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Database: UniProt
Entry: H0TDW4_9BRAD
LinkDB: H0TDW4_9BRAD
Original site: H0TDW4_9BRAD 
ID   H0TDW4_9BRAD            Unreviewed;       391 AA.
AC   H0TDW4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Nitrite reductase (NAD(P)H), large subunit {ECO:0000313|EMBL:CCE04652.1};
DE            EC=1.7.1.4 {ECO:0000313|EMBL:CCE04652.1};
GN   Name=nasD {ECO:0000313|EMBL:CCE04652.1};
GN   ORFNames=BRAS3843_1100030 {ECO:0000313|EMBL:CCE04652.1};
OS   Bradyrhizobium sp. STM 3843.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE04652.1, ECO:0000313|Proteomes:UP000002686};
RN   [1] {ECO:0000313|Proteomes:UP000002686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM3843 {ECO:0000313|Proteomes:UP000002686};
RX   PubMed=24704842; DOI=10.3390/genes3010035;
RA   Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA   Smith A.A., Giraud E., Medigue C., Moulin L.;
RT   "Comparative genomics of aeschynomene symbionts: insights into the
RT   ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL   Genes (Basel) 3:35-61(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00006442}.
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:CCE04652.1}.
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DR   EMBL; CAFK01000014; CCE04652.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0TDW4; -.
DR   Proteomes; UP000002686; 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; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; 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   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000313|EMBL:CCE04652.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002686}.
FT   DOMAIN          3..283
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          304..370
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
SQ   SEQUENCE   391 AA;  41854 MW;  0C8749E06CB78EFB CRC64;
     MAAARLVEEL SKTALGRYAI AVIGEEPRLA YNRVLLSSVL AGEVGSHEIE LKAASWWRER
     GVTLKYGTRV TEIDVGRREL KIENDESIAF SKLVLATGSL PIRLNVPGVE LAGVHTFRDS
     RDADILLALA AQKKRVVVVG GGLLGLEAAY GLARAGAPVT LVHLMDRLME RQLDPPAAAL
     LKSLVERKGI EVLLNANTAR IDGDGKVEAV ELADGRRIAA EAVIFAAGIR PNIALAKEGG
     LAVNRGIVID DQMQSSAPDI FALGECAEHR GTCYGLVEPA HEQARVLARH LAGATASYQG
     SVVATNLKVS GVSVFSAGDY IGADGSEAIV LKDFRRGIYK KLVIAEGRLT GAVLIGDTQD
     ALWYRDLIRA REQIAPIRTE MMFGRARPKA A
//
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