Protocatechuate 3,4-dioxygenase beta chain - Acinetobacter sp. (strain ADP1)

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Reviewed, UniProtKB/Swiss-Prot P20372 (PCXB_ACIAD)

Last modified June 16, 2009. Version 77. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
Ordered Locus Names:	ACIAD1711

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

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Protein attributes

Sequence length	241 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.

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Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	3D-structure Complete proteome 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 protocatechuate catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	ferric iron binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct protocatechuate 3,4-dioxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
pcaG	P20371	1	EBI-1029420,EBI-1029428

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 241

241

Protocatechuate 3,4-dioxygenase beta chain

PRO_0000085097

Sites

Metal binding

109

Iron; catalytic By similarity

Metal binding

148

Iron; catalytic By similarity

Metal binding

161

Iron; catalytic By similarity

Metal binding

163

Iron; catalytic By similarity

Secondary structure

241

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P20372-1 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: 0D2F945C92FE675A
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FASTA

241

27,548

        10         20         30         40         50         60 
MSQIIWGAYA QRNTEDHPPA YAPGYKTSVL RSPKNALISI AETLSEVTAP HFSADKFGPK 

        70         80         90        100        110        120 
DNDLILNYAK DGLPIGERVI VHGYVRDQFG RPVKNALVEV WQANASGRYR HPNDQYIGAM 

       130        140        150        160        170        180 
DPNFGGCGRM LTDDNGYYVF RTIKPGPYPW RNRINEWRPA HIHFSLIADG WAQRLISQFY 

       190        200        210        220        230        240 
FEGDTLIDSC PILKTIPSEQ QRRALIALED KSNFIEADSR CYRFDITLRG RRATYFENDL 


T

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequences of genes encoding Acinetobacter calcoaceticus protocatechuate 3,4-dioxygenase: evidence indicating shuffling of genes and of DNA sequences within genes during their evolutionary divergence." Hartnett C., Neidle E.L., Ngai K.-L., Ornston L.N. J. Bacteriol. 172:956-966(1990) [PubMed: 2298704] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10.
[2]	"Contrasting patterns of evolutionary divergence within the Acinetobacter calcoaceticus pca operon." Kowalchuk G.A., Hartnett G.B., Benson A., Houghton J.E., Ngai K.-L., Ornston L.N. Gene 146:23-30(1994) [PubMed: 8063101] [Abstract] Cited for: SEQUENCE REVISION TO 12; 22; 36 AND 232-241.
[3]	"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C. Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+	Additional computationally mapped references.

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Cross-references

Sequence databases

L05770 Genomic DNA. Translation: AAC37153.1.
CR543861 Genomic DNA. Translation: CAG68553.1.

PIR

C35119.

RefSeq

YP_046375.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EO2	X-ray	2.25	B	1-241	[»]
1EO9	X-ray	2.00	B	1-241	[»]
1EOA	X-ray	2.15	B	1-241	[»]
1EOB	X-ray	2.20	B	1-241	[»]
1EOC	X-ray	2.25	B	1-241	[»]
2BUM	X-ray	1.80	B	1-241	[»]
2BUQ	X-ray	1.80	B	1-241	[»]
2BUR	X-ray	1.80	B	1-241	[»]
2BUT	X-ray	1.85	B	1-241	[»]
2BUU	X-ray	1.80	B	1-241	[»]
2BUV	X-ray	1.80	B	1-241	[»]
2BUW	X-ray	1.80	B	1-241	[»]
2BUX	X-ray	1.80	B	1-241	[»]
2BUY	X-ray	1.80	B	1-241	[»]
2BUZ	X-ray	1.80	B	1-241	[»]
2BV0	X-ray	1.80	B	1-241	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P20372. 1 interaction.

Genome annotation databases

GeneID

2879437.

GenomeReviews

Gene locus ACIAD1711 in contig CR543861_GR.

KEGG

aci:ACIAD1711.

NMPDR

fig|62977.3.peg.1637.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P20372.

OMA

P20372. NFGGCGR.

Enzyme and pathway databases

BioCyc

ASP62977:ACIAD1711-MON.

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...

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Entry information

Entry name

PCXB_ACIAD

Accession

Primary (citable) accession number: P20372
Secondary accession number(s): Q43976

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	July 15, 1999
Last modified:	June 16, 2009
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents