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Database: UniProt
Entry: A0A132MN24_9ACTN
LinkDB: A0A132MN24_9ACTN
Original site: A0A132MN24_9ACTN 
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
//
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