ID A0A0L0GIA2_9ENTR Unreviewed; 198 AA.
AC A0A0L0GIA2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=GM31_19385 {ECO:0000313|EMBL:KNC93496.1};
OS Trabulsiella odontotermitis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Trabulsiella.
OX NCBI_TaxID=379893 {ECO:0000313|EMBL:KNC93496.1, ECO:0000313|Proteomes:UP000037393};
RN [1] {ECO:0000313|EMBL:KNC93496.1, ECO:0000313|Proteomes:UP000037393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12 {ECO:0000313|EMBL:KNC93496.1,
RC ECO:0000313|Proteomes:UP000037393};
RX PubMed=26162887;
RA Sapountzis P., Gruntjes T., Otani S., Estevez J., da Costa R.R.,
RA Plunkett G.3rd., Perna N.T., Poulsen M.;
RT "The Enterobacterium Trabulsiella odontotermitis Presents Novel Adaptations
RT Related to Its Association with Fungus-Growing Termites.";
RL Appl. Environ. Microbiol. 81:6577-6588(2015).
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: 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:KNC93496.1}.
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DR EMBL; JNGI01000050; KNC93496.1; -; Genomic_DNA.
DR RefSeq; WP_049850218.1; NZ_JNGI01000050.1.
DR AlphaFoldDB; A0A0L0GIA2; -.
DR STRING; 379893.GCA_001297775_02682; -.
DR PATRIC; fig|379893.3.peg.2648; -.
DR OrthoDB; 9801479at2; -.
DR Proteomes; UP000037393; 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|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:UP000037393}.
FT DOMAIN 4..189
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 78..80
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
FT BINDING 113..118
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
FT BINDING 133
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
SQ SEQUENCE 198 AA; 20890 MW; 4F02684F38D7CB07 CRC64;
MAKILVLYYS MYGHIETMAK AVAEGANKVD GVDVVIKRVP ETMPAEVFEK AGGKSQNAPV
ATPQELADYD AIIFGTPTRF GNMSGQMRTF LDQTGGLWAS GALYGKLASV FSSTGTGGGQ
EQTITSTWTT LAHHGMVIVP IGYAAQELFD VSQVRGGTPY GATTIAGGDG SRQPSQEELS
IARYQGEYVA GLAKKLKG
//
