Reviewed, UniProtKB/Swiss-Prot Q8GR45 (BPHC_BACPJ)

Names and origin

Protein names

Recommended name:
    Manganese-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase
    EC=1.13.11.39
Alternative name(s):
    Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase
    Mn(II)-dependent 23OHBP oxygenase

Gene names

Name:

bphC

Organism

Bacillus sp. (strain JF8)

Taxonomic identifier

209076 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	315 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the meta-cleavage of the hydroxylated biphenyl ring. The enzyme can oxidize a wide range of substrates, and the substrate preference order is 2,3-dihydroxybiphenyl > 3-methylcatechol > catechol > 4-methylcatechol > 4-chlorocatechol.
Catalytic activity	Biphenyl-2,3-diol + O2 = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O.
Cofactor	Binds 1 manganese ion per subunit. Ref.1
Pathway	Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-pentadienoic acid and benzoic acid from biphenyl: step 3/4.
Subunit structure	Homotetramer. Ref.1
Sequence similarities	Belongs to the extradiol ring-cleavage dioxygenase family.
biophysicochemical properties	Kinetic parameters: KM=0.095 µM for 2,3-dihydroxybiphenyl (at 60 degrees Celsius and pH 7.5) KM=1.0 µM for 3-methylcatechol (at 60 degrees Celsius and pH 7.5) KM=25.0 µM for 4-chlorocatechol (at 60 degrees Celsius and pH 7.5) KM=103.0 µM for catechol (at 60 degrees Celsius and pH 7.5) KM=111.0 µM for 4-methylcatechol (at 60 degrees Celsius and pH 7.5) Vmax=5.7 µmol/min/mg enzyme with 2,3-dihydroxybiphenyl as substrate (at 60 degrees Celsius and pH 7.5) Vmax=3.4 µmol/min/mg enzyme with 3-methylcatechol as substrate (at 60 degrees Celsius and pH 7.5) Vmax=1.8 µmol/min/mg enzyme with catechol as substrate (at 60 degrees Celsius and pH 7.5) Vmax=1.3 µmol/min/mg enzyme with 4-methylcatechol as substrate (at 60 degrees Celsius and pH 7.5) Vmax=0.68 µmol/min/mg enzyme with 4-chlorocatechol as substrate (at 60 degrees Celsius and pH 7.5) pH dependence: Optimum pH is 7.5. Temperature dependence: Optimum temperature is 85 degrees Celsius.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	Manganese Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	biphenyl-2,3-diol 1,2-dioxygenase activity Inferred from electronic annotation. Source: EC manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 315	315	Manganese-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase		PRO_0000085040
Sites
	Metal binding	153	1	Manganese By similarity
	Metal binding	216	1	Manganese By similarity
	Metal binding	269	1	Manganese By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8GR45-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 306CD094914E1AF4	FASTA	315	36,323
	10 20 30 40 50 60 MTAEIAKFGH IALITPNLEK SVWFFRDIVG LEEVDRQGDT IFLRAWGDWE HHTLSLTPGN 70 80 90 100 110 120 RARVDHIAWR TKRPEDVETF AEQLKAKGTE VQWIEPGEEK GQGKAIRFRL PNGYPFEIYY 130 140 150 160 170 180 DVEKPKAPEG KKSRLKNNVY RPSYGIAPRR IDHVNVWTTN PSEIHQWLKD NMGFKMREYI 190 200 210 220 230 240 RLNNGFVAGG WMSVTPLVHD IGVMVDPKGQ PNRLHHFAYY LDNVTDILRA ADILREHDIT 250 260 270 280 290 300 IEMGGPGRHG ISQAFFLYVK DPGSGHRLEL FSGGYLIFDP DWEPIEWQEH ELQEGLIWYG 310 PEMKPGGPMD DTTEC

References

[1]

"Characterization of a novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase from a polychlorinated biphenyl- and naphthalene-degrading Bacillus sp. JF8." Hatta T., Mukerjee-Dhar G., Damborsky J., Kiyohara H., Kimbara K. J. Biol. Chem. 278:21483-21492(2003) [PubMed: 12672826] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-41, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COFACTOR, CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB092521 Genomic DNA. Translation: BAC23089.1.
3D structure databases
HSSP	HSSP built from PDB template 1F1U based on UniProtKB Q44048.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.13.11.39. 1000.
Family and domain databases
InterPro	IPR004360. Glyas_bleo-R_dOase. [Graphical view]
Pfam	PF00903. Glyoxalase. 2 hits. [Graphical view]
ProDom	PD002334. Gly_diox. 2 hits. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

BPHC_BACPJ

Accession

Primary (citable) accession number: Q8GR45

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	March 1, 2003
Last modified:	January 20, 2009
This is version 26 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)