[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P., Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.; Submitted (SEP-2006) 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

CP000647; ABR77549.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001335779.1; -.

3D structure databases

ModBase

A6TAC8.

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; 2.

Pfam

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

BLOCKS

A6TAC8.

Genome annotation databases

GeneID

5340517; -.

GenomeReviews

CP000647_GR; KPN78578_20880.

KEGG

kpn:KPN_02121; -.

CMR

A6TAC8; KPN78578_20880.

Other

ProtoNet

A6TAC8.

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`	`1 314`	`314`	`2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase.`	`PRO_0000337652`
`ACT_SITE`	`115 115`		`Proton donor (By similarity).`
`ACT_SITE`	`179 179`		`Proton acceptor (By similarity).`

Sequence information

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

Molecular weight: 34404 Da [This is the MW of the unprocessed precursor]

CRC64: 1B7069BDD1A9C77B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHAYLHCLSH TPLVGFVDPE QAVLDEVNRV IADARRRIAE FDPELVVLFA PDHYNGFFYD 

        70         80         90        100        110        120 
VMPPFCLGIG ATAIGDFASA AGDLPVPAEL AEACAHAILN SGIDLAVSYN MQVDHGFAQP 

       130        140        150        160        170        180 
LEFLLGGLDR VPVLPVFING VAAPLPGFQR TRLLGEAMGR FLNTLNKRVL ILGSGGLSHQ 

       190        200        210        220        230        240 
PPVPELAKAD AHLRDRLLGG GKQLPPDERE RRQQRVISAA RRFTEDPHSL HPLNPVWDNR 

       250        260        270        280        290        300 
FMSLLEQGRL SELDAIGNDE LSAMAGKSTH EIKTWVAAFA ALSAFGRWRS EGRYYRPIPE 

       310 
WIAGFGSLSA TTEI

A6TAC8 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