVV LGGGLLGLEA ARGLALRGLR VEVLHAMGHL
MERQLDPGAS RVLTRTLRGL GVSVRLNALT EAVLCDQGRV RAVRLAGGEV VEADLLVVAC
GVRPETALAE AAGLKVDRGV VVDDQLRTCD PAIYAIGDCA EHDGTVYGLV APAWEQARVV
ADVITGADPR ARYAGSRVVT RLKATGVDLA AMGDTQVEED EEHEVLQFVD PTRGTYKKVV
IRDDRLVGAI LLGENATVGT VTQLFDRSAP VPVDRRALLF ADLRGQAART VESPVQIPDR
TTICQCNSVT KSAITKSWLA GARSVEDVIK ETRATTGCGG CRDTVEGIVE WLAASDPQTT
GSCS
//