Reviewed, UniProtKB/Swiss-Prot Q53034 (CATA_RHORH)

Names and origin

Protein names

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

Gene names

Name:

catA

Organism

Rhodococcus rhodochrous

Taxonomic identifier

1829 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length	318 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 By similarity.
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
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 xenobiotic catabolic process Inferred from electronic annotation. Source: InterPro
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 – 318	318	Metapyrocatechase		PRO_0000085031
Sites
	Metal binding	146	1	Iron By similarity
	Metal binding	209	1	Iron By similarity
	Metal binding	259	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q53034-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: ED9EB5EAA9659058	FASTA	318	35,438
	10 20 30 40 50 60 MALVTGIGYI GIGVSDLPAW EEFAETIGFQ IRERGEDGTL YLRMDKAHHR VAVHPTGEDD 70 80 90 100 110 120 LTYVGWQVAD ENGFDELERT LRAAGVPVEM AGEDDAELRG VARLMRFEDP SGIKSEAYYG 130 140 150 160 170 180 LVSEPEVPYV SPYAVDFVTE DQGFGHIVVM VDDYDETMRF YREVLGLQTS DLVKVGAGGV 190 200 210 220 230 240 QTRMAFMRCN PRQHSLAFWA GDSTTRLNHF MLQTQTLDQT GMTLDRCFHG GIPATNLGRH 250 260 270 280 290 300 VNDYAVSFYI TTPSGFMIEY GWGVREVVSD YPVDKYRSVS IWGHRNLDGI HYTQALPPEA 310 AESPAEQHLV EEPVAAAV

References

[1]

"Cloning of new Rhodococcus extradiol dioxygenase genes and study of their distribution in different Rhodococcus strains." Kulakov L.A., Delcroix V.A., Larkin M.J., Ksenzenko V.N., Kulakova A.N. Microbiology 144:955-963(1998) [PubMed: 9579069] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NCIMB 13064 / Isolate P200.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L77225 Genomic DNA. Translation: AAC18907.1.
3D structure databases
HSSP	HSSP built from PDB template 1DHY based on UniProtKB P17297.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.13.11.2. 343.
Family and domain databases
InterPro	IPR017626. DiOHbiphenyl_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	TIGR03213. 23dbph12diox. 1 hit.
PROSITE	PS00082. EXTRADIOL_DIOXYGENAS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CATA_RHORH

Accession

Primary (citable) accession number: Q53034

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	March 3, 2009
This is version 41 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)