FUNCTION: Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-ketononatrienedioate, respectively (By similarity).
CATALYTIC ACTIVITY: 3-(2,3-dihydroxyphenyl)propanoate + O₂ = 2-hydroxy-6-oxonona-2,4-diene-1,9-dioate.
CATALYTIC ACTIVITY: 2,3-dihydroxicinnamic acid + O₂ = 2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate.
COFACTOR: Fe(2+) ion (By similarity).
PATHWAY: Aromatic compound metabolism; 3-phenylpropionic acid degradation .
SUBUNIT: Homotetramer (By similarity).
SIMILARITY: Belongs to the ligB/mhpB extradiol dioxygenase family.

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

CP000325; ABL03071.1; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_904542.1; -.

3D structure databases

ModBase

A0PL52.

Organism-specific databases

BuruList

MUL_0347; -.

Ontologies

GO:0008669;	Molecular function: 2,3-dihydroxy-phenylpropionate 1,2-dioxygenase activity (inferred from electronic annotation from HAMAP).
GO:0047070;	Molecular function: 3-carboxyethylcatechol 2,3-dioxygenase activity (inferred from electronic annotation from EC).
GO:0019439;	Biological process: aromatic compound catabolic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01653; -; 1.
PBIL [Tree]

InterPro

IPR004183; Xdiol_dOase_3B.
Graphical view of domain structure.

Pfam

PF02900; LigB; 1.
Pfam graphical view of domain structure.

BLOCKS

A0PL52.

Genome annotation databases

GeneID

4550878; -.

GenomeReviews

CP000325_GR; MUL_0347.

KEGG

mul:MUL_0347; -.

CMR

A0PL52; MUL_0347.

Other

ProtoNet

A0PL52.

UniRef

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

Keywords

Aromatic hydrocarbons catabolism; Complete proteome; Dioxygenase; Iron; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 313`	`313`	`2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase.`	`PRO_0000337659`
`ACT_SITE`	`115 115`		`Proton donor (By similarity).`
`ACT_SITE`	`179 179`		`Proton acceptor (By similarity).`

Sequence information

Length: 313 AA [This is the length of the unprocessed precursor]

Molecular weight: 33564 Da [This is the MW of the unprocessed precursor]

CRC64: 0EB633671CBFC800 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALALCRMSH SPLLNLPGPR LDLLDEVHAA IAEAAEFVRA YDPDLVVIFS PDHYNGFFYR 

        70         80         90        100        110        120 
AMHPFCIGMY ASAVGDYGTH IGALDVPTDL AADCAKAVLG ADVDVAVSAS MDVDHGTVQP 

       130        140        150        160        170        180 
LEKLFGTATA RPVIPIFINA IAAPLGPLRR CRALGTAVGT FLSTLDLRVL VIGSGGLSHS 

       190        200        210        220        230        240 
PPVPTLHSAD PQVRERIVHG QPLTPAQRQA RQTVVMEAAK SFAAGNSDLQ PLNPAWDQRF 

       250        260        270        280        290        300 
LEIIDNGHLS DLDRWSNSFV THEGGSLAHE IRTWISAFAA MAVAGPYQTK VRYYKQAADL 

       310 
IAGFAIRTAV PIP

A0PL52 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