[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 23975 / B-10 / NCIB 12602 / Biotype A; PubMed=8407791 [NCBI, ExPASy, EBI, Israel, Japan] Frazee R.W., Livingston D.M., Laporte D.C., Lipscomb J.D.; "Cloning, sequencing, and expression of the Pseudomonas putida protocatechuate 3,4-dioxygenase genes."; J. Bacteriol. 175:6194-6202(1993).
[2]	PROTEIN SEQUENCE OF 2-201. STRAIN=ATCC 23975 / B-10 / NCIB 12602 / Biotype A; PubMed=465136 [NCBI, ExPASy, EBI, Israel, Japan] Kohlmiller N.A., Howard J.B.; "The primary structure of the alpha subunit of protocatechuate 3,4-dioxygenase. II. Isolation and sequence of overlap peptides and complete sequence."; J. Biol. Chem. 254:7309-7315(1979).
[3]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). DOI=10.1038/336403a0; PubMed=3194022 [NCBI, ExPASy, EBI, Israel, Japan] Ohlendorf D.H., Lipscomb J.D., Weber P.C.; "Structure and assembly of protocatechuate 3,4-dioxygenase."; Nature 336:403-405(1988).
[4]	X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS). STRAIN=ATCC 23975 / B-10 / NCIB 12602 / Biotype A; DOI=10.1006/jmbi.1994.1754; PubMed=7990141 [NCBI, ExPASy, EBI, Israel, Japan] Ohlendorf D.H., Orville A.M., Lipscomb J.D.; "Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15-A resolution."; J. Mol. Biol. 244:586-608(1994).
[5]	X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS). STRAIN=ATCC 23975 / B-10 / NCIB 12602 / Biotype A; DOI=10.1021/bi970468n; PubMed=9254599 [NCBI, ExPASy, EBI, Israel, Japan] Orville A.M., Elango N., Lipscomb J.D., Ohlendorf D.H.; "Structures of competitive inhibitor complexes of protocatechuate 3,4-dioxygenase: multiple exogenous ligand binding orientations within the active site."; Biochemistry 36:10039-10051(1997).
[6]	X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS). STRAIN=ATCC 23975 / B-10 / NCIB 12602 / Biotype A; DOI=10.1021/bi970469f; PubMed=9254600 [NCBI, ExPASy, EBI, Israel, Japan] Orville A.M., Lipscomb J.D., Ohlendorf D.H.; "Crystal structures of substrate and substrate analog complexes of protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in response to substrate binding."; Biochemistry 36:10052-10066(1997).
[7]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). STRAIN=ATCC 23975 / B-10 / NCIB 12602 / Biotype A; DOI=10.1021/bi970691k; PubMed=9298971 [NCBI, ExPASy, EBI, Israel, Japan] Elgren T.E., Orville A.M., Kelly K.A., Lipscomb J.D., Ohlendorf D.H., Que L. Jr.; "Crystal structure and resonance Raman studies of protocatechuate 3,4-dioxygenase complexed with 3,4-dihydroxyphenylacetate."; Biochemistry 36:11504-11513(1997).

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 Fe(3+) ion per subunit.
PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway; 3-carboxy-cis,cis-muconate from 3,4-dihydroxybenzoate: step 1/1 .
SUBUNIT: The enzyme is an oligomer of 12 copies of the alpha and beta chains.
SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CAUTION: Strain ATCC 23975 was originally classified as being from Pseudomonas aeruginosa.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L14836; AAB41025.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B36930; DAPSAA.

3D structure databases

PDB

1YKK; X-ray; 2.06 A; A/C/E/G/I/K=1-201.	[ExPASy / RCSB / EBI]
1YKL; X-ray; 2.25 A; A/C/E/G/I/K=1-201.	[ExPASy / RCSB / EBI]
1YKM; X-ray; 2.22 A; A/C/E/G/I/K=1-201.	[ExPASy / RCSB / EBI]
1YKN; X-ray; 2.06 A; A/C/E/G/I/K=1-201.	[ExPASy / RCSB / EBI]
1YKO; X-ray; 2.54 A; A/C/E/G/I/K=1-201.	[ExPASy / RCSB / EBI]
1YKP; X-ray; 2.41 A; A/C/E/G/I/K=1-201.	[ExPASy / RCSB / EBI]
2PCD; X-ray; 2.15 A; A/B/C/D/E/F=1-201.	[ExPASy / RCSB / EBI]
3PCA; X-ray; 2.20 A; A/B/C/D/E/F=1-201.	[ExPASy / RCSB / EBI]
3PCB; X-ray; 2.19 A; A/B/C/D/E/F=1-201.	[ExPASy / RCSB / EBI]
3PCC; X-ray; 1.98 A; A/B/C/D/E/F=1-201.	[ExPASy / RCSB / EBI]
3PCD; X-ray; 2.10 A; A/B/C/D/E/F=1-201.	[ExPASy / RCSB / EBI]
3PCE; X-ray; 2.06 A; A/B/C/D/E/F=1-201.	[ExPASy / RCSB / EBI]
3PCF; X-ray; 2.15 A; A/B/C/D/E/F=1-201.	[ExPASy / RCSB / EBI]
3PCG; X-ray; 1.96 A; A/B/C/D/E/F=1-201.	[ExPASy / RCSB / EBI]
3PCH; X-ray; 2.05 A; A/B/C/D/E/F=2-201.	[ExPASy / RCSB / EBI]
3PCI; X-ray; 2.21 A; A/B/C/D/E/F=1-201.	[ExPASy / RCSB / EBI]
3PCJ; X-ray; 2.13 A; A/B/C/D/E/F=1-201.	[ExPASy / RCSB / EBI]
3PCK; X-ray; 2.13 A; A/B/C/D/E/F=1-201.	[ExPASy / RCSB / EBI]
3PCL; X-ray; 2.15 A; A/B/C/D/E/F=1-201.	[ExPASy / RCSB / EBI]
3PCM; X-ray; 2.25 A; A/B/C/D/E/F=1-201.	[ExPASy / RCSB / EBI]
3PCN; X-ray; 2.40 A; A/B/C/D/E/F=1-201.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1YKK; -.
1YKL; -.
1YKM; -.
1YKN; -.
1YKO; -.
1YKP; -.
2PCD; -.
3PCA; -.
3PCB; -.
3PCC; -.
3PCD; -.
3PCE; -.
3PCF; -.
3PCG; -.
3PCH; -.
3PCI; -.
3PCJ; -.
3PCK; -.
3PCL; -.
3PCM; -.
3PCN; -.

ModBase

P00436.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-3186; -.

Ontologies

GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000627; Intradiol_dOase_C.
IPR015889; Intradiol_dOase_core.
IPR012786; Protocat_dOase_a.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.130.10; Intradiol_dOase_core; 1.

Pfam

PF00775; Dioxygenase_C; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02423; protocat_alph; 1.

PROSITE

PS00083; INTRADIOL_DIOXYGENAS; 1.

Other

P00436; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase; Direct protein sequencing; Iron; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 201`	`200`	`Protocatechuate 3,4-dioxygenase alpha chain.`	`PRO_0000085095`
`BINDING`	`134 134`		`Protocatechuate (Potential).`
`CONFLICT`	`60 60`		`N -> D (in Ref. 2; AA sequence).`
`CONFLICT`	`77 77`		`N -> D (in Ref. 2; AA sequence).`
`TURN`	`16 18`	`3`
`HELIX`	`19 22`	`4`
`TURN`	`24 28`	`5`
`STRAND`	`49 54`	`6`
`STRAND`	`68 72`	`5`
`STRAND`	`88 90`	`3`
`STRAND`	`92 97`	`6`
`STRAND`	`104 110`	`7`
`STRAND`	`127 132`	`6`
`STRAND`	`140 146`	`7`
`HELIX`	`147 149`	`3`
`HELIX`	`150 153`	`4`
`HELIX`	`159 161`	`3`
`HELIX`	`165 168`	`4`
`HELIX`	`169 171`	`3`
`STRAND`	`172 178`	`7`
`STRAND`	`181 185`	`5`

Sequence information

Length: 201 AA [This is the length of the unprocessed precursor]

Molecular weight: 22387 Da [This is the MW of the unprocessed precursor]

CRC64: BF95DB892076FBAF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPIELLPETP SQTAGPYVHI GLALEAAGNP TRDQEIWNRL AKPDAPGEHI LLLGQVYDGN 

        70         80         90        100        110        120 
GHLVRDSFLE VWQADANGEY QDAYNLENAF NSFGRTATTF DAGEWTLHTV KPGVVNNAAG 

       130        140        150        160        170        180 
VPMAPHINIS LFARGINIHL HTRLYFDDEA QANAKCPVLN LIEQPQRRET LIAKRCEVDG 

       190        200 
KTAYRFDIRI QGEGETVFFD F

P00436 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools