[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 2-239. PubMed=115853 [NCBI, ExPASy, EBI, Israel, Japan] Iwaki M., Kagamiyama H., Nozaki M.; "The complete amino acid sequence of the beta-subunit of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa."; J. Biochem. 86:1159-1162(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; AAB41024.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A36930; DAPSBA.

3D structure databases

PDB

1YKK; X-ray; 2.06 A; B/D/F/H/J/L=1-239.	[ExPASy / RCSB / EBI]
1YKL; X-ray; 2.25 A; B/D/F/H/J/L=1-239.	[ExPASy / RCSB / EBI]
1YKM; X-ray; 2.22 A; B/D/F/H/J/L=1-239.	[ExPASy / RCSB / EBI]
1YKN; X-ray; 2.06 A; B/D/F/H/J/L=1-239.	[ExPASy / RCSB / EBI]
1YKO; X-ray; 2.54 A; B/D/F/H/J/L=1-239.	[ExPASy / RCSB / EBI]
1YKP; X-ray; 2.41 A; B/D/F/H/J/L=1-239.	[ExPASy / RCSB / EBI]
2PCD; X-ray; 2.15 A; M/N/O/P/Q/R=1-239.	[ExPASy / RCSB / EBI]
3PCA; X-ray; 2.20 A; M/N/O/P/Q/R=1-239.	[ExPASy / RCSB / EBI]
3PCB; X-ray; 2.19 A; M/N/O/P/Q/R=1-239.	[ExPASy / RCSB / EBI]
3PCC; X-ray; 1.98 A; M/N/O/P/Q/R=1-239.	[ExPASy / RCSB / EBI]
3PCD; X-ray; 2.10 A; M/N/O/P/Q/R=1-239.	[ExPASy / RCSB / EBI]
3PCE; X-ray; 2.06 A; M/N/O/P/Q/R=1-239.	[ExPASy / RCSB / EBI]
3PCF; X-ray; 2.15 A; M/N/O/P/Q/R=1-239.	[ExPASy / RCSB / EBI]
3PCG; X-ray; 1.96 A; M/N/O/P/Q/R=1-239.	[ExPASy / RCSB / EBI]
3PCH; X-ray; 2.05 A; M/N/O/P/Q/R=2-239.	[ExPASy / RCSB / EBI]
3PCI; X-ray; 2.21 A; M/N/O/P/Q/R=1-239.	[ExPASy / RCSB / EBI]
3PCJ; X-ray; 2.13 A; M/N/O/P/Q/R=1-239.	[ExPASy / RCSB / EBI]
3PCK; X-ray; 2.13 A; M/N/O/P/Q/R=1-239.	[ExPASy / RCSB / EBI]
3PCL; X-ray; 2.15 A; M/N/O/P/Q/R=1-239.	[ExPASy / RCSB / EBI]
3PCM; X-ray; 2.25 A; M/N/O/P/Q/R=1-239.	[ExPASy / RCSB / EBI]
3PCN; X-ray; 2.40 A; M/N/O/P/Q/R=1-239.	[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

P00437.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-3185; -.

Ontologies

GO:0019439;	Biological process: aromatic compound catabolic process (inferred from electronic annotation from UniProtKB-KW).
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.
IPR012785; Protocat_dOase_b.
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

TIGR02422; protocat_beta; 1.

PROSITE

PS00083; INTRADIOL_DIOXYGENAS; 1.

Other

P00437; -.

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 239`	`238`	`Protocatechuate 3,4-dioxygenase beta chain.`	`PRO_0000085098`
`METAL`	`109 109`		`Iron; catalytic.`
`METAL`	`148 148`		`Iron; catalytic.`
`METAL`	`161 161`		`Iron; catalytic.`
`METAL`	`163 163`		`Iron; catalytic.`
`CONFLICT`	`62 62`		`H -> D (in Ref. 2; AA sequence).`
`CONFLICT`	`70 70`		`N -> D (in Ref. 2; AA sequence).`
`CONFLICT`	`72 72`		`Missing (in Ref. 2; AA sequence).`
`CONFLICT`	`218 218`		`D -> N (in Ref. 2; AA sequence).`
`STRAND`	`7 9`	`3`
`TURN`	`14 16`	`3`
`HELIX`	`26 28`	`3`
`TURN`	`29 31`	`3`
`HELIX`	`44 47`	`4`
`TURN`	`59 62`	`4`
`TURN`	`64 66`	`3`
`STRAND`	`70 72`	`3`
`STRAND`	`78 87`	`10`
`STRAND`	`97 102`	`6`
`STRAND`	`127 131`	`5`
`STRAND`	`136 143`	`8`
`STRAND`	`148 153`	`6`
`STRAND`	`156 158`	`3`
`STRAND`	`160 166`	`7`
`TURN`	`171 173`	`3`
`STRAND`	`175 181`	`7`
`HELIX`	`187 189`	`3`
`TURN`	`191 195`	`5`
`HELIX`	`199 203`	`5`
`STRAND`	`206 209`	`4`
`TURN`	`216 218`	`3`
`STRAND`	`219 223`	`5`
`STRAND`	`226 228`	`3`
`STRAND`	`231 233`	`3`

Sequence information

Length: 239 AA [This is the length of the unprocessed precursor]

Molecular weight: 26793 Da [This is the MW of the unprocessed precursor]

CRC64: 8F8CC293B6E434CE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPAQDNSRFV IRDRNWHPKA LTPDYKTSIA RSPRQALVSI PQSISETTGP NFSHLGFGAH 

        70         80         90        100        110        120 
DHDLLLNFNN GGLPIGERII VAGRVVDQYG KPVPNTLVEM WQANAGGRYR HKNDRYLAPL 

       130        140        150        160        170        180 
DPNFGGVGRC LTDSDGYYSF RTIKPGPYPW RNGPNDWRPA HIHFGISGPS IATKLITQLY 

       190        200        210        220        230 
FEGDPLIPMC PIVKSIANPE AVQQLIAKLD MNNANPMDCL AYRFDIVLRG QRKTHFENC

P00437 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