Reviewed, UniProtKB/Swiss-Prot P17262 (DMPB_PSEUF)

Names and origin

Protein names

Recommended name:
    Metapyrocatechase
      Short name=MPC
    EC=1.13.11.2
Alternative name(s):
    CatO2ase
    Catechol 2,3-dioxygenase
      Short name=C23O

Gene names

Name:

dmpB

Encoded on

Plasmid pVI150

Organism

Pseudomonas sp. (strain CF600)

Taxonomic identifier

79676 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria

Protein attributes

Sequence length	307 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	Catechol + O2 = 2-hydroxymuconate semialdehyde.
Cofactor	Fe2+ ion.
Pathway	Aromatic compound metabolism; benzoic acid degradation via hydroxylation.
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the extradiol ring-cleavage dioxygenase family.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Plasmid
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	catechol 2,3-dioxygenase activity Inferred from electronic annotation. Source: EC ferrous iron binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 307	307	Metapyrocatechase		PRO_0000085029
Sites
	Metal binding	153	1	Iron By similarity
	Metal binding	214	1	Iron By similarity
	Metal binding	265	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	P17262-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 96439652C23800BF	FASTA	307	35,255
	10 20 30 40 50 60 MKKGVMRPGH VQLRVLNLES ALAHYRDLLG LIEMDRDEQG RVYLKAWTEV DKFSVVLREA 70 80 90 100 110 120 DQPGMDFMGF KVIDEDCLNR LTQDLLNYGC LIETIPAGEL KGCGRRVRFQ TPSGHFFELY 130 140 150 160 170 180 ADKEYTGKWG LEEINPEAWP RNLKGMRAVR FDHCLLYGDE LQATYALFTE VLGFYLAEQV 190 200 210 220 230 240 IDDDGTRVAQ FLSLSTKAHD VAFIHCPEKG KFHHVSFFLE TWEDVLRAAD LISMTDTSID 250 260 270 280 290 300 IGPTRHGLTH GKTIYFFDPS GNRNEVFCGG DYNYQDHKPV TWLAKDLGKA IFYHDRVLNE RFLTVLT

References

[1]	"Nucleotide sequence and expression of the catechol 2,3-dioxygenase-encoding gene of phenol-catabolizing Pseudomonas CF600." Bartilson M., Shingler V. Gene 85:233-238(1989) [PubMed: 2620833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Nucleotide sequences of the meta-cleavage pathway enzymes 2-hydroxymuconic semialdehyde dehydrogenase and 2-hydroxymuconic semialdehyde hydrolase from Pseudomonas CF600." Nordlund I., Shingler V. Biochim. Biophys. Acta 1049:227-230(1990) [PubMed: 2194577] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 287-307.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M33263 Genomic DNA. Translation: AAA27512.1. X52805 Genomic DNA. Translation: CAA36991.1.
PIR	JQ0182.
3D structure databases
HSSP	HSSP built from PDB template 1MPY based on UniProtKB P06622.
SMR	P17262. Positions 1-307.
ModBase	Search...
Family and domain databases
InterPro	IPR017624. Catechol_2-3_dOase. IPR004360. Glyas_bleo-R_dOase. IPR000486. Xdiol_dOase_1_2. [Graphical view]
Pfam	PF00903. Glyoxalase. 2 hits. [Graphical view]
ProDom	PD002334. Gly_diox. 2 hits. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR03211. catechol_2_3. 1 hit.
PROSITE	PS00082. EXTRADIOL_DIOXYGENAS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DMPB_PSEUF

Accession

Primary (citable) accession number: P17262

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)