QDO_PSEPU
ID QDO_PSEPU Reviewed; 264 AA.
AC O33472; Q9R5I6;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase;
DE EC=1.13.11.47;
GN Name=qdo;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC STRAIN=33/1;
RX PubMed=10350631; DOI=10.1016/s0167-4838(99)00083-7;
RA Max N., Betz A., Facey S., Lingens F., Hauer B., Fetzner S.;
RT "Cloning, sequence analysis, and expression of the Pseudomonas putida 33/1
RT 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase gene, encoding a carbon
RT monoxide forming dioxygenase.";
RL Biochim. Biophys. Acta 1431:547-552(1999).
RN [2]
RP PROTEIN SEQUENCE OF 1-24, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=33/1;
RX PubMed=1515060; DOI=10.1515/bchm3.1992.373.1.343;
RA Block D.W., Lingens F.;
RT "Microbial metabolism of quinoline and related compounds. XIV. Purification
RT and properties of 1H-3-hydroxy-4-oxoquinoline oxygenase, a new extradiol
RT cleavage enzyme from Pseudomonas putida strain 33/1.";
RL Biol. Chem. Hoppe-Seyler 373:343-349(1992).
RN [3]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP SER-95; ASP-120 AND HIS-244.
RC STRAIN=33/1;
RX PubMed=10482514; DOI=10.1128/jb.181.18.5725-5733.1999;
RA Fischer F., Kunne S., Fetzner S.;
RT "Bacterial 2,4-dioxygenases: new members of the alpha/beta hydrolase-fold
RT superfamily of enzymes functionally related to serine hydrolases.";
RL J. Bacteriol. 181:5725-5733(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS), CATALYTIC ACTIVITY, LACK OF
RP COFACTOR, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP ASP-120.
RC STRAIN=33/1;
RX PubMed=20080731; DOI=10.1073/pnas.0909033107;
RA Steiner R.A., Janssen H.J., Roversi P., Oakley A.J., Fetzner S.;
RT "Structural basis for cofactor-independent dioxygenation of N-
RT heteroaromatic compounds at the alpha/beta-hydrolase fold.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:657-662(2010).
CC -!- FUNCTION: Ring-cleaving dioxygenase involved in oxoquinoline
CC degradation and utilization. {ECO:0000269|PubMed:20080731}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-1H-quinolin-4-one + O2 = CO + H(+) + N-
CC formylanthranilate; Xref=Rhea:RHEA:17949, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16569, ChEBI:CHEBI:17245,
CC ChEBI:CHEBI:18410; EC=1.13.11.47;
CC Evidence={ECO:0000269|PubMed:10350631, ECO:0000269|PubMed:10482514,
CC ECO:0000269|PubMed:1515060, ECO:0000269|PubMed:20080731};
CC -!- COFACTOR:
CC Note=None. Contrary to most other dioxygenases, this enzyme does not
CC require a cofactor for catalysis.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=24 uM for 1H-3-hydroxy-4-oxoquinoline
CC {ECO:0000269|PubMed:10482514, ECO:0000269|PubMed:1515060,
CC ECO:0000269|PubMed:20080731};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:10482514,
CC ECO:0000269|PubMed:1515060, ECO:0000269|PubMed:20080731};
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; Y14779; CAA75082.2; -; Genomic_DNA.
DR PIR; S23121; S23121.
DR PDB; 3IBT; X-ray; 2.60 A; A=1-264.
DR PDBsum; 3IBT; -.
DR AlphaFoldDB; O33472; -.
DR SMR; O33472; -.
DR ESTHER; psepu-QDO; HOD-cofactorfree-dioxygenase.
DR KEGG; ag:CAA75082; -.
DR BRENDA; 1.13.11.47; 5092.
DR SABIO-RK; O33472; -.
DR EvolutionaryTrace; O33472; -.
DR GO; GO:0047078; F:3-hydroxy-4-oxoquinoline 2,4-dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0019439; P:aromatic compound catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Direct protein sequencing; Oxidoreductase.
FT CHAIN 1..264
FT /note="1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase"
FT /id="PRO_0000418916"
FT ACT_SITE 244
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:B1MFK2"
FT BINDING 30..32
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 94..95
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 120
FT /note="Increases basicity of active site His"
FT /evidence="ECO:0000250|UniProtKB:B1MFK2"
FT MUTAGEN 95
FT /note="S->A,C: Reduced affinity for substrate, and strongly
FT reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:10482514"
FT MUTAGEN 120
FT /note="D->A: Strongly reduced affinity for substrate.
FT Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:10482514,
FT ECO:0000269|PubMed:20080731"
FT MUTAGEN 244
FT /note="H->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:10482514"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:3IBT"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:3IBT"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:3IBT"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:3IBT"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:3IBT"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:3IBT"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:3IBT"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:3IBT"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:3IBT"
FT HELIX 97..107
FT /evidence="ECO:0007829|PDB:3IBT"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:3IBT"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:3IBT"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:3IBT"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:3IBT"
FT HELIX 142..154
FT /evidence="ECO:0007829|PDB:3IBT"
FT HELIX 160..168
FT /evidence="ECO:0007829|PDB:3IBT"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:3IBT"
FT HELIX 175..192
FT /evidence="ECO:0007829|PDB:3IBT"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:3IBT"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:3IBT"
FT HELIX 218..230
FT /evidence="ECO:0007829|PDB:3IBT"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:3IBT"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:3IBT"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:3IBT"
FT HELIX 251..261
FT /evidence="ECO:0007829|PDB:3IBT"
SQ SEQUENCE 264 AA; 30347 MW; DEBE92440554FA84 CRC64;
MQSLNVNGTL MTYSESGDPH APTLFLLSGW CQDHRLFKNL APLLARDFHV ICPDWRGHDA
KQTDSGDFDS QTLAQDLLAF IDAKGIRDFQ MVSTSHGCWV NIDVCEQLGA ARLPKTIVID
WLLQPHPGFW QQLAEGQHPT EYVAGRQSFF DEWAETTDNA DVLNHLRNEM PWFHGEMWQR
ACREIEANYR TWGSPLDRME SLPQKPEICH IYSQPLSQDY RQLQLDFAAG HSWFHPRHIP
GRTHFPSLEN PVAVAQAIRE FLQA
