ID A0A165QL29_9SPHN Unreviewed; 200 AA.
AC A0A165QL29;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=A3736_01365 {ECO:0000313|EMBL:KZY55988.1};
OS Erythrobacter sp. HI0063.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1822240 {ECO:0000313|EMBL:KZY55988.1, ECO:0000313|Proteomes:UP000077326};
RN [1] {ECO:0000313|EMBL:KZY55988.1, ECO:0000313|Proteomes:UP000077326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI0063 {ECO:0000313|EMBL:KZY55988.1,
RC ECO:0000313|Proteomes:UP000077326};
RA Sosa O.A.;
RT "Microbial cycling of marine high molecular weight dissolved organic
RT matter.";
RL Submitted (MAR-2016) 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:KZY55988.1}.
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DR EMBL; LWFF01000274; KZY55988.1; -; Genomic_DNA.
DR RefSeq; WP_067682032.1; NZ_LWFF01000274.1.
DR AlphaFoldDB; A0A165QL29; -.
DR OrthoDB; 9801479at2; -.
DR Proteomes; UP000077326; Unassembled WGS sequence.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
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; IPR001226; Flavodoxin_CS.
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; PS00201; FLAVODOXIN; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000077326}.
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; 20950 MW; D006621358332A15 CRC64;
MTKILVLYYS SYGHTAKMAE AVAEGIREGG AEAVIRHVAE TAPQEVVESA GFQQMEGHTC
IGGPDELAEY DGIVVGSPTR YGRMTSQMAA FWDQTGGLWQ KGALIGKVGA AFTSTASQHG
GQETTLWSIL NNLLHMGMTV VGLDYGFQDQ MGTDEVKGGA PYGATTIAGG DGSRQPSETD
LAGARYLGKR VAQTAAKLGA
//
