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Database: UniProt
Entry: A0A0W1DTE1_9SPHN
LinkDB: A0A0W1DTE1_9SPHN
Original site: A0A0W1DTE1_9SPHN 
ID   A0A0W1DTE1_9SPHN        Unreviewed;       200 AA.
AC   A0A0W1DTE1;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
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   ORFNames=ATE67_08720 {ECO:0000313|EMBL:KTE21364.1};
OS   Sphingopyxis sp. H050.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1759072 {ECO:0000313|EMBL:KTE21364.1, ECO:0000313|Proteomes:UP000053439};
RN   [1] {ECO:0000313|Proteomes:UP000053439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H050 {ECO:0000313|Proteomes:UP000053439};
RA   Gomez-Alvarez V., Revetta R.P.;
RL   Submitted (NOV-2015) 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}.
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:KTE21364.1}.
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DR   EMBL; LNRZ01000003; KTE21364.1; -; Genomic_DNA.
DR   RefSeq; WP_058816321.1; NZ_LNRZ01000003.1.
DR   AlphaFoldDB; A0A0W1DTE1; -.
DR   STRING; 1759072.ATE67_08720; -.
DR   OrthoDB; 9801479at2; -.
DR   Proteomes; UP000053439; Unassembled WGS sequence.
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|HAMAP-Rule:MF_01017};
KW   FMN {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}.
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;  20629 MW;  B730896F14F8CE28 CRC64;
     MAKVLVLYYS SYGHVEQMAD AVAEGARAAG AEVDIRRVAE TAPQAVIEAA GFKTDTAHPL
     LSDPNELATY DAIVVGTPTR FGRMASQMAS FWDAAGGVWA QGKLNGKVGA AFTSTATQHG
     GQETTLFSVL TNLLHFGLTI VGLDYGYAGQ MGVGEVKGGA PYGATTVADG DGSRQPSEAD
     LGGARYLGER VAKTAAKLIA
//
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