(data stored in ACNUC29543 zone)

SWISSPROT: NQOR_PARP8

ID   NQOR_PARP8              Reviewed;         199 AA.
AC   B2JML0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   08-MAY-2019, entry version 70.
DE   RecName: Full=NAD(P)H dehydrogenase (quinone) {ECO:0000255|HAMAP-Rule:MF_01017};
DE            EC=1.6.5.2 {ECO:0000255|HAMAP-Rule:MF_01017};
DE   AltName: Full=Flavoprotein WrbA;
DE   AltName: Full=NAD(P)H:quinone oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01017};
DE            Short=NQO {ECO:0000255|HAMAP-Rule:MF_01017};
GN   OrderedLocusNames=Bphy_3669;
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815;
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A.,
RA   Melkonian R., James E.K., Young J.P., Bena G., Hauser L., Land M.,
RA   Kyrpides N., Bruce D., Chain P., Copeland A., Pitluck S., Woyke T.,
RA   Lizotte-Waniewski M., Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad
RT   host range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
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:0000255|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;
CC         EC=1.6.5.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01017};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01017};
CC       Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_01017};
CC   -!- SIMILARITY: Belongs to the WrbA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01017}.
DR   EMBL; CP001044; ACC72804.1; -; Genomic_DNA.
DR   RefSeq; WP_012402977.1; NC_010623.1.
DR   SMR; B2JML0; -.
DR   STRING; 391038.Bphy_3669; -.
DR   CAZy; AA6; Auxiliary Activities 6.
DR   EnsemblBacteria; ACC72804; ACC72804; Bphy_3669.
DR   GeneID; 27743335; -.
DR   KEGG; bph:Bphy_3669; -.
DR   eggNOG; ENOG4105CS1; Bacteria.
DR   eggNOG; COG0655; LUCA.
DR   HOGENOM; HOG000030539; -.
DR   KO; K03809; -.
DR   OMA; VGVPYAC; -.
DR   OrthoDB; 796211at2; -.
DR   BioCyc; BPHY391038:G1GBS-3764-MONOMER; -.
DR   Proteomes; UP000001192; Chromosome 2.
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;
DR   PRODOM; B2JML0.
DR   SWISS-2DPAGE; B2JML0.
KW   Complete proteome; Flavoprotein; FMN; NAD; NADP; Nucleotide-binding;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN         1    199       NAD(P)H dehydrogenase (quinone).
FT                                /FTId=PRO_1000200620.
FT   DOMAIN        4    190       Flavodoxin-like. {ECO:0000255|HAMAP-
FT                                Rule:MF_01017}.
FT   NP_BIND      10     15       FMN. {ECO:0000255|HAMAP-Rule:MF_01017}.
FT   NP_BIND      78     80       FMN. {ECO:0000255|HAMAP-Rule:MF_01017}.
FT   NP_BIND     113    119       FMN. {ECO:0000255|HAMAP-Rule:MF_01017}.
FT   BINDING      12     12       NAD(P). {ECO:0000255|HAMAP-
FT                                Rule:MF_01017}.
FT   BINDING      98     98       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01017}.
FT   BINDING     134    134       FMN. {ECO:0000255|HAMAP-Rule:MF_01017}.
SQ   SEQUENCE   199 AA;  20943 MW;  A0572B4A47EC48F6 CRC64;
     MARVLVLYYS SYGHIEKMAE AIAEGARGAG AQVDIKRVPE TVPEEIAKKA NFKLDQQAPI
     ATVADLEQYD AIVVGTGTRY GRISSQMAAF LDQTGGLWMR GALNGKVGAA FASTATQHGG
     QETTLFSIIT NLMHLGMIIV GLPYSHQGMM NMTEIVGGAP YGATTIAAGD GSRQPSAIDL
     EGARHQGELV AKTAAKLFG
//

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