ID A0A3A6TDL6_ECOLX Unreviewed; 198 AA. AC A0A3A6TDL6; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 10-APR-2019, entry version 4. 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=D3Y67_03010 {ECO:0000313|EMBL:RJY06153.1}; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562 {ECO:0000313|EMBL:RJY06153.1, ECO:0000313|Proteomes:UP000277698}; RN [1] {ECO:0000313|EMBL:RJY06153.1, ECO:0000313|Proteomes:UP000277698} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12-269M {ECO:0000313|EMBL:RJY06153.1, RC ECO:0000313|Proteomes:UP000277698}; RA Le Devendec L., Jouy E., Paboeuf F., De Boisseson C., Lucas P., RA Drider D., Kempf I.; RT "Development of a pig infection model with colistin-resistant RT Escherichia coli."; RL Submitted (SEP-2018) 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; CC EC=1.6.5.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01017, CC ECO:0000256|SAAS:SAAS01115134}; 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; CC EC=1.6.5.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01017, CC ECO:0000256|SAAS:SAAS01115133}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000256|HAMAP- CC 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|HAMAP- CC Rule:MF_01017, ECO:0000256|SAAS:SAAS00561325}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:RJY06153.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; QZWA01000008; RJY06153.1; -; Genomic_DNA. DR Proteomes; UP000277698; 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:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule. 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 Pfam; PF03358; FMN_red; 1. DR SUPFAM; SSF52218; SSF52218; 1. DR TIGRFAMs; TIGR01755; flav_wrbA; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000277698}; KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01017, KW ECO:0000256|SAAS:SAAS00956512}; KW FMN {ECO:0000256|HAMAP-Rule:MF_01017, ECO:0000256|SAAS:SAAS00956506}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01017, ECO:0000256|SAAS:SAAS00956503}; KW NADP {ECO:0000256|HAMAP-Rule:MF_01017, ECO:0000256|SAAS:SAAS00956510}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01017, KW ECO:0000256|SAAS:SAAS00956507}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01017, KW ECO:0000256|SAAS:SAAS00956509}. FT DOMAIN 4 189 Flavodoxin-like. {ECO:0000259|PROSITE: FT PS50902}. FT NP_BIND 10 15 FMN. {ECO:0000256|HAMAP-Rule:MF_01017}. FT NP_BIND 78 80 FMN. {ECO:0000256|HAMAP-Rule:MF_01017}. FT NP_BIND 113 118 FMN. {ECO:0000256|HAMAP-Rule:MF_01017}. FT BINDING 12 12 NAD(P). {ECO:0000256|HAMAP-Rule: FT MF_01017}. FT BINDING 98 98 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01017}. FT BINDING 133 133 FMN. {ECO:0000256|HAMAP-Rule:MF_01017}. SQ SEQUENCE 198 AA; 20858 MW; 6B334D67D49C292C CRC64; MAKVLVLYYS MYGHIETMAR AVAEGASKVD GAEVVVKRVP ETMPPQLFEK AGGKTQTAPV ATPQELADYD AIIFGTPTRF GNMSGQMRIF LDQTGGLWAS GALYGKLASV FSSTGTGGGQ EQTITSTWTT LAHHGMVIVP IGYAAQELFD VSQVRGGTPY GATTIAGGDG SRQPSQEELS IARYQGEYVA GLAVKLNG //