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

CP000580; ABN99565.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001072056.1; -.

3D structure databases

ModBase

A3Q338.

Ontologies

GO:0008669;	Molecular function: 2,3-dihydroxy-phenylpropionate 1,2-dioxygenase activity (inferred from electronic annotation from HAMAP).
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.

Gene3D

G3DSA:3.40.830.10; Xdiol_dOase_3B; 1.

Pfam

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

BLOCKS

A3Q338.

Genome annotation databases

GeneID

4879499; -.

GenomeReviews

CP000580_GR; Mjls_3789.

KEGG

mjl:Mjls_3789; -.

CMR

A3Q338; Mjls_3789.

Other

ProtoNet

A3Q338.

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_0000337656`
`ACT_SITE`	`116 116`		`Proton donor (By similarity).`
`ACT_SITE`	`180 180`		`Proton acceptor (By similarity).`

Sequence information

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

Molecular weight: 33047 Da [This is the MW of the unprocessed precursor]

CRC64: 2FE96B1CB6B9219F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAQIALCCTS HSPLLNLPGP SRELLDDIGS ALAVARDFVT EFDPDLVVTF SPDHYNGFFY 

        70         80         90        100        110        120 
KVMPPFCVGT SAQGVGDYGT HAGPLDVPED LANELATAVL EAGVDVAISA SMDVDHGTVQ 

       130        140        150        160        170        180 
PLQNLFGDAM ARPVIPVFIN SVATPLGPLR RTRALGTAIG RYLATLDKRV LVIGSGGLSH 

       190        200        210        220        230        240 
DPPVPTLATA PPAALDRIVH GAPMSTEQRM ARQSAVIDAA HAFAHGESPL QPLNPAWDAT 

       250        260        270        280        290        300 
FLEILDEGWL SDLDGWSNAF IAREGGNSAH EIRTWVAAFA ALAAGGDYRT GLRFYRAAPE 

       310 
LIAGFAIRTA VLA

A3Q338 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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