CHQB_NOCSI
ID CHQB_NOCSI Reviewed; 293 AA.
AC Q5PXQ6;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Hydroxyquinol 1,2-dioxygenase;
DE EC=1.13.11.37 {ECO:0000269|PubMed:9141483};
DE AltName: Full=1,2-HQD;
GN Name=chqB;
OS Nocardioides simplex (Arthrobacter simplex).
OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC Pimelobacter.
OX NCBI_TaxID=2045;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, X-RAY
RP CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH FE(3+), COFACTOR, AND
RP CHARACTERIZATION.
RC STRAIN=3E;
RX PubMed=15772073; DOI=10.1074/jbc.m500666200;
RA Ferraroni M., Seifert J., Travkin V.M., Thiel M., Kaschabek S.,
RA Scozzafava A., Golovleva L., Schloemann M., Briganti F.;
RT "Crystal structure of the hydroxyquinol 1,2-dioxygenase from Nocardioides
RT simplex 3E, a key enzyme involved in polychlorinated aromatics
RT biodegradation.";
RL J. Biol. Chem. 280:21144-21154(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP ACTIVITY REGULATION.
RC STRAIN=3E;
RX PubMed=9141483; DOI=10.1016/s0014-5793(97)00297-4;
RA Travkin V.M., Jadan A.P., Briganti F., Scozzafava A., Golovleva L.A.;
RT "Characterization of an intradiol dioxygenase involved in the
RT biodegradation of the chlorophenoxy herbicides 2,4-D and 2,4,5-T.";
RL FEBS Lett. 407:69-72(1997).
CC -!- FUNCTION: Catalyzes the ortho-cleavage of the aromatic ring of
CC hydroxyquinol. {ECO:0000269|PubMed:9141483}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzene-1,2,4-triol + O2 = 2 H(+) + maleylacetate;
CC Xref=Rhea:RHEA:35595, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16468, ChEBI:CHEBI:16971; EC=1.13.11.37;
CC Evidence={ECO:0000269|PubMed:9141483};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000269|PubMed:15772073};
CC Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000269|PubMed:15772073};
CC -!- ACTIVITY REGULATION: Inhibited by 3,5-dichlorocatechol,
CC chlorohydroquinone and 4,5-dibromocatechol.
CC {ECO:0000269|PubMed:9141483}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 uM for hydroxyquinol {ECO:0000269|PubMed:9141483};
CC Vmax=55 umol/min/mg enzyme with hydroxyquinol as substrate
CC {ECO:0000269|PubMed:9141483};
CC Note=5-chlorohydroxyquinols and 6-chloro-chlorohydroxyquinols are
CC also substrates.;
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:9141483};
CC Temperature dependence:
CC Optimum temperature is 50-55 degrees Celsius.
CC {ECO:0000269|PubMed:9141483};
CC -!- PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway; 3-
CC oxoadipate from 3,4-dihydroxybenzoate: step 2/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15772073,
CC ECO:0000269|PubMed:9141483}.
CC -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; AY822041; AAV71144.1; -; Genomic_DNA.
DR PDB; 1TMX; X-ray; 1.75 A; A/B=1-293.
DR PDBsum; 1TMX; -.
DR AlphaFoldDB; Q5PXQ6; -.
DR SMR; Q5PXQ6; -.
DR STRING; 2045.KR76_25510; -.
DR DrugBank; DB03793; Benzoic acid.
DR KEGG; ag:AAV71144; -.
DR eggNOG; COG3485; Bacteria.
DR BRENDA; 1.13.11.37; 456.
DR SABIO-RK; Q5PXQ6; -.
DR UniPathway; UPA00157; UER00268.
DR EvolutionaryTrace; Q5PXQ6; -.
DR GO; GO:0047074; F:4-hydroxycatechol 1,2-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0018576; F:catechol 1,2-dioxygenase activity; IEA:InterPro.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0018581; F:hydroxyquinol 1,2-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0042952; P:beta-ketoadipate pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0009712; P:catechol-containing compound metabolic process; IEA:InterPro.
DR CDD; cd03461; 1_2-HQD; 1.
DR Gene3D; 2.60.130.10; -; 1.
DR InterPro; IPR039390; 1_2-HQD/HQD.
DR InterPro; IPR007535; Catechol_dOase_N.
DR InterPro; IPR000627; Intradiol_dOase_C.
DR InterPro; IPR015889; Intradiol_dOase_core.
DR Pfam; PF00775; Dioxygenase_C; 1.
DR Pfam; PF04444; Dioxygenase_N; 1.
DR SUPFAM; SSF49482; SSF49482; 1.
DR PROSITE; PS00083; INTRADIOL_DIOXYGENAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase;
KW Direct protein sequencing; Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..293
FT /note="Hydroxyquinol 1,2-dioxygenase"
FT /id="PRO_0000085086"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:15772073"
FT BINDING 197
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:15772073"
FT BINDING 221
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:15772073"
FT BINDING 223
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:15772073"
FT HELIX 7..23
FT /evidence="ECO:0007829|PDB:1TMX"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1TMX"
FT HELIX 30..50
FT /evidence="ECO:0007829|PDB:1TMX"
FT HELIX 54..70
FT /evidence="ECO:0007829|PDB:1TMX"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:1TMX"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:1TMX"
FT STRAND 133..142
FT /evidence="ECO:0007829|PDB:1TMX"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:1TMX"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:1TMX"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1TMX"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:1TMX"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:1TMX"
FT HELIX 204..211
FT /evidence="ECO:0007829|PDB:1TMX"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:1TMX"
FT STRAND 234..240
FT /evidence="ECO:0007829|PDB:1TMX"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:1TMX"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:1TMX"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:1TMX"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1TMX"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:1TMX"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:1TMX"
SQ SEQUENCE 293 AA; 31967 MW; DEE403CF2AB8F5B0 CRC64;
MSTPVSAEQQ AREQDLVERV LRSFDATADP RLKQVMQALT RHLHAFLREV RLTEAEWETG
IGFLTDAGHV TNERRQEFIL LSDVLGASMQ TIAMNNEAHG DATEATVFGP FFVEGSPRIE
SGGDIAGGAA GEPCWVEGTV TDTDGNPVPD ARIEVWEADD DGFYDVQYDD DRTAARAHLL
SGPDGGYAFW AITPTPYPIP HDGPVGRMLA ATGRSPMRAS HLHFMVTAPG RRTLVTHIFV
EGDELLDRDS VFGVKDSLVK SFERQPAGAP TPGGREIDGP WSRVRFDIVL APA
