NQRED_PSEAE
ID NQRED_PSEAE Reviewed; 328 AA.
AC Q9I4V0;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=NADH:quinone reductase {ECO:0000303|PubMed:27502282};
DE EC=1.6.5.9 {ECO:0000269|PubMed:27502282};
GN OrderedLocusNames=PA1024;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION AS A NADH:QUINONE REDUCTASE, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, LACK OF NITRONATE
RP MONOOXYGENASE ACTIVITY, AND REACTION MECHANISM.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=27502282; DOI=10.1074/jbc.m116.739151;
RA Ball J., Salvi F., Gadda G.;
RT "Functional annotation of a presumed nitronate monooxygenase reveals a new
RT class of NADH:quinone reductases.";
RL J. Biol. Chem. 291:21160-21170(2016).
RN [3] {ECO:0007744|PDB:2GJL, ECO:0007744|PDB:2GJN}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEXES WITH 2-NITROPROPANE AND
RP FMN, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=16682407; DOI=10.1074/jbc.m601658200;
RA Ha J.Y., Min J.Y., Lee S.K., Kim H.S., Kim do J., Kim K.H., Lee H.H.,
RA Kim H.K., Yoon H.-J., Suh S.W.;
RT "Crystal structure of 2-nitropropane dioxygenase complexed with FMN and
RT substrate. Identification of the catalytic base.";
RL J. Biol. Chem. 281:18660-18667(2006).
CC -!- FUNCTION: Catalyzes the NADH-dependent reduction of a broad spectrum of
CC quinone substrates, generating the corresponding hydroquinones. Highly
CC prefers NADH to NADPH as a reducing substrate. Also displays a small
CC NADH oxidase activity. Does not exhibit nitronate monooxygenase
CC activity; is inactive against propionate 3-nitronate, 3-
CC nitropropionate, nitroethane, 1-nitropropane, 2-nitropropane, and the
CC anionic forms ethylnitronate, propyl-1-nitronate, and propyl-2-
CC nitronate. Has no azoreductase activity since it is not able to reduce
CC the azo dye methyl red with NADH. May be required to maintain an
CC appropriate [NAD(+)]/[NADH] ratio for the catabolism of fatty acids in
CC P.aeruginosa PAO1. {ECO:0000269|PubMed:27502282}.
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=1.6.5.9;
CC Evidence={ECO:0000269|PubMed:27502282};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:16682407, ECO:0000269|PubMed:27502282};
CC Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:16682407,
CC ECO:0000269|PubMed:27502282};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for 5,8-dihydroxy-1,4-naphthoquinone
CC {ECO:0000269|PubMed:27502282};
CC KM=14 uM for 5-hydroxy-1,4-naphthoquinone
CC {ECO:0000269|PubMed:27502282};
CC KM=18 uM for 2-methyl-5-hydroxy-1,4-naphthoquinone
CC {ECO:0000269|PubMed:27502282};
CC KM=60 uM for 2-methyl-1,4-naphthoquinone
CC {ECO:0000269|PubMed:27502282};
CC KM=185 uM for 2-methoxy-1,4-naphthoquinone
CC {ECO:0000269|PubMed:27502282};
CC KM=15 uM for 1,4-benzoquinone {ECO:0000269|PubMed:27502282};
CC KM=70 uM for 2-methyl-5,6-dimethoxy-1,4-benzoquinone
CC {ECO:0000269|PubMed:27502282};
CC KM=355 uM for 2,3,4,6-tetramethyl-1,4-benzoquinone
CC {ECO:0000269|PubMed:27502282};
CC Note=kcat is 14 sec(-1) with 5,8-dihydroxy-1,4-naphthoquinone as
CC substrate. kcat is 17 sec(-1) with 5-hydroxy-1,4-naphthoquinone as
CC substrate. kcat is 16 sec(-1) with 2-methyl-5-hydroxy-1,4-
CC naphthoquinone as substrate. kcat is 16 sec(-1) with 2-methyl-1,4-
CC naphthoquinone as substrate. kcat is 6 sec(-1) with 2-methoxy-1,4-
CC naphthoquinone as substrate. kcat is 27 sec(-1) with 1,4-benzoquinone
CC as substrate. kcat is 24 sec(-1) with 2-methyl-5,6-dimethoxy-1,4-
CC benzoquinone as substrate. kcat is 28 sec(-1) with 2,3,4,6-
CC tetramethyl-1,4-benzoquinone as substrate.
CC {ECO:0000269|PubMed:27502282};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16682407}.
CC -!- MISCELLANEOUS: The two-electron reduction of quinones by this enzyme
CC occurs through a Ping-Pong-Bi-Bi steady-state kinetic mechanism.
CC {ECO:0000269|PubMed:27502282}.
CC -!- SIMILARITY: Belongs to the nitronate monooxygenase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was reported to be a 2-nitropropane dioxygenase, the previous
CC name for nitronate monooxygenase (PubMed:16682407). However, later
CC experiments demonstrate that this protein does not have any nitronate
CC monooxygenase activity, the activity reported by Ha et al. was likely
CC due to the non-enzymatic reaction of propyl-2-nitronate with oxygen
CC (PubMed:27502282). {ECO:0000269|PubMed:16682407,
CC ECO:0000269|PubMed:27502282}.
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DR EMBL; AE004091; AAG04413.1; -; Genomic_DNA.
DR PIR; A83519; A83519.
DR RefSeq; NP_249715.1; NC_002516.2.
DR RefSeq; WP_003086306.1; NZ_QZGE01000006.1.
DR PDB; 2GJL; X-ray; 2.00 A; A=1-328.
DR PDB; 2GJN; X-ray; 2.30 A; A=1-328.
DR PDB; 6E2A; X-ray; 2.20 A; A=1-328.
DR PDBsum; 2GJL; -.
DR PDBsum; 2GJN; -.
DR PDBsum; 6E2A; -.
DR AlphaFoldDB; Q9I4V0; -.
DR SMR; Q9I4V0; -.
DR STRING; 287.DR97_920; -.
DR PaxDb; Q9I4V0; -.
DR EnsemblBacteria; AAG04413; AAG04413; PA1024.
DR GeneID; 882956; -.
DR KEGG; pae:PA1024; -.
DR PATRIC; fig|208964.12.peg.1058; -.
DR PseudoCAP; PA1024; -.
DR HOGENOM; CLU_038732_1_0_6; -.
DR InParanoid; Q9I4V0; -.
DR OMA; IDDLPSC; -.
DR PhylomeDB; Q9I4V0; -.
DR BioCyc; PAER208964:G1FZ6-1045-MON; -.
DR BRENDA; 1.13.12.16; 5087.
DR EvolutionaryTrace; Q9I4V0; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0018580; F:nitronate monooxygenase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:PseudoCAP.
DR CDD; cd04730; NPD_like; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR004136; NMO.
DR Pfam; PF03060; NMO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Flavoprotein; FMN; NAD; Nucleotide-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..328
FT /note="NADH:quinone reductase"
FT /id="PRO_0000392207"
FT BINDING 22..24
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16682407,
FT ECO:0007744|PDB:2GJL, ECO:0007744|PDB:2GJN"
FT BINDING 75
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16682407,
FT ECO:0007744|PDB:2GJL, ECO:0007744|PDB:2GJN"
FT BINDING 124
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16682407,
FT ECO:0007744|PDB:2GJL, ECO:0007744|PDB:2GJN"
FT BINDING 150
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16682407,
FT ECO:0007744|PDB:2GJL, ECO:0007744|PDB:2GJN"
FT BINDING 178..180
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16682407,
FT ECO:0007744|PDB:2GJL, ECO:0007744|PDB:2GJN"
FT BINDING 201..202
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16682407,
FT ECO:0007744|PDB:2GJL, ECO:0007744|PDB:2GJN"
FT HELIX 7..12
FT /evidence="ECO:0007829|PDB:2GJL"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:2GJL"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:2GJL"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:2GJL"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2GJL"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:2GJL"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2GJL"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:2GJL"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:2GJL"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:2GJL"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:2GJL"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:2GJL"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:2GJL"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:2GJL"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:2GJL"
FT HELIX 160..168
FT /evidence="ECO:0007829|PDB:2GJL"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:2GJL"
FT HELIX 184..193
FT /evidence="ECO:0007829|PDB:2GJL"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:2GJL"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:2GJL"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:2GJL"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:2GJL"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:2GJL"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:2GJL"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:2GJL"
FT HELIX 245..255
FT /evidence="ECO:0007829|PDB:2GJL"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:2GJL"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:2GJL"
FT HELIX 270..279
FT /evidence="ECO:0007829|PDB:2GJL"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:2GJL"
FT HELIX 302..318
FT /evidence="ECO:0007829|PDB:2GJL"
FT HELIX 320..325
FT /evidence="ECO:0007829|PDB:2GJL"
SQ SEQUENCE 328 AA; 34819 MW; 57A9B16894527E8B CRC64;
MGVFRTRFTE TFGVEHPIMQ GGMQWVGRAE MAAAVANAGG LATLSALTQP SPEALAAEIA
RCRELTDRPF GVNLTLLPTQ KPVPYAEYRA AIIEAGIRVV ETAGNDPGEH IAEFRRHGVK
VIHKCTAVRH ALKAERLGVD AVSIDGFECA GHPGEDDIPG LVLLPAAANR LRVPIIASGG
FADGRGLVAA LALGADAINM GTRFLATREC PIHPAVKAAI RAADERSTDL IMRSLRNTAR
VARNAISQEV LAIEARGGAG YADIAALVSG QRGRQVYQQG DTDLGIWSAG MVQGLIDDEP
ACAELLRDIV EQARQLVRQR LEGMLAGV
