Reviewed, UniProtKB/Swiss-Prot P15110 (PCXB_BURCE)

Names and origin

Protein names

Recommended name:
    Protocatechuate 3,4-dioxygenase beta chain
    EC=1.13.11.3
Alternative name(s):
    3,4-PCD

Gene names

Name:

pcaH

Organism

Burkholderia cepacia (Pseudomonas cepacia)

Taxonomic identifier

292 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

Protein attributes

Sequence length	235 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Plays an essential role in the utilization of numerous aromatic and hydroaromatic compounds via the beta-ketoadipate pathway.
Catalytic activity	3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate.
Cofactor	Binds Fe3+ ion per subunit.
Pathway	Aromatic compound metabolism; beta-ketoadipate pathway; 3-carboxy-cis,cis-muconate from 3,4-dihydroxybenzoate: step 1/1.
Subunit structure	The enzyme is an oligomer of 12 copies of the alpha and beta chains.
Sequence similarities	Belongs to the intradiol 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 protocatechuate catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	ferric iron binding Inferred from electronic annotation. Source: InterPro protocatechuate 3,4-dioxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 235	235	Protocatechuate 3,4-dioxygenase beta chain		PRO_0000085099
Sites
	Metal binding	107	1	Iron; catalytic By similarity
	Metal binding	146	1	Iron; catalytic By similarity
	Metal binding	159	1	Iron; catalytic By similarity
	Metal binding	161	1	Iron; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	P15110-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: E8D00C95C8854324	FASTA	235	26,550
	10 20 30 40 50 60 MDSPTILTPR DWPSHPAYVH PDYRSSVKRG PTRPMIPLKE RLRDQYAPVY GAEDLGPLDH 70 80 90 100 110 120 DLTKNAVKNG EPLGERIVVT GRVLDEGGKP VRNTLVEVWQ ANAAGRYVHK VDQHDAPLDP 130 140 150 160 170 180 NFLGAGRCMT DAEGRYRFLT IKPGAYPWGN HPNAWRPNHI HFSLFGDYFG SRLVTQMYFP 190 200 210 220 230 GDPLLAYDPI FQGTPEAARD RLISRFSLDT TEEGHALGYE FDIVLRGRDA TPMER

References

[1]	"Genetic organization and sequence of the Pseudomonas cepacia genes for the alpha and beta subunits of protocatechuate 3,4-dioxygenase." Zylstra G.J., Olsen R.H., Ballou D.P. J. Bacteriol. 171:5915-5921(1989) [PubMed: 2808303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	M30791 Genomic DNA. Translation: AAA25924.1.
PIR	B33487.
3D structure databases
HSSP	HSSP built from PDB template 3PCC based on UniProtKB P00437.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.13.11.3. 74079.
Family and domain databases
InterPro	IPR000627. Intradiol_dOase_C. IPR015889. Intradiol_dOase_core. IPR012785. Protocat_dOase_b. [Graphical view]
Gene3D	G3DSA:2.60.130.10. Intradiol_dOase_core. 1 hit.
Pfam	PF00775. Dioxygenase_C. 1 hit. [Graphical view]
TIGRFAMs	TIGR02422. protocat_beta. 1 hit.
PROSITE	PS00083. INTRADIOL_DIOXYGENAS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PCXB_BURCE

Accession

Primary (citable) accession number: P15110

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	June 16, 2009
This is version 56 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)