Reviewed, UniProtKB/Swiss-Prot P00436 (PCXA_PSEPU)

Names and origin

Protein names

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

Gene names

Name:

pcaG

Organism

Pseudomonas putida

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	201 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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.
Caution	Strain ATCC 23975 was originally classified as being from Pseudomonas aeruginosa.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	Iron
Molecular function	Dioxygenase Oxidoreductase
Technical term	3D-structure Direct protein sequencing
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
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

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 201

200

Protocatechuate 3,4-dioxygenase alpha chain

PRO_0000085095

Sites

Binding site

134

1

Protocatechuate Potential

Experimental info

Sequence conflict

60

1

N → D AA sequence Ref.2

Sequence conflict

77

1

N → D AA sequence Ref.2

Secondary structure

1

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201

Helix Strand Turn

Details...

Turn

16 – 18

3

Helix

19 – 22

4

Turn

24 – 28

5

Beta strand

49 – 54

6

Beta strand

68 – 72

5

Beta strand

88 – 90

3

Beta strand

92 – 97

6

Beta strand

104 – 110

7

Beta strand

127 – 132

6

Beta strand

140 – 146

7

Helix

147 – 149

3

Helix

150 – 153

4

Helix

159 – 161

3

Helix

165 – 168

4

Helix

169 – 171

3

Beta strand

172 – 178

7

Beta strand

181 – 185

5

Sequences

	Sequence		Length	Mass (Da)
	P00436-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: BF95DB892076FBAF	FASTA	201	22,387
	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

References

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

Cross-references

Sequence databases

EMBLGenBankDDBJ

L14836 Genomic DNA. Translation: AAB41025.1.

PIR

DAPSAA. B36930.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YKK	X-ray	2.06	A/C/E/G/I/K	2-200	[»]
1YKL	X-ray	2.25	A/C/E/G/I/K	2-200	[»]
1YKM	X-ray	2.22	A/C/E/G/I/K	2-200	[»]
1YKN	X-ray	2.06	A/C/E/G/I/K	2-200	[»]
1YKO	X-ray	2.54	A/C/E/G/I/K	2-200	[»]
1YKP	X-ray	2.41	A/C/E/G/I/K	2-200	[»]
2PCD	X-ray	2.15	A/B/C/D/E/F	2-201	[»]
3PCA	X-ray	2.20	A/B/C/D/E/F	2-201	[»]
3PCB	X-ray	2.19	A/B/C/D/E/F	2-201	[»]
3PCC	X-ray	1.98	A/B/C/D/E/F	2-201	[»]
3PCD	X-ray	2.10	A/B/C/D/E/F	2-200	[»]
3PCE	X-ray	2.06	A/B/C/D/E/F	2-201	[»]
3PCF	X-ray	2.15	A/B/C/D/E/F	2-201	[»]
3PCG	X-ray	1.96	A/B/C/D/E/F	2-201	[»]
3PCH	X-ray	2.05	A/B/C/D/E/F	2-201	[»]
3PCI	X-ray	2.21	A/B/C/D/E/F	2-201	[»]
3PCJ	X-ray	2.13	A/B/C/D/E/F	2-201	[»]
3PCK	X-ray	2.13	A/B/C/D/E/F	2-201	[»]
3PCL	X-ray	2.15	A/B/C/D/E/F	2-201	[»]
3PCM	X-ray	2.25	A/B/C/D/E/F	2-201	[»]
3PCN	X-ray	2.40	A/B/C/D/E/F	2-201	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MON-3186.

BRENDA

1.13.11.3. 403.

Family and domain databases

InterPro

IPR000627. Intradiol_dOase_C.
IPR015889. Intradiol_dOase_core.
IPR012786. Protocat_dOase_a.
[Graphical view]

Gene3D

G3DSA:2.60.130.10. Intradiol_dOase_core. 1 hit.

Pfam

PF00775. Dioxygenase_C. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02423. protocat_alph. 1 hit.

PROSITE

PS00083. INTRADIOL_DIOXYGENAS. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PCXA_PSEPU

Accession

Primary (citable) accession number: P00436

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 77 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)