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P17262 (DMPB_PSEUF) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 onPlasmid pVI150
OrganismPseudomonas sp. (strain CF600)
Taxonomic identifier79676 [NCBI]
Taxonomic lineageBacteriaProteobacteria

Protein attributes

Sequence length307 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Catechol + O2 = 2-hydroxymuconate semialdehyde.

Cofactor

Fe2+ ion.

Pathway

Aromatic compound metabolism; benzoate degradation via hydroxylation.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the extradiol ring-cleavage dioxygenase family.

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   Technical termPlasmid
Gene Ontology (GO)
   Biological processaromatic compound catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncatechol 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 307307Metapyrocatechase
PRO_0000085029

Sites

Metal binding1531Iron By similarity
Metal binding2141Iron By similarity
Metal binding2651Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
P17262 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 96439652C23800BF

FASTA30735,255
        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 

« Hide

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

EMBL
GenBank
DDBJ
M33263 Genomic DNA. Translation: AAA27512.1.
X52805 Genomic DNA. Translation: CAA36991.1.
PIRJQ0182.

3D structure databases

ProteinModelPortalP17262.
SMRP17262. Positions 1-307.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR017624. Catechol_2-3_dOase.
IPR004360. Glyas_Fos-R_dOase.
IPR000486. Xdiol_ring_cleave_dOase_1/2.
[Graphical view]
PfamPF00903. Glyoxalase. 1 hit.
[Graphical view]
TIGRFAMsTIGR03211. Catechol_2_3. 1 hit.
PROSITEPS00082. EXTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDMPB_PSEUF
AccessionPrimary (citable) accession number: P17262
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: September 21, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families