Q9S157 (MHPB_COMTE) Reviewed, UniProtKB/Swiss-Prot

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

Organism

Comamonas testosteroni (Pseudomonas testosteroni)

Taxonomic identifier

285 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Comamonas

Protein attributes

Sequence length	321 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. Ref.1
Catalytic activity	3-(2,3-dihydroxyphenyl)propanoate + O2 = 2-hydroxy-6-oxonona-2,4-diene-1,9-dioate. HAMAP MF_01653 (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + O2 = 2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate. HAMAP MF_01653
Cofactor	Fe2+ ion By similarity. HAMAP MF_01653
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: Vmax=0.73 µmol/min/mg enzyme with 3-(2,3-dihydroxyphenyl)propanoate (at pH 7.5) Ref.1 Vmax=0.45 µmol/min/mg enzyme withd 2,3-dihydroxybiphenyl (at pH 7.5) Vmax=0.22 µmol/min/mg enzyme withd 3-methylcatechol (at pH 7.5) Vmax=0.10 µmol/min/mg enzyme withd catechol (at pH 7.5)

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: UniProtKB-KW
Molecular function	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 – 321	321	2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase HAMAP MF_01653		PRO_0000337647
Sites
	Active site	123	1	Proton donor By similarity
	Active site	189	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9S157 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 6FC238E939E5CF64	FASTA	321	34,366
	10 20 30 40 50 60 MSGSAIATAR RAFLGMSHSP LLGLNPVAAD DQIAIDKAIA AARAAVHEFA PELIVLLGPD 70 80 90 100 110 120 HYNGFFNELM PPFCIGSQAT AVGDYLSPAG PLNVAGELAI ALADHLMDRH FDIAVSRRML 130 140 150 160 170 180 VDHGFSQALQ FLWGDEMDTP PVIPIFMNAV AQPGIARMAR CKALGEGVGS FLDQLPLRTL 190 200 210 220 230 240 LIGSGGLSHE PPVPTLAHPD PAVRERITVR STPTEQEREL KTERVKAAGL ALAHGDSWMK 250 260 270 280 290 300 PLNPEWDLQW MDAMASGQLD GLCAMNEASI GAMAGNSAHE SKTWLVARSA LPANTRLSCP 310 320 VRAYRAIPSL IAGYGVMFMH H

References

[1]

"Genetic organization and characteristics of the 3-(3-hydroxyphenyl)propionic acid degradation pathway of Comamonas testosteroni TA441." Arai H., Yamamoto T., Ohishi T., Shimizu T., Nakata T., Kudo T. Microbiology 145:2813-2820(1999) [PubMed: 10537203] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN CATABOLISM OF 3-HYDROXY DERIVATIVES OF PHENYLPROPIONIC ACID, BIOPHYSICOCHEMICAL PROPERTIES. Strain: TA441.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB024335 Genomic DNA. Translation: BAA82879.1.
3D structure databases
ProteinModelPortal	Q9S157.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
HAMAP	MF_01653. MhpB. [Tree]
InterPro	IPR023789. DHPP/DHXA_dioxygenase. IPR004183. Xdiol_dOase_suB. [Graphical view]
Gene3D	G3DSA:3.40.830.10. Xdiol_dOase_3B. 2 hits.
Pfam	PF02900. LigB. 1 hit. [Graphical view]
SUPFAM	SSF53213. Xdiol_dOase_3B. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MHPB_COMTE

Accession

Primary (citable) accession number: Q9S157

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program