ECMDB: 2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase (P0ABR9)

Identification

Name:

2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase

Synonyms:

Not Available

Gene Name:

mhpB

Enzyme Class:

1.13.11.16

Biological Properties

General Function:

Involved in iron ion binding

Specific 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

Cellular Location:

Not Available

SMPDB Pathways:

2-Oxopent-4-enoate metabolism PW001890
2-Oxopent-4-enoate metabolism 2 PW002035
Phenylalanine metabolism PW000921

KEGG Pathways:

Microbial metabolism in diverse environments ec01120
Phenylalanine metabolism ec00360

KEGG Reactions:

1.0

→

1.0

1.03-(2,3-Dihydroxyphenyl)propionic acid + 1.0Oxygen → 1.0Hydrogen ion + 1.02-Hydroxy-6-ketononadienedicarboxylate
ReactionCard

1.0

→

1.0

1.0Trans-2,3-Dihydroxycinnamate + 1.0Oxygen → 1.0Hydrogen ion + 1.02-Hydroxy-6-ketononatrienedioate
ReactionCard

1.0

↔

1.0

1.03-(2,3-Dihydroxyphenyl)propionic acid + 1.0Oxygen ↔ 1.02-Hydroxy-6-ketononadienedicarboxylate
ReactionCard

1.0

↔

1.0

1.0Trans-2,3-Dihydroxycinnamate + 1.0Oxygen ↔ 1.02-Hydroxy-6-ketononatrienedioate
ReactionCard

1.0

↔

1.0

1.03-(2,3-Dihydroxyphenyl)propionic acid + 1.0Oxygen + 1.0Trans-2,3-Dihydroxycinnamate ↔ 1.02-Hydroxy-6-ketononadienedicarboxylate + 1.02-Hydroxy-6-ketononatrienedioate
ReactionCard

SMPDB Reactions:

1.02-Hydroxy-3-(4-hydroxyphenyl)propenoic acid

1.0

→

1.0

1.02-Hydroxy-3-(4-hydroxyphenyl)propenoic acid + 1.0Oxygen + 1.02-Hydroxy-3-(4-hydroxyphenyl)propenoic acid → 1.0Hydrogen ion + 1.02-Hydroxy-6-ketononatrienedioate
ReactionCard

1.0

→

1.0(2E,4Z)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate

1.0

1.03-(2,3-Dihydroxyphenyl)propionic acid + 1.0Oxygen → 1.0(2E,4Z)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate + 1.0Hydrogen ion
ReactionCard

EcoCyc Reactions:

1.0

→

1.0

1.03-(2,3-Dihydroxyphenyl)propionic acid + 1.0Oxygen → 1.0Hydrogen ion + 1.02-Hydroxy-6-ketononadienedicarboxylate
ReactionCard

1.0

→

1.0

1.0Trans-2,3-Dihydroxycinnamate + 1.0Oxygen → 1.0Hydrogen ion + 1.02-Hydroxy-6-ketononatrienedioate
ReactionCard

Complex Reactions:

1.0

→

1.0

1.0Trans-2,3-Dihydroxycinnamate + 1.0Oxygen → 1.02-Hydroxy-6-ketononatrienedioate
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB24915	2-Hydroxy-3-(4-hydroxyphenyl)propenoic acid	MetaboCard
ECMDB04081	2-Hydroxy-6-ketononadienedicarboxylate	MetaboCard
ECMDB20042	2-Hydroxy-6-ketononatrienedioate	MetaboCard
ECMDB20064	3-(2,3-Dihydroxyphenyl)propanoate	MetaboCard
ECMDB04061	3-(2,3-Dihydroxyphenyl)propionic acid	MetaboCard
ECMDB21225	Hydrogen ion	MetaboCard
ECMDB04124	Oxygen	MetaboCard
ECMDB20197	Trans-2,3-Dihydroxycinnamate	MetaboCard

GO Classification:

Function
binding
catalytic activity
cation binding
ferrous iron binding
ion binding
iron ion binding
metal ion binding
oxidoreductase activity
transition metal ion binding
Process
cellular aromatic compound metabolic process
cellular metabolic process
metabolic process

Gene Properties

Blattner:

b0348

Gene Orientation

Clockwise

Centisome Percentage:

7.96

Left Sequence End

369501

Right Sequence End

370445

Gene Sequence:

>945 bp
ATGCCAGAGGTACAAACAGATCATCCAGAGACGGCGGAGTTAAGCAAACCACAGCTACGC
ATGGTCGATCTCAACTTATTAACCGTTTTCGATGCCGTGATGCAGGAGCAAAACATTACT
CGTGCCGCTCATGTTCTGGGAATGTCGCAACCTGCGGTCAGTAACGCTGTTGCACGCCTG
AAGGTGATGTTTAATGACGAGCTTTTTGTTCGTTATGGCCGTGGTATTCAACCGACTGCT
CGCGCATTTCAACTTTTTGGTTCAGTTCGTCAGGCATTGCAACTAGTACAAAATGAATTG
CCTGGTTCAGGTTTTGAACCCGCGAGCAGTGAACGTGTATTTCATCTTTGTGTTTGCAGC
CCGTTAGACAGCATTCTGACCTCGCAGATTTATAATCACATTGAGCAGATTGCGCCAAAT
ATACATGTTATGTTCAAGTCTTCATTAAATCAGAACACTGAACATCAGCTGCGTTATCAG
GAAACGGAGTTTGTGATTAGTTATGAAGACTTCCATCGTCCTGAATTTACCAGCGTACCA
TTATTTAAAGATGAAATGGTGCTGGTAGCCAGCAAAAATCATCCAACAATTAAGGGCCCG
TTACTGAAACATGATGTTTATAACGAACAACATGCGGCGGTTTCGCTCGATCGTTTCGCG
TCATTTAGTCAACCTTGGTATGACACGGTAGATAAGCAAGCCAGTATCGCGTATCAGGGC
ATGGCAATGATGAGCGTACTTAGCGTGGTGTCGCAAACGCATTTGGTCGCTATTGCGCCG
CGTTGGCTGGCTGAAGAGTTCGCTGAATCCTTAGAATTACAGGTATTACCGCTGCCGTTA
AAACAAAACAGCAGAACCTGTTATCTCTCCTGGCATGAAGCTGCCGGGCGCGATAAAGGC
CATCAGTGGATGGAAGAGCAATTAGTCTCAATTTGCAAACGCTAA

Protein Properties

Pfam Domain Function:

LigB (PF02900 )

Protein Residues:

314

Protein Molecular Weight:

34196

Protein Theoretical pI:

Signaling Regions:

None

Transmembrane Regions:

None

Protein Sequence:

>2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase
MHAYLHCLSHSPLVGYVDPAQEVLDEVNGVIASARERIAAFSPELVVLFAPDHYNGFFYD
VMPPFCLGVGATAIGDFGSAAGELPVPVELAEACAHAVMKSGIDLAVSYCMQVDHGFAQP
LEFLLGGLDKVPVLPVFINGVATPLPGFQRTRMLGEAIGRFTSTLNKRVLFLGSGGLSHQ
PPVPELAKADAHMRDRLLGSGKDLPASERELRQQRVISAAEKFVEDQRTLHPLNPIWDNQ
FMTLLEQGRIQELDAVSNEELSAIAGKSTHEIKTWVAAFAAISAFGNWRSEGRYYRPIPE
WIAGFGSLSARTEN

References

External Links:

Resource	Link
Uniprot ID:	P0ABR9
Uniprot Name:	MHPB_ECOLI
GenBank Gene ID:	AP009048
Genebank Protein ID:	85674318
Ecogene ID:	EG20274
Ecocyc:	EG20274
ColiBase:	b0348
Kegg Gene:	b0348
EchoBASE ID:	EB4167
CCDB:	MHPB_ECOLI
BacMap:	16128333

General Reference:

Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
Bugg, T. D. (1993). "Overproduction, purification and properties of 2,3-dihydroxyphenylpropionate 1,2-dioxygenase from Escherichia coli." Biochim Biophys Acta 1202:258-264. Pubmed: 8399388
Ferrandez, A., Garcia, J. L., Diaz, E. (1997). "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. Pubmed: 9098055
Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
Mendel, S., Arndt, A., Bugg, T. D. (2004). "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. Pubmed: 15491145
Spence, E. L., Kawamukai, M., Sanvoisin, J., Braven, H., Bugg, T. D. (1996). "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. Pubmed: 8752345