NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 23-34.
STRAIN=SYK-6;
PubMed=2185230 [NCBI, ExPASy, EBI, Israel, Japan]
Noda Y., Nishikawa S., Shiozuka K., Kadokura H., Nakajima H., Yoda K., Katayama Y., Morohoshi N., Haraguchi T., Yamasaki M.;
"Molecular cloning of the protocatechuate 4,5-dioxygenase genes of Pseudomonas paucimobilis.";
J. Bacteriol. 172:2704-2709(1990).

Comments

FUNCTION: Responsible for the aromatic ring fission of protocatechuate.
CATALYTIC ACTIVITY: Protocatechuate + O₂ = 4-carboxy-2-hydroxymuconate semialdehyde.
COFACTOR: Fe(2+) ion.
SUBUNIT: Composed of two subunits (alpha and beta) in a 1:1 ratio.

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

M34835; AAA17727.1; -; Unassigned_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A35271; A35271.

3D structure databases

PDB

1B4U; X-ray; 2.20 A; A/C=1-139.	[ExPASy / RCSB / EBI]
1BOU; X-ray; 2.20 A; A/C=1-139.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1B4U; -.
1BOU; -.

ModBase

P22635.

Protein-protein interaction databases

IntAct

P22635; -.

Ontologies

GO:0018579;	Molecular function: protocatechuate 4,5-dioxygenase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR014159; PCA_ligA.
IPR011986; Xdiol_dOase_LigA.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.700.10; Xdiol_dOase_LigA; 1.

Pfam

PF07746; LigA; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02792; PCA_ligA; 1.

Other

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`
`CHAIN`	`1 139`	`139`	`Protocatechuate 4,5-dioxygenase alpha chain.`	`PRO_0000085100`
`HELIX`	`10 15`	`6`
`HELIX`	`16 19`	`4`
`HELIX`	`28 33`	`6`
`HELIX`	`35 43`	`9`
`HELIX`	`47 55`	`9`
`HELIX`	`57 62`	`6`
`TURN`	`63 65`	`3`
`HELIX`	`68 76`	`9`
`HELIX`	`79 84`	`6`
`HELIX`	`89 98`	`10`
`HELIX`	`103 109`	`7`
`TURN`	`110 112`	`3`
`HELIX`	`115 123`	`9`
`TURN`	`135 137`	`3`

Sequence information

Length: 139 AA [This is the length of the unprocessed precursor]

Molecular weight: 15549 Da [This is the MW of the unprocessed precursor]

CRC64: E6CFEF0499A3FD26 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTEKKERIDV HAYLAEFDDI PGTRVFTAQR ARKGYNLNQF AMSLMKAENR ERFKADESAY 

        70         80         90        100        110        120 
LDEWNLTPAA KAAVLARDYN AMIDEGGNVY FLSKLFSTDG KSFQFAAGSM TGMTQEEYAQ 

       130 
MMIDGGRSPA GVRSIKGGY

P22635 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