Reviewed, UniProtKB/Swiss-Prot P86029 (HQD2_CANAL)

Names and origin

Protein names

Recommended name:
    Catechol 1,2-dioxygenase
    EC=1.13.11.1

Gene names

Name:	HQD2
ORF Names:	CaO19.4567, CaO19.12036

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	303 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Can cleave 4-methylcatechol at lower rates than catechol, but has no activity with 3-methylcatechol, 4-chlorocatechol, 4-carboxycatechol or hydroxyquinol. Ref.2
Catalytic activity	Catechol + O2 = cis,cis-muconate. Ref.2
Cofactor	Binds 1 Fe3+ ion per subunit. Ref.2
Enzyme regulation	Inhibited by Ag+, Cu+, Hg2+ and Pb2+. Ref.2
Pathway	Aromatic compound metabolism; beta-ketoadipate pathway; 5-oxo-4,5-dihydro-2-furylacetate from catechol: step 1/3. Ref.2
Subunit structure	Homodimer. Ref.2
Induction	By phenol. Ref.2
Sequence similarities	Belongs to the intradiol ring-cleavage dioxygenase family.
Biophysicochemical properties	Kinetic parameters: KM=9.3 µM for catechol Ref.2 KM=21.5 µM for 4-methylcatechol Ref.2 pH dependence: Optimum pH is 8.0. Active from pH 7.0 to 9.0. Ref.2 Temperature dependence: Optimum temperature is 25 degrees Celsius. Stable at temperatures lower than 40 degrees Celsuis. Ref.2
Mass spectrometry	Molecular mass is 31994±2 Da . Determined by ESI. Ref.2

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW catechol catabolic process Ref.2 Inferred from direct assay. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	catechol 1,2-dioxygenase activity Ref.2 Inferred from direct assay. Source: UniProtKB ferric iron binding Ref.2 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 303	303	Catechol 1,2-dioxygenase		PRO_0000351556
Sites
	Metal binding	156	1	Iron By similarity
	Metal binding	191	1	Iron By similarity
	Metal binding	215	1	Iron By similarity
	Metal binding	217	1	Iron By similarity
Experimental info
	Sequence conflict	62 – 63	2	SR → DK AA sequence Ref.2
	Sequence conflict	71	1	C → Y AA sequence Ref.2
	Sequence conflict	74	1	I → L AA sequence Ref.2
	Sequence conflict	78	1	T → S AA sequence Ref.2
	Sequence conflict	161	1	D → E AA sequence Ref.2
	Sequence conflict	166	1	E → D AA sequence Ref.2
	Sequence conflict	216	1	I → L AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P86029-1 [UniParc]. Last modified October 14, 2008. Version 1. Checksum: 51BA8D5B0C8C6FBA	FASTA	303	33,800
	10 20 30 40 50 60 MSQAFTESVK TSLGPNATPR AKKLIASLVQ HVHDFARENH LTTEDWLWGV DFINRIGQMS 70 80 90 100 110 120 DSRRNEGILV CDIIGLETLV DALTNESEQS NHTSSAILGP FYLPDSPVYP NGGSIVQKAI 130 140 150 160 170 180 PTDVKCFVRG KVTDTEGKPL GGAQLEVWQC NSAGFYSQQA DHDGPEFNLR GTFITDDEGN 190 200 210 220 230 240 YSFECLRPTS YPIPYDGPAG DLLKIMDRHP NRPSHIHWRV SHPGYHTLIT QIYDAECPYT 250 260 270 280 290 300 NNDSVYAVKD DIIVHFEKVD NKDKDLVGKV EYKLDYDISL ATESSIQEAR AAAKARQDAE IKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314.
[2]	"Purification and characterization of a catechol 1,2-dioxygenase from a phenol degrading Candida albicans TL3." Tsai S.-C., Li Y.-K. Arch. Microbiol. 187:199-206(2007) [PubMed: 17089147] [Abstract] Cited for: PROTEIN SEQUENCE OF 56-80; 161-169 AND 212-219, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBUNIT, INDUCTION, MASS SPECTROMETRY. Strain: TL3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACQ01000006 Genomic DNA. Translation: EAL03902.1. AACQ01000005 Genomic DNA. Translation: EAL04056.1.
RefSeq	XP_722639.1. XP_722784.1.
3D structure databases
SMR	P86029. Positions 2-281.
ModBase	Search...
Genome annotation databases
GeneID	3635484. 3635693.
KEGG	cal:CaO19.12036. cal:CaO19.4567.
Organism-specific databases
CGD	CAL0002834. orf19.4567.
Phylogenomic databases
OrthoDB	EOG91VMK9.
Family and domain databases
InterPro	IPR007535. Catechol_dOase_N. IPR000627. Intradiol_dOase_C. IPR015889. Intradiol_dOase_core. [Graphical view]
Gene3D	G3DSA:2.60.130.10. Intradiol_dOase_core. 1 hit.
Pfam	PF00775. Dioxygenase_C. 1 hit. PF04444. Dioxygenase_N. 1 hit. [Graphical view]
PROSITE	PS00083. INTRADIOL_DIOXYGENAS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HQD2_CANAL

Accession

Primary (citable) accession number: P86029
Secondary accession number(s): Q5AMS9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 14, 2008
Last sequence update:	October 14, 2008
Last modified:	January 19, 2010
This is version 10 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)