[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND BIOPHYSICOCHEMICAL PROPERTIES. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; PubMed=8752345 [NCBI, ExPASy, EBI, Israel, Japan] Spence E.L., Kawamukai M., Sanvoisin J., Braven H., Bugg T.D.H.; "Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes eutrophus (MpcI): sequence analysis and biochemical properties of a third family of extradiol dioxygenases."; J. Bacteriol. 178:5249-5256(1996).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12 / CS520; PubMed=9098055 [NCBI, ExPASy, EBI, Israel, Japan] Ferrandez A., Garcia J.L., Diaz E.; "Genetic characterization and expression in heterologous hosts of the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12."; J. Bacteriol. 179:2573-2581(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; "Sequence of minutes 4-25 of Escherichia coli."; Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[6]	PROTEIN SEQUENCE OF 1-15, SUBUNIT, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR. DOI=10.1016/0167-4838(93)90013-H; PubMed=8399388 [NCBI, ExPASy, EBI, Israel, Japan] Bugg T.D.H.; "Overproduction, purification and properties of 2,3-dihydroxyphenylpropionate 1,2-dioxygenase from Escherichia coli."; Biochim. Biophys. Acta 1202:258-264(1993).
[7]	MUTAGENESIS OF ASP-114; HIS-115; HIS-179 AND PRO-181, AND REACTION MECHANISM. DOI=10.1021/bi048518t; PubMed=15491145 [NCBI, ExPASy, EBI, Israel, Japan] Mendel S., Arndt A., Bugg T.D.H.; "Acid-base catalysis in the extradiol catechol dioxygenase reaction mechanism: site-directed mutagenesis of His-115 and His-179 in Escherichia coli 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB)."; Biochemistry 43:13390-13396(2004).

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.
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.

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=26 µM for 2,3-dihydroxyphenylpropionic acid (at 20 degrees Celsius and pH 8);
	K_M=36 µM for 2,3-dihydroxycinnamic acid (at 20 degrees Celsius and pH 8);
	K_M=37 µM for methyl-2,3-dihydroxyphenylpropionate (at 20 degrees Celsius and pH 8);
	K_M=90 µM for 3-methylcatechol (at 20 degrees Celsius and pH 8);
	K_M=94 µM for 3-phenethylcatechol (at 20 degrees Celsius and pH 8);
	K_M=154 µM for 3-propylcatechol (at 20 degrees Celsius and pH 8);
	K_M=185 µM for 3-ethylcatechol (at 20 degrees Celsius and pH 8);
	K_M=300 µM for 2,3-dihydroxyphenoxyacetic acid (at 20 degrees Celsius and pH 8);
	K_M=700 µM for catechol (at 20 degrees Celsius and pH 8);

PATHWAY: Aromatic compound metabolism; 3-phenylpropionic acid degradation .
SUBUNIT: Homotetramer.
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

D86239; BAA13053.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Y09555; CAA70748.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U73857; AAB18072.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73451.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76130.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D64762; D64762.

RefSeq

AP_001000.1; -.
NP_414882.1; -.

3D structure databases

ModBase

P0ABR9.

Enzyme and pathway databases

BioCyc

EcoCyc:DHPDIOXYGEN-MON; -.
MetaCyc:DHPDIOXYGEN-MON; -.

Organism-specific databases

EchoBASE

EB4167; -.

EcoGene

EG20274; mhpB.

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.

Genome annotation databases

GeneID

945047; -.

GenomeReviews

AP009048_GR; JW0339.
U00096_GR; b0348.

KEGG

ecj:JW0339; -.
eco:b0348; -.

Phylogenomic databases

HOGENOM

P0ABR9; -.

Genome annotation databases

CMR

P0ABR9; b0348.

Other

ProtoNet

P0ABR9.

UniRef

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

Keywords

Aromatic hydrocarbons catabolism; Complete proteome; Dioxygenase; Direct protein sequencing; 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_0000085103`
`ACT_SITE`	`115 115`		`Proton donor.`
`ACT_SITE`	`179 179`		`Proton acceptor.`
`MUTAGEN`	`114 114`		`D->A: Complete loss of extradiol cleavage activity.`
`MUTAGEN`	`114 114`		`D->N: Low level of catalytic activity, 600-fold lower than the wild-type enzyme. More than 8000-fold decrease in affinity.`
`MUTAGEN`	`115 115`		`H->A: Complete loss of extradiol cleavage activity.`
`MUTAGEN`	`115 115`		`H->Q: Complete loss of activity.`
`MUTAGEN`	`115 115`		`H->Y: Complete loss of activity.`
`MUTAGEN`	`179 179`		`H->A: Complete loss of activity.`
`MUTAGEN`	`179 179`		`H->Q: Complete loss of activity.`
`MUTAGEN`	`179 179`		`H->Y: Complete loss of activity.`
`MUTAGEN`	`181 181`		`P->A: More than 2-fold decrease in catalytic activity and 100-fold decrease in affinity.`
`MUTAGEN`	`181 181`		`P->H: More than 60-fold decrease in catalytic activity and affinity.`
`CONFLICT`	`138 140`		`ING -> NKA (in Ref. 1; BAA13053).`
`CONFLICT`	`152 152`		`R -> H (in Ref. 1; BAA13053).`
`CONFLICT`	`157 157`		`A -> T (in Ref. 1; BAA13053).`

Sequence information

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

Molecular weight: 34196 Da [This is the MW of the unprocessed precursor]

CRC64: E1D5A8574E5DFE05 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHAYLHCLSH SPLVGYVDPA QEVLDEVNGV IASARERIAA FSPELVVLFA PDHYNGFFYD 

        70         80         90        100        110        120 
VMPPFCLGVG ATAIGDFGSA AGELPVPVEL AEACAHAVMK SGIDLAVSYC MQVDHGFAQP 

       130        140        150        160        170        180 
LEFLLGGLDK VPVLPVFING VATPLPGFQR TRMLGEAIGR FTSTLNKRVL FLGSGGLSHQ 

       190        200        210        220        230        240 
PPVPELAKAD AHMRDRLLGS GKDLPASERE LRQQRVISAA EKFVEDQRTL HPLNPIWDNQ 

       250        260        270        280        290        300 
FMTLLEQGRI QELDAVSNEE LSAIAGKSTH EIKTWVAAFA AISAFGNWRS EGRYYRPIPE 

       310 
WIAGFGSLSA RTEN

P0ABR9 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