[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PLASMID=pHMT112; STRAIN=ML2; Panicker G., Tan H.M.; "mhpB from Pseudomonas putida ML2."; Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PLASMID=pKW1; STRAIN=GJ31; Reineke W., Kunze M.; "GJ31 meta-operon."; Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.

Comments

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

AF176355; AAG09232.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY831461; AAX50134.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q9F9U5.

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:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0008198;	Molecular function: ferrous iron binding (inferred from electronic annotation from InterPro).
GO:0019439;	Biological process: aromatic compound catabolic process (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

ProtoNet

Q9F9U5.

Other

UniRef

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

Keywords

Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Oxidoreductase; Plasmid.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 314`	`314`	`2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase 2.`	`PRO_0000337663`
`ACT_SITE`	`115 115`		`Proton donor (By similarity).`
`ACT_SITE`	`179 179`		`Proton acceptor (By similarity).`
`CONFLICT`	`20 20`		`N -> T (in Ref. 1; AAX50134).`
`CONFLICT`	`70 70`		`E -> A (in Ref. 1; AAX50134).`
`CONFLICT`	`81 81`		`A -> V (in Ref. 1; AAX50134).`
`CONFLICT`	`89 90`		`DV -> EL (in Ref. 1; AAX50134).`
`CONFLICT`	`122 122`		`D -> E (in Ref. 1; AAX50134).`
`CONFLICT`	`156 156`		`D -> E (in Ref. 1; AAX50134).`
`CONFLICT`	`203 203`		`N -> D (in Ref. 1; AAX50134).`
`CONFLICT`	`215 215`		`R -> Q (in Ref. 1; AAX50134).`
`CONFLICT`	`226 226`		`N -> D (in Ref. 1; AAX50134).`
`CONFLICT`	`239 239`		`R -> Q (in Ref. 1; AAX50134).`
`CONFLICT`	`250 250`		`L -> V (in Ref. 1; AAX50134).`
`CONFLICT`	`259 259`		`A -> S (in Ref. 1; AAX50134).`
`CONFLICT`	`283 283`		`S -> A (in Ref. 1; AAX50134).`

Sequence information

Length: 314 AA [This is the length of the unprocessed precursor]

Molecular weight: 34581 Da [This is the MW of the unprocessed precursor]

CRC64: F1B8670FF5D5BD50 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNAYLHCLSH TPLIGHFDPN QDVLDEVAEV VRAARARIEA FNPELVVLFA PDHYNGFFYD 

        70         80         90        100        110        120 
VMPPFCLGME AEAIGDFGSL AGTLSVPKDV AEACAESVLT SGIDLAVSYR MQVDHGFAQP 

       130        140        150        160        170        180 
LDFLLGGLDK YPVLPVFVNC VAPPLPTFER VRLLGDAIGR FTRGLNKRVL FLGSGGLSHQ 

       190        200        210        220        230        240 
PPVPELAKVD ARMADRLMGS GRNLPPEERD ARTQRVVVAA ERFVENQNTL HPLNPKWDRY 

       250        260        270        280        290        300 
FLDVVEQDLL SQLDDLSNAH LSELAGKSTH EVKAWVAAFS ALSAHGAYTA TDRYYRPIPE 

       310 
WIAGFGSISA HTQR

Q9F9U5 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