HQD2_CANAL
ID HQD2_CANAL Reviewed; 303 AA.
AC P86029; A0A1D8PLI0; Q5AMS9;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Catechol 1,2-dioxygenase;
DE EC=1.13.11.1;
GN Name=HQD2; OrderedLocusNames=CAALFM_C402230CA;
GN ORFNames=CaO19.12036, CaO19.4567;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP PROTEIN SEQUENCE OF 56-80; 161-169 AND 212-219, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, SUBUNIT, INDUCTION, AND MASS SPECTROMETRY.
RC STRAIN=TL3 {ECO:0000269|PubMed:17089147};
RX PubMed=17089147; DOI=10.1007/s00203-006-0187-4;
RA Tsai S.-C., Li Y.-K.;
RT "Purification and characterization of a catechol 1,2-dioxygenase from a
RT phenol degrading Candida albicans TL3.";
RL Arch. Microbiol. 187:199-206(2007).
CC -!- FUNCTION: Can cleave 4-methylcatechol at lower rates than catechol, but
CC has no activity with 3-methylcatechol, 4-chlorocatechol, 4-
CC carboxycatechol or hydroxyquinol. {ECO:0000269|PubMed:17089147}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=catechol + O2 = cis,cis-muconate + 2 H(+);
CC Xref=Rhea:RHEA:23852, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:18135, ChEBI:CHEBI:32379; EC=1.13.11.1;
CC Evidence={ECO:0000269|PubMed:17089147};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000269|PubMed:17089147};
CC Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000269|PubMed:17089147};
CC -!- ACTIVITY REGULATION: Inhibited by Ag(+), Cu(+), Hg(2+) and Pb(2+).
CC {ECO:0000269|PubMed:17089147}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.3 uM for catechol {ECO:0000269|PubMed:17089147};
CC KM=21.5 uM for 4-methylcatechol {ECO:0000269|PubMed:17089147};
CC pH dependence:
CC Optimum pH is 8.0. Active from pH 7.0 to 9.0.
CC {ECO:0000269|PubMed:17089147};
CC Temperature dependence:
CC Optimum temperature is 25 degrees Celsius. Stable at temperatures
CC lower than 40 degrees Celsius. {ECO:0000269|PubMed:17089147};
CC -!- PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-
CC 4,5-dihydro-2-furylacetate from catechol: step 1/3.
CC {ECO:0000269|PubMed:17089147}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17089147}.
CC -!- INDUCTION: By phenol. {ECO:0000269|PubMed:17089147}.
CC -!- MASS SPECTROMETRY: Mass=31994; Mass_error=2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:17089147};
CC -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CC {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017626; AOW28994.1; -; Genomic_DNA.
DR RefSeq; XP_722639.1; XM_717546.1.
DR AlphaFoldDB; P86029; -.
DR SMR; P86029; -.
DR STRING; 237561.P86029; -.
DR GeneID; 3635693; -.
DR KEGG; cal:CAALFM_C402230CA; -.
DR CGD; CAL0000188195; orf19.12036.
DR VEuPathDB; FungiDB:C4_02230C_A; -.
DR eggNOG; ENOG502QU2V; Eukaryota.
DR HOGENOM; CLU_046727_1_1_1; -.
DR InParanoid; P86029; -.
DR OMA; IATYDNY; -.
DR OrthoDB; 979452at2759; -.
DR SABIO-RK; P86029; -.
DR UniPathway; UPA00157; UER00258.
DR PRO; PR:P86029; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0018576; F:catechol 1,2-dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0008199; F:ferric iron binding; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
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:0019615; P:catechol catabolic process, ortho-cleavage; IDA:CGD.
DR GO; GO:0019614; P:catechol-containing compound catabolic process; IDA:UniProtKB.
DR GO; GO:0009712; P:catechol-containing compound metabolic process; IDA:UniProtKB.
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 Aromatic hydrocarbons catabolism; Dioxygenase; Direct protein sequencing;
KW Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..303
FT /note="Catechol 1,2-dioxygenase"
FT /id="PRO_0000351556"
FT BINDING 156
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CONFLICT 62..63
FT /note="SR -> DK (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="C -> Y (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="I -> L (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="T -> S (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="D -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="E -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="I -> L (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 303 AA; 33800 MW; 51BA8D5B0C8C6FBA CRC64;
MSQAFTESVK TSLGPNATPR AKKLIASLVQ HVHDFARENH LTTEDWLWGV DFINRIGQMS
DSRRNEGILV CDIIGLETLV DALTNESEQS NHTSSAILGP FYLPDSPVYP NGGSIVQKAI
PTDVKCFVRG KVTDTEGKPL GGAQLEVWQC NSAGFYSQQA DHDGPEFNLR GTFITDDEGN
YSFECLRPTS YPIPYDGPAG DLLKIMDRHP NRPSHIHWRV SHPGYHTLIT QIYDAECPYT
NNDSVYAVKD DIIVHFEKVD NKDKDLVGKV EYKLDYDISL ATESSIQEAR AAAKARQDAE
IKL
