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Database: UniProt
Entry: D5C2Z5_NITHN
LinkDB: D5C2Z5_NITHN
Original site: D5C2Z5_NITHN 
ID   D5C2Z5_NITHN            Unreviewed;       200 AA.
AC   D5C2Z5;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=NAD(P)H dehydrogenase (quinone) {ECO:0000256|HAMAP-Rule:MF_01017};
DE            EC=1.6.5.2 {ECO:0000256|HAMAP-Rule:MF_01017};
DE   AltName: Full=NAD(P)H:quinone oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01017};
DE            Short=NQO {ECO:0000256|HAMAP-Rule:MF_01017};
GN   OrderedLocusNames=Nhal_1766 {ECO:0000313|EMBL:ADE14887.1};
OS   Nitrosococcus halophilus (strain Nc4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Nitrosococcus.
OX   NCBI_TaxID=472759 {ECO:0000313|EMBL:ADE14887.1, ECO:0000313|Proteomes:UP000001844};
RN   [1] {ECO:0000313|Proteomes:UP000001844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nc4 {ECO:0000313|Proteomes:UP000001844};
RG   US DOE Joint Genome Institute;
RA   Campbell M.A., Malfatti S.A., Chain P.S.G., Heidelberg J.F., Ward B.B.,
RA   Klotz M.G.;
RT   "Complete genome sequence of Nitrosococcus halophilus Nc4, a salt-adapted,
RT   aerobic obligate ammonia-oxidizing sulfur purple bacterium.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC         Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01017};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+);
CC         Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01017};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01017};
CC       Note=Binds 1 FMN per monomer. {ECO:0000256|HAMAP-Rule:MF_01017};
CC   -!- SIMILARITY: Belongs to the WrbA family. {ECO:0000256|ARBA:ARBA00006961,
CC       ECO:0000256|HAMAP-Rule:MF_01017}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01017}.
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DR   EMBL; CP001798; ADE14887.1; -; Genomic_DNA.
DR   RefSeq; WP_013032772.1; NC_013960.1.
DR   AlphaFoldDB; D5C2Z5; -.
DR   STRING; 472759.Nhal_1766; -.
DR   KEGG; nhl:Nhal_1766; -.
DR   eggNOG; COG0655; Bacteria.
DR   HOGENOM; CLU_051402_0_2_6; -.
DR   OrthoDB; 9801479at2; -.
DR   Proteomes; UP000001844; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IEA:RHEA.
DR   Gene3D; 3.40.50.360; -; 1.
DR   HAMAP; MF_01017; NQOR; 1.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR010089; Flavoprotein_WrbA-like.
DR   InterPro; IPR005025; FMN_Rdtase-like.
DR   InterPro; IPR037513; NQO.
DR   NCBIfam; TIGR01755; flav_wrbA; 1.
DR   PANTHER; PTHR30546; FLAVODOXIN-RELATED PROTEIN WRBA-RELATED; 1.
DR   PANTHER; PTHR30546:SF23; PROTEIN RFS1-RELATED; 1.
DR   Pfam; PF03358; FMN_red; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_01017};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_01017};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01017};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_01017};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01017};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01017};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001844}.
FT   DOMAIN          4..191
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   BINDING         10..15
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
FT   BINDING         12
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
FT   BINDING         79..81
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
FT   BINDING         135
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
SQ   SEQUENCE   200 AA;  21636 MW;  92DA6C67B81A0B56 CRC64;
     MAKLLVLYYS MYGHVETMAH AVAEGARSVD EVEVTLKRVP ELMPEEVARN AGAKLDQEAP
     IATVDELPEY DGIIFGTPTR FGNMCAQMRN FLDQTGKHWM SGALIGKVGS VFTSTASQHG
     GQETTITSFH STLLHQGMAI VGVPYSCQAL LNMNEITGGS PYGASTLADA DGSRQPSENE
     LTIARFQGEY VAKFTKKVVE
//
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