Reviewed, UniProtKB/Swiss-Prot P17295 (MHPB_RALEU)

Names and origin

Protein names

Recommended name:
    2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase
    EC=1.13.11.16

Gene names

Name:	mhpB
Synonyms:	mcpI

Organism

Ralstonia eutropha (Alcaligenes eutrophus)

Taxonomic identifier

106590 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length	313 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (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. Also catalyzes the cleavage of catechol. Ref.2
Catalytic activity	3-(2,3-dihydroxyphenyl)propanoate + O2 = 2-hydroxy-6-oxonona-2,4-diene-1,9-dioate. HAMAP MF_01653 2,3-dihydroxicinnamic acid + O2 = 2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate. HAMAP MF_01653
Cofactor	Fe2+ ion. Ref.2
Pathway	Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP MF_01653
Subunit structure	Homotetramer By similarity. HAMAP MF_01653
Sequence similarities	Belongs to the ligB/mhpB extradiol dioxygenase family.
Biophysicochemical properties	Kinetic parameters: KM=7.1 µM for 2,3-dihydroxyphenylpropionic acid (at 20 degrees Celsius and pH 8) HAMAP MF_01653 KM=14 µM for 2,3-dihydroxycinnamic acid (at 20 degrees Celsius and pH 8) KM=59 µM for 3-ethylcatechol (at 20 degrees Celsius and pH 8) KM=130 µM for 3-methylcatechol (at 20 degrees Celsius and pH 8)

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	Iron
Molecular function	Dioxygenase Oxidoreductase
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2,3-dihydroxy-phenylpropionate 1,2-dioxygenase activity Inferred from electronic annotation. Source: HAMAP 3-carboxyethylcatechol 2,3-dioxygenase activity Inferred from electronic annotation. Source: EC ferrous iron binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 313	313	2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase HAMAP MF_01653		PRO_0000085102
Sites
	Active site	115	1	Proton donor By similarity
	Active site	179	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	P17295-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: E1506B3785E9D0F9	FASTA	313	33,143
	10 20 30 40 50 60 MPIQLECLSH TPLHGYVDPA PEVVAEVERV QAAARDRVRA FDPELVVVFA PDHFNGFFYD 70 80 90 100 110 120 VMPPFCIGAA ATAIGDFKSL AGKLPVPADL ALSLAESVMA ADIDVALSHR MQVDHGCADA 130 140 150 160 170 180 LAALTGSLHR YPVIPVFINS VAPPMATLRR ARLLGDAVGR FLSRAGKRVL VVGSGGISHE 190 200 210 220 230 240 PPVPELAGAS EEVAERLIAG RNPSPESAAR QARTVAAAKS FVAGDSHLHP LNPEWDRAFL 250 260 270 280 290 300 SLLASGELTA VDGMTNDAIT RDGGKSAHEI RTWVAAFGAL AAYGPYRASL DFYRAIPEWI 310 AGFATMHAEP AAV

References

[1]

"Nucleotide sequence of metapyrocatechase I (catechol 2,3-oxygenase I) gene mpcI from Alcaligenes eutrophus JMP222." Kabisch M., Fortnagel P. Nucleic Acids Res. 18:3405-3405(1990) [PubMed: 2356133] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: JMP222.

[2]

"Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes eutrophus (MpcI): sequence analysis and biochemical properties of a third family of extradiol dioxygenases." Spence E.L., Kawamukai M., Sanvoisin J., Braven H., Bugg T.D.H. J. Bacteriol. 178:5249-5256(1996) [PubMed: 8752345] [Abstract] Cited for: FUNCTION IN CATABOLISM OF 3-HYDROXY DERIVATIVES OF PHENYLPROPIONIC ACID, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X52414 Genomic DNA. Translation: CAA36665.1.
PIR	S10154.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.13.11.2. 1263.
Family and domain databases
HAMAP	MF_01653. MhpB. [Tree]
InterPro	IPR004183. Xdiol_dOase_3B. [Graphical view]
Pfam	PF02900. LigB. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MHPB_RALEU

Accession

Primary (citable) accession number: P17295

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	January 19, 2010
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)