NQO1_RAT
ID NQO1_RAT Reviewed; 274 AA.
AC P05982; Q63478;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=NAD(P)H dehydrogenase [quinone] 1;
DE EC=1.6.5.2 {ECO:0000269|PubMed:1703398, ECO:0000269|PubMed:7862630, ECO:0000269|PubMed:8999809};
DE AltName: Full=Azoreductase;
DE AltName: Full=DT-diaphorase {ECO:0000303|PubMed:8999809};
DE Short=DTD;
DE AltName: Full=Menadione reductase;
DE AltName: Full=NAD(P)H:quinone oxidoreductase 1 {ECO:0000303|PubMed:2141979};
DE AltName: Full=Phylloquinone reductase;
DE AltName: Full=Quinone reductase 1;
DE Short=QR1;
GN Name=Nqo1; Synonyms=Nmor1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=3536915; DOI=10.1016/s0021-9258(18)66789-4;
RA Robertson J.A., Chen H.-C., Nebert D.W.;
RT "NAD(P)H:menadione oxidoreductase. Novel purification of enzyme cDNA and
RT complete amino acid sequence, and gene regulation.";
RL J. Biol. Chem. 261:15794-15799(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RA Robertson J.A., Nebert D.W., Hankinson O.;
RT "Autoregulation plus positive and negative elements controlling
RT transcription of genes in the [Ah] battery.";
RL Chem. Scr. 27:83-87(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=3100515; DOI=10.1016/s0021-9258(19)75821-9;
RA Bayney R.M., Rodkey J.A., Bennett C.D., Lu A.Y.H., Pickett C.B.;
RT "Rat liver NAD(P)H: quinone reductase nucleotide sequence analysis of a
RT quinone reductase cDNA clone and prediction of the amino acid sequence of
RT the corresponding protein.";
RL J. Biol. Chem. 262:572-575(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Liver;
RX PubMed=2480957; DOI=10.1016/s0021-9258(20)88253-2;
RA Bayney R.M., Morton M.R., Favreau L.V., Pickett C.B.;
RT "Rat liver NAD(P)H:quinone reductase. Regulation of quinone reductase gene
RT expression by planar aromatic compounds and determination of the exon
RT structure of the quinone reductase structural gene.";
RL J. Biol. Chem. 264:21793-21797(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-274, CLEAVAGE OF INITIATOR METHIONINE, AND
RP ACETYLATION AT ALA-2.
RX PubMed=3143406; DOI=10.1021/bi00418a033;
RA Haniu M., Yuan H., Chen S.A., Iyanagi T., Lee T.D., Shively J.E.;
RT "Structure-function relationship of NAD(P)H:quinone reductase:
RT characterization of NH2-terminal blocking group and essential tyrosine and
RT lysine residues.";
RL Biochemistry 27:6877-6883(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE OF 1-57.
RX PubMed=2963593; DOI=10.1016/0003-9861(88)90516-4;
RA Bayney R.M., Pickett C.B.;
RT "Rat liver NAD(P)H:quinone reductase: isolation of a quinone reductase
RT structural gene and prediction of the NH2 terminal sequence of the protein
RT by double-stranded sequencing of exons 1 and 2.";
RL Arch. Biochem. Biophys. 260:847-850(1988).
RN [8]
RP PROTEIN SEQUENCE OF 2-21, FUNCTION, COFACTOR, SUBCELLULAR LOCATION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=1703398; DOI=10.1016/0003-9861(90)90648-i;
RA Ma Q., Wang R., Yang C.S., Lu A.Y.H.;
RT "Expression of mammalian DT-diaphorase in Escherichia coli: purification
RT and characterization of the expressed protein.";
RL Arch. Biochem. Biophys. 283:311-317(1990).
RN [9]
RP PROTEIN SEQUENCE OF 24-131 AND 156-270.
RX PubMed=3144286; DOI=10.1016/0006-2952(88)90336-x;
RA Knox R.J., Boland M.P., Friedlos F., Coles B., Southan C., Roberts J.J.;
RT "The nitroreductase enzyme in Walker cells that activates 5-(aziridin-1-
RT yl)-2,4-dinitrobenzamide (CB 1954) to 5-(aziridin-1-yl)-4-hydroxylamino-2-
RT nitrobenzamide is a form of NAD(P)H dehydrogenase (quinone) (EC
RT 1.6.99.2).";
RL Biochem. Pharmacol. 37:4671-4677(1988).
RN [10]
RP NUCLEOTIDE SEQUENCE OF 80-274.
RX PubMed=2504488;
RA Dear T.N., McDonald D.A., Kefford R.F.;
RT "Transcriptional down-regulation of a rat gene, WDNM2, in metastatic DMBA-8
RT cells.";
RL Cancer Res. 49:5323-5328(1989).
RN [11]
RP PROTEIN SEQUENCE OF 147-156 AND 263-271.
RX PubMed=2499768;
RA Liu X.F., Yuan H., Haniu M., Iyanagi T., Shively J.E., Chen S.A.;
RT "Reaction of rat liver DT-diaphorase (NAD(P)H:quinone acceptor reductase)
RT with 5'-[p-(fluorosulfonyl)benzoyl]-adenosine.";
RL Mol. Pharmacol. 35:818-822(1989).
RN [12]
RP MUTAGENESIS OF 117-PHE--GLU-118; VAL-161 AND ASP-164.
RX PubMed=2141979; DOI=10.1016/0006-291x(90)92006-l;
RA Forrest G.L., Qian J., Ma J.-X., Kaplan W.D., Akman S., Doroshow J.,
RA Chen S.A.;
RT "Rat liver NAD(P)H:quinone oxidoreductase: cDNA expression and site-
RT directed mutagenesis.";
RL Biochem. Biophys. Res. Commun. 169:1087-1093(1990).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF HIS-195.
RX PubMed=7862630; DOI=10.1073/pnas.92.4.1043;
RA Cui K., Lu A.Y., Yang C.S.;
RT "Subunit functional studies of NAD(P)H:quinone oxidoreductase with a
RT heterodimer approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:1043-1047(1995).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF TYR-105; THR-131; VAL-204; SER-219 AND LEU-239.
RX PubMed=8999809; DOI=10.1074/jbc.272.3.1437;
RA Chen S., Knox R., Wu K., Deng P.S., Zhou D., Bianchet M.A., Amzel L.M.;
RT "Molecular basis of the catalytic differences among DT-diaphorase of human,
RT rat, and mouse.";
RL J. Biol. Chem. 272:1437-1439(1997).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FAD AND DUROQUINONE,
RP AND SUBUNIT.
RC TISSUE=Liver;
RX PubMed=7568029; DOI=10.1073/pnas.92.19.8846;
RA Li R., Bianchet M.A., Talalay P., Amzel L.M.;
RT "The three-dimensional structure of NAD(P)H:quinone reductase, a
RT flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism
RT of the two-electron reduction.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8846-8850(1995).
RN [16]
RP ERRATUM OF PUBMED:7568029.
RA Li R., Bianchet M.A., Talalay P., Amzel L.M.;
RL Proc. Natl. Acad. Sci. U.S.A. 92:10815-10815(1995).
CC -!- FUNCTION: Flavin-containing quinone reductase that catalyzes two-
CC electron reduction of quinones to hydroquinones using either NADH or
CC NADPH as electron donors. In a ping-pong kinetic mechanism, the
CC electrons are sequentially transferred from NAD(P)H to flavin cofactor
CC and then from reduced flavin to the quinone, bypassing the formation of
CC semiquinone and reactive oxygen species (PubMed:8999809,
CC PubMed:1703398, PubMed:7862630). Regulates cellular redox state
CC primarily through quinone detoxification. Reduces components of plasma
CC membrane redox system such as coenzyme Q and vitamin quinones,
CC producing antioxidant hydroquinone forms. In the process may function
CC as superoxide scavenger to prevent hydroquinone oxidation and
CC facilitate excretion (By similarity). Alternatively, can activate
CC quinones and their derivatives by generating redox reactive
CC hydroquinones with DNA cross-linking antitumor potential (By
CC similarity). Acts as a gatekeeper of the core 20S proteasome known to
CC degrade proteins with unstructured regions. Upon oxidative stress,
CC interacts with tumor suppressors TP53 and TP73 in a NADH-dependent way
CC and inhibits their ubiquitin-independent degradation by the 20S
CC proteasome (By similarity). {ECO:0000250|UniProtKB:P15559,
CC ECO:0000269|PubMed:1703398, ECO:0000269|PubMed:7862630,
CC ECO:0000269|PubMed:8999809}.
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:0000269|PubMed:1703398, ECO:0000269|PubMed:7862630,
CC ECO:0000269|PubMed:8999809};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46161;
CC Evidence={ECO:0000305|PubMed:1703398, ECO:0000305|PubMed:7862630,
CC ECO:0000305|PubMed:8999809};
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:0000269|PubMed:1703398, ECO:0000269|PubMed:7862630};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46165;
CC Evidence={ECO:0000305|PubMed:1703398, ECO:0000305|PubMed:7862630};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + ubiquinone-10 = NAD(+) + ubiquinol-10;
CC Xref=Rhea:RHEA:61984, ChEBI:CHEBI:15378, ChEBI:CHEBI:46245,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:64183;
CC Evidence={ECO:0000250|UniProtKB:P15559};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61985;
CC Evidence={ECO:0000250|UniProtKB:P15559};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + menadione + NADH = menadiol + NAD(+);
CC Xref=Rhea:RHEA:69695, ChEBI:CHEBI:6746, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28869, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:8999809};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69696;
CC Evidence={ECO:0000305|PubMed:8999809};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:1703398};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=85 uM for NADH {ECO:0000269|PubMed:7862630};
CC KM=39 uM for NADPH {ECO:0000269|PubMed:7862630};
CC KM=110 uM for NADH {ECO:0000269|PubMed:8999809};
CC KM=2.5 uM for menadione {ECO:0000269|PubMed:8999809};
CC KM=840 uM for 5-(aziridin-1-yl)-2,4-dinitrobenzamide
CC {ECO:0000269|PubMed:8999809};
CC Vmax=2400 umol/min/mg enzyme toward menadione
CC {ECO:0000269|PubMed:8999809};
CC Vmax=140 nmol/min/mg enzyme toward 5-(aziridin-1-yl)-2,4-
CC dinitrobenzamide {ECO:0000269|PubMed:8999809};
CC Note=kcat is 0.075 min(-1) NADH with as substrate. kcat is 0.074
CC min(-1) with NADPH as substrate. {ECO:0000269|PubMed:7862630};
CC -!- SUBUNIT: Homodimer (PubMed:7568029). Interacts with PDLIM4 isoform 2;
CC this interaction stabilizes PDLIM4 isoform 2 in response to oxidative
CC stress and protects it from ubiquitin-independent degradation by the
CC core 20S proteasome (By similarity). Interacts with TP73 (via SAM
CC domain); this interaction is NADH-dependent, stabilizes TP73 in
CC response to oxidative stress and protects it from ubiquitin-independent
CC degradation by the 20S proteasome (By similarity). Interacts with TP53;
CC this interaction is NADH-dependent, stabilizes TP53 in response to
CC oxidative stress and protects it from ubiquitin-independent degradation
CC by the 20S proteasome (By similarity). {ECO:0000250|UniProtKB:P15559,
CC ECO:0000269|PubMed:7568029}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:1703398}.
CC -!- INDUCTION: By polycyclic hydrocarbons (Governed by the aromatic
CC hydrocarbon-responsive (AH) locus).
CC -!- MISCELLANEOUS: Quinone reductase accepts electrons from both NADH and
CC NADPH with equal efficiency.
CC -!- MISCELLANEOUS: This protein is inhibited by dicoumarol.
CC -!- SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) family.
CC {ECO:0000305}.
CC -!- CAUTION: PubMed:2480957 sequence seems incorrectly to be attributed to
CC a mouse sequence while it really seems to correspond to the rat
CC sequence. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA41988.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J02608; AAA41716.1; -; mRNA.
DR EMBL; J02679; AAA41715.1; -; mRNA.
DR EMBL; M36660; AAA39829.1; -; mRNA.
DR EMBL; J02640; AAA41988.1; ALT_INIT; mRNA.
DR EMBL; M31805; AAA41989.1; -; Genomic_DNA.
DR EMBL; M31801; AAA41989.1; JOINED; Genomic_DNA.
DR EMBL; M31802; AAA41989.1; JOINED; Genomic_DNA.
DR EMBL; M31804; AAA41989.1; JOINED; Genomic_DNA.
DR EMBL; M33039; AAA41990.1; -; Genomic_DNA.
DR EMBL; M33038; AAA41990.1; JOINED; Genomic_DNA.
DR EMBL; BC083542; AAH83542.1; -; mRNA.
DR EMBL; X17464; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A34162; A34162.
DR RefSeq; NP_058696.2; NM_017000.3.
DR PDB; 1QRD; X-ray; 2.40 A; A/B=2-274.
DR PDBsum; 1QRD; -.
DR AlphaFoldDB; P05982; -.
DR SMR; P05982; -.
DR IntAct; P05982; 2.
DR STRING; 10116.ENSRNOP00000017175; -.
DR BindingDB; P05982; -.
DR ChEMBL; CHEMBL3091269; -.
DR iPTMnet; P05982; -.
DR PhosphoSitePlus; P05982; -.
DR World-2DPAGE; 0004:P05982; -.
DR jPOST; P05982; -.
DR PaxDb; P05982; -.
DR PRIDE; P05982; -.
DR Ensembl; ENSRNOT00000112166; ENSRNOP00000082814; ENSRNOG00000012772.
DR GeneID; 24314; -.
DR KEGG; rno:24314; -.
DR UCSC; RGD:2503; rat.
DR CTD; 1728; -.
DR RGD; 2503; Nqo1.
DR eggNOG; ENOG502QQMI; Eukaryota.
DR GeneTree; ENSGT00940000159150; -.
DR HOGENOM; CLU_058643_2_0_1; -.
DR InParanoid; P05982; -.
DR OMA; WFERVLV; -.
DR OrthoDB; 1394543at2759; -.
DR PhylomeDB; P05982; -.
DR TreeFam; TF300296; -.
DR BRENDA; 1.6.5.2; 5301.
DR Reactome; R-RNO-350562; Regulation of ornithine decarboxylase (ODC).
DR EvolutionaryTrace; P05982; -.
DR PRO; PR:P05982; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000012772; Expressed in stomach and 20 other tissues.
DR Genevisible; P05982; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IDA:RGD.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IDA:UniProtKB.
DR GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0004784; F:superoxide dismutase activity; IMP:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0045454; P:cell redox homeostasis; ISO:RGD.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:RGD.
DR GO; GO:0071248; P:cellular response to metal ion; IEP:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0006116; P:NADH oxidation; IDA:RGD.
DR GO; GO:0070995; P:NADPH oxidation; IDA:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:0043086; P:negative regulation of catalytic activity; ISO:RGD.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:0019430; P:removal of superoxide radicals; ISS:UniProtKB.
DR GO; GO:0043279; P:response to alkaloid; IEP:RGD.
DR GO; GO:0014075; P:response to amine; IDA:RGD.
DR GO; GO:0009743; P:response to carbohydrate; IEP:RGD.
DR GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:1905395; P:response to flavonoid; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:1904880; P:response to hydrogen sulfide; IEP:RGD.
DR GO; GO:0002931; P:response to ischemia; IEP:RGD.
DR GO; GO:1904844; P:response to L-glutamine; IDA:RGD.
DR GO; GO:1901698; P:response to nitrogen compound; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IEP:RGD.
DR GO; GO:0033574; P:response to testosterone; IEP:RGD.
DR GO; GO:1904772; P:response to tetrachloromethane; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
DR GO; GO:0006801; P:superoxide metabolic process; IMP:RGD.
DR GO; GO:0006743; P:ubiquinone metabolic process; ISS:UniProtKB.
DR GO; GO:0042360; P:vitamin E metabolic process; ISS:UniProtKB.
DR GO; GO:0042373; P:vitamin K metabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR003680; Flavodoxin_fold.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR Pfam; PF02525; Flavodoxin_2; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; FAD;
KW Flavoprotein; Isopeptide bond; NAD; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1703398,
FT ECO:0000269|PubMed:3143406"
FT CHAIN 2..274
FT /note="NAD(P)H dehydrogenase [quinone] 1"
FT /id="PRO_0000071625"
FT REGION 225..274
FT /note="Important for apoenzyme conformational stability"
FT /evidence="ECO:0000250|UniProtKB:P15559"
FT BINDING 12
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:7568029"
FT BINDING 18..19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:7568029"
FT BINDING 67
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:7568029"
FT BINDING 104..107
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:7568029"
FT BINDING 126..128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 148..151
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:7568029"
FT BINDING 156
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:7568029"
FT BINDING 201
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:7568029"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:3143406"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15559"
FT CROSSLNK 251
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P15559"
FT MUTAGEN 105
FT /note="Y->Q: Decreases the catalytic efficiency toward
FT menadione and nitrobenzene substrates."
FT /evidence="ECO:0000269|PubMed:8999809"
FT MUTAGEN 117..118
FT /note="FE->KK: Destroys enzyme activity."
FT /evidence="ECO:0000269|PubMed:2141979"
FT MUTAGEN 131
FT /note="T->A: Decreases the catalytic efficiency toward
FT menadione. Has no effect on the catalytic efficiency toward
FT nitrobenzene substrate."
FT /evidence="ECO:0000269|PubMed:8999809"
FT MUTAGEN 161
FT /note="V->D: Destroys enzyme activity."
FT /evidence="ECO:0000269|PubMed:2141979"
FT MUTAGEN 164
FT /note="D->Q: Destroys enzyme activity."
FT /evidence="ECO:0000269|PubMed:2141979"
FT MUTAGEN 195
FT /note="H->A: Induces a very low catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:7862630"
FT MUTAGEN 204
FT /note="V->I: Has no effect on the catalytic efficiency
FT toward menadione and nitrobenzene substrates."
FT /evidence="ECO:0000269|PubMed:8999809"
FT MUTAGEN 219
FT /note="S->T: Has no effect on the catalytic efficiency
FT toward menadione and nitrobenzene substrates."
FT /evidence="ECO:0000269|PubMed:8999809"
FT MUTAGEN 239
FT /note="L->M: Has no effect on the catalytic efficiency
FT toward menadione. Slightly decreases the catalytic
FT efficiency toward nitrobenzene substrate."
FT /evidence="ECO:0000269|PubMed:8999809"
FT CONFLICT 31
FT /note="Missing (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="R -> G (in Ref. 10; X17464)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="K -> Q (in Ref. 3; AAA41988)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="W -> E (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="S -> E (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="S -> I (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="Q -> E (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:1QRD"
FT HELIX 18..32
FT /evidence="ECO:0007829|PDB:1QRD"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:1QRD"
FT TURN 42..46
FT /evidence="ECO:0007829|PDB:1QRD"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:1QRD"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:1QRD"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:1QRD"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:1QRD"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:1QRD"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1QRD"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:1QRD"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:1QRD"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:1QRD"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:1QRD"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:1QRD"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:1QRD"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:1QRD"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1QRD"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:1QRD"
FT HELIX 198..212
FT /evidence="ECO:0007829|PDB:1QRD"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:1QRD"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:1QRD"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:1QRD"
FT HELIX 241..247
FT /evidence="ECO:0007829|PDB:1QRD"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:1QRD"
FT TURN 266..270
FT /evidence="ECO:0007829|PDB:1QRD"
SQ SEQUENCE 274 AA; 30947 MW; 40E8801320A20F09 CRC64;
MAVRRALIVL AHAERTSFNY AMKEAAVEAL KKKGWEVVES DLYAMNFNPL ISRNDITGEP
KDSENFQYPV ESSLAYKEGR LSPDIVAEQK KLEAADLVIF QFPLYWFGVP AILKGWFERV
LVAGFAYTYA TMYDKGPFQN KKTLLSITTG GSGSMYSLQG VHGDMNVILW PIQSGILRFC
GFQVLEPQLV YSIGHTPPDA RVQVLEGWKK RLETVWEESP LYFAPSSLFD LNFQAGFLLK
KEVQEEQKKN KFGLSVGHHL GKSIPADNQI KARK
