HOD_PAENT
ID HOD_PAENT Reviewed; 276 AA.
AC O31266; A4V8M9; J7LVS0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase;
DE EC=1.13.11.48;
GN Name=hod; Synonyms=meqE; ORFNames=ARUE_113p00080, pAL1.008;
OS Paenarthrobacter nitroguajacolicus (Arthrobacter nitroguajacolicus).
OG Plasmid pAL1.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=211146;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, FUNCTION, AND
RP MUTAGENESIS OF SER-101 AND ASP-233.
RC STRAIN=Rue61a;
RX PubMed=10746195;
RX DOI=10.1002/(sici)1521-4028(200002)40:1<7::aid-jobm7>3.0.co;2-5;
RA Betz A., Facey S.J., Hauer B., Tshisuaka B., Lingens F.;
RT "Molecular cloning, sequencing, expression, and site-directed mutagenesis
RT of the 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase gene from Arthrobacter
RT spec. Ru61a.";
RL J. Basic Microbiol. 40:7-23(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=Rue61a;
RX PubMed=17337569; DOI=10.1128/jb.00089-07;
RA Parschat K., Overhage J., Strittmatter A.W., Henne A., Gottschalk G.,
RA Fetzner S.;
RT "Complete nucleotide sequence of the 113-kilobase linear catabolic plasmid
RT pAL1 of Arthrobacter nitroguajacolicus Ru61a and transcriptional analysis
RT of genes involved in quinaldine degradation.";
RL J. Bacteriol. 189:3855-3867(2007).
RN [3]
RP CATALYTIC ACTIVITY, MUTAGENESIS OF SER-101; HIS-102 AND TYR-196, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=Rue61a;
RX PubMed=15533053; DOI=10.1021/bi048735u;
RA Frerichs-Deeken U., Ranguelova K., Kappl R., Huttermann J., Fetzner S.;
RT "Dioxygenases without requirement for cofactors and their chemical model
RT reaction: compulsory order ternary complex mechanism of 1H-3-hydroxy-4-
RT oxoquinaldine 2,4-dioxygenase involving general base catalysis by histidine
RT 251 and single-electron oxidation of the substrate dianion.";
RL Biochemistry 43:14485-14499(2004).
RN [4]
RP CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-251, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVE SITE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Rue61a;
RX PubMed=16187153; DOI=10.1007/s00284-005-0065-3;
RA Frerichs-Deeken U., Fetzner S.;
RT "Dioxygenases without requirement for cofactors: identification of amino
RT acid residues involved in substrate binding and catalysis, and testing for
RT rate-limiting steps in the reaction of 1H-3-hydroxy-4-oxoquinaldine 2,4-
RT dioxygenase.";
RL Curr. Microbiol. 51:344-352(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEXES WITH
RP 2-(ACETYLAMINO)BENZOIC ACID AND 3-HYDROXY-2-METHYLQUINOLIN-4(1H)-ONE,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, LACK OF COFACTOR, AND
RP MUTAGENESIS OF HIS-251.
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 quinaldine degradation
CC and utilization. {ECO:0000269|PubMed:10746195}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-2-methyl-1H-quinolin-4-one + O2 = CO + H(+) + N-
CC acetylanthranilate; Xref=Rhea:RHEA:21572, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16803, ChEBI:CHEBI:17245,
CC ChEBI:CHEBI:29216; EC=1.13.11.48;
CC Evidence={ECO:0000269|PubMed:10746195, ECO:0000269|PubMed:15533053,
CC ECO:0000269|PubMed:16187153, 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=1.5 uM for 1H-3-hydroxy-4-oxoquinaldine
CC {ECO:0000269|PubMed:15533053, ECO:0000269|PubMed:16187153,
CC ECO:0000269|PubMed:20080731};
CC KM=180 uM for 1H-3-hydroxy-4-oxoquinoline
CC {ECO:0000269|PubMed:15533053, ECO:0000269|PubMed:16187153,
CC ECO:0000269|PubMed:20080731};
CC pH dependence:
CC Optimum pH is 8-11. {ECO:0000269|PubMed:15533053,
CC ECO:0000269|PubMed:16187153, ECO:0000269|PubMed:20080731};
CC -!- INDUCTION: Expressed from a large linear plasmid that contains the
CC operon for quinaldine degradation. {ECO:0000269|PubMed:17337569}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; Y14778; CAA75080.1; -; Genomic_DNA.
DR EMBL; CP003205; AFR34517.1; -; Genomic_DNA.
DR PDB; 2WJ3; X-ray; 2.09 A; A/B/C/D=1-276.
DR PDB; 2WJ4; X-ray; 2.10 A; A/B/C/D=1-276.
DR PDB; 2WJ6; X-ray; 2.00 A; A/B/C/D=1-276.
DR PDB; 2WM2; X-ray; 2.70 A; A/B/C/D=1-276.
DR PDB; 4CFS; X-ray; 1.94 A; A/B/C/D=3-275.
DR PDBsum; 2WJ3; -.
DR PDBsum; 2WJ4; -.
DR PDBsum; 2WJ6; -.
DR PDBsum; 2WM2; -.
DR PDBsum; 4CFS; -.
DR AlphaFoldDB; O31266; -.
DR SMR; O31266; -.
DR ESTHER; artsp-hod; HOD-cofactorfree-dioxygenase.
DR EnsemblBacteria; AFR34517; AFR34517; ARUE_113p00080.
DR KEGG; ag:CAA75080; -.
DR KEGG; arr:ARUE_113p00080; -.
DR PATRIC; fig|1118963.3.peg.4723; -.
DR HOGENOM; CLU_087588_0_0_11; -.
DR BRENDA; 1.13.11.47; 8910.
DR BRENDA; 1.13.11.48; 8910.
DR GO; GO:0050586; F:3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; 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; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Oxidoreductase; Plasmid.
FT CHAIN 1..276
FT /note="1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase"
FT /id="PRO_0000418915"
FT DOMAIN 28..150
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 251
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:16187153"
FT BINDING 36..38
FT /ligand="substrate"
FT BINDING 100..101
FT /ligand="substrate"
FT BINDING 160
FT /ligand="substrate"
FT SITE 126
FT /note="Increases basicity of active site His"
FT /evidence="ECO:0000250|UniProtKB:B1MFK2"
FT MUTAGEN 38
FT /note="H->A: Strongly reduced affinity for substrate.
FT Reduced enzyme activity."
FT MUTAGEN 101
FT /note="S->A: Strongly reduced affinity for substrate.
FT Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:10746195,
FT ECO:0000269|PubMed:15533053"
FT MUTAGEN 102
FT /note="H->L: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:15533053"
FT MUTAGEN 102
FT /note="H->Q: Reduces enzyme activity by about half."
FT /evidence="ECO:0000269|PubMed:15533053"
FT MUTAGEN 126
FT /note="D->A: Strongly reduced enzyme activity."
FT MUTAGEN 196
FT /note="Y->A,K,R: Strongly reduced affinity for substrate.
FT Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:15533053"
FT MUTAGEN 233
FT /note="D->A: Reduces enzyme activity by about half."
FT /evidence="ECO:0000269|PubMed:10746195"
FT MUTAGEN 251
FT /note="H->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:16187153,
FT ECO:0000269|PubMed:20080731"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:2WJ6"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:4CFS"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:4CFS"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:4CFS"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:4CFS"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:4CFS"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:4CFS"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:4CFS"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:4CFS"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:4CFS"
FT HELIX 76..90
FT /evidence="ECO:0007829|PDB:4CFS"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:4CFS"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:4CFS"
FT HELIX 104..118
FT /evidence="ECO:0007829|PDB:4CFS"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:4CFS"
FT HELIX 134..144
FT /evidence="ECO:0007829|PDB:4CFS"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:4CFS"
FT HELIX 149..161
FT /evidence="ECO:0007829|PDB:4CFS"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:4CFS"
FT TURN 175..179
FT /evidence="ECO:0007829|PDB:4CFS"
FT HELIX 182..199
FT /evidence="ECO:0007829|PDB:4CFS"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:4CFS"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:4CFS"
FT HELIX 225..237
FT /evidence="ECO:0007829|PDB:4CFS"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:4CFS"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:4CFS"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:4CFS"
FT HELIX 258..273
FT /evidence="ECO:0007829|PDB:4CFS"
SQ SEQUENCE 276 AA; 31858 MW; 7153BCF652C653DB CRC64;
MTDTYLHETL VFDNKLSYID NQRDTDGPAI LLLPGWCHDH RVYKYLIQEL DADFRVIVPN
WRGHGLSPCE VPDFGYQEQV KDALEILDQL GVETFLPVSH SHGGWVLVEL LEQAGPERAP
RGIIMDWLMW APKPDFAKSL TLLKDPERWR EGTHGLFDVW LDGHDEKRVR HHLLEEMADY
GYDCWGRSGR VIEDAYGRNG SPMQMMANLT KTRPIRHIFS QPTEPEYEKI NSDFAEQHPW
FSYAKLGGPT HFPAIDVPDR AAVHIREFAT AIRQGQ
