Reviewed, UniProtKB/Swiss-Prot P19731 (DMPM_PSEUF)

Names and origin

Protein names

Recommended name:
    Phenol hydroxylase P2 protein
    EC=1.14.13.7
Alternative name(s):
    Phenol 2-monooxygenase P2 component

Gene names

Name:	dmpM
Synonyms:	pheA3

Encoded on

Plasmid pVI150

Organism

Pseudomonas sp. (strain CF600)

Taxonomic identifier

79676 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria

Protein attributes

Sequence length	90 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catabolizes phenol, and some of its methylated derivatives. P2 is required for growth on phenol, and for in vitro phenol hydroxylase activity.
Catalytic activity	Phenol + NADPH + O2 = catechol + NADP+ + H2O.
Cofactor	FAD. Fe2+.
Pathway	Aromatic compound metabolism; phenol degradation.
Subunit structure	The multicomponent enzyme phenol hydroxylase is formed by P0, P1, P2, P3, P4 and P5 polypeptides.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	FAD Flavoprotein Iron NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	3D-structure Plasmid
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	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW phenol 2-monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 90

90

Phenol hydroxylase P2 protein

PRO_0000079943

Secondary structure

1

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90

Helix Strand Turn

Details...

Beta strand

8 – 10

3

Helix

14 – 25

12

Beta strand

26 – 28

3

Beta strand

43 – 48

6

Helix

50 – 58

9

Helix

60 – 62

3

Helix

63 – 68

6

Beta strand

69 – 72

4

Beta strand

84 – 88

5

Sequences

	Sequence		Length	Mass (Da)
	P19731-1 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 32B3A5FB72664AED	FASTA	90	10,491
	10 20 30 40 50 60 MSSLVYIAFQ DNDNARYVVE AIIQDNPHAV VQHHPAMIRI EAEKRLEIRR ETVEENLGRA 70 80 90 WDVQEMLVDV ITIGGNVDED DDRFVLEWKN

References

[1]	"Complete nucleotide sequence and polypeptide analysis of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600." Nordlund I., Powlowski J., Shingler V. J. Bacteriol. 172:6826-6833(1990) [PubMed: 2254258] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Takeo M., Maeda Y., Okada H., Miyama K., Mori K., Ike M., Fujita M. Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BH.
[3]	"Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy." Qian H., Edlund U., Powlowski J., Shingler V., Sethson I. Biochemistry 36:495-504(1997) [PubMed: 9012665] [Abstract] Cited for: STRUCTURE BY NMR.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M60276 Genomic DNA. Translation: AAA25941.1.
D28864 Genomic DNA. Translation: BAA06016.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HQI	NMR	-	A	1-90	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MON-12796.

Family and domain databases

InterPro

IPR003454. mOase_MmoB_DmpM.
[Graphical view]

Gene3D

G3DSA:3.90.56.10. mOase_MmoB_DmpM. 1 hit.

Pfam

PF02406. MmoB_DmpM. 1 hit.
[Graphical view]

ProDom

PD004249. MmoB_DmpM. 1 hit.
[Graphical view] [Entries sharing at least one domain]

ProtoNet

Search...

Entry information

Entry name

DMPM_PSEUF

Accession

Primary (citable) accession number: P19731

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	June 16, 2009
This is version 57 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)