Reviewed, UniProtKB/Swiss-Prot P19734 (DMPP_PSEUF)

Names and origin

Protein names

Recommended name:
    Phenol hydroxylase P5 protein
    EC=1.14.13.7
Alternative name(s):
    Phenol 2-monooxygenase P5 component

Gene names

Name:

dmpP

Encoded on

Plasmid pVI150

Organism

Pseudomonas sp. (strain CF600)

Taxonomic identifier

79676 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria

Protein attributes

Sequence length	353 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catabolizes phenol, and some of its methylated derivatives. P5 is required for growth on phenol, and for in vitro phenol hydroxylase activity. Ref.2 Probable electron transfer from NADPH, via FAD and the 2Fe-2S center, to the oxygenase activity site of the enzyme. Ref.2
Catalytic activity	Phenol + NADPH + O2 = catechol + NADP+ + H2O.
Cofactor	Binds 1 FAD per subunit. Binds 1 2Fe-2S cluster per subunit.
Pathway	Aromatic compound metabolism; phenol degradation.
Subunit structure	The multicomponent enzyme phenol hydroxylase is formed by P0, P1, P2, P3, P4 and P5 polypeptides.
Sequence similarities	Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 FAD-binding FR-type domain.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism Electron transport Transport
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological process	aerobic phenol catabolic process Ref.2 Inferred from direct assay. Source: UniProtKB electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extrachromosomal circular DNA Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW phenol 2-monooxygenase activity Ref.2 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 353	352	Phenol hydroxylase P5 protein		PRO_0000189407
Regions
	Domain	3 – 93	91	2Fe-2S ferredoxin-type
	Domain	102 – 201	100	FAD-binding FR-type
Sites
	Metal binding	37	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	42	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	45	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	77	1	Iron-sulfur (2Fe-2S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P19734-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 007E85A5DF189CD0	FASTA	353	38,478
	10 20 30 40 50 60 MSYNVTIEPT GEVIEVEDGQ TILQAALRQG VWLPFACGHG TCATCKVQVV EGEVDIGEAS 70 80 90 100 110 120 PFALMDIERD ERKVLACCAI PLSDLVIEAD VDADPDFLGH PVEDYRGVVS ALVDLSPTIK 130 140 150 160 170 180 GLHIKLDRPM PFQAGQYVNL ALPGIDGTRA FSLANPPSRN DEVELHVRLV EGGAATGFIH 190 200 210 220 230 240 KQLKVGDAVE LSGPYGQFFV RDSQAGDLIF IAGGSGLSSP QSMILDLLER GDTRRITLFQ 250 260 270 280 290 300 GARNRAELYN CELFEELAAR HPNFSYVPAL NQANDDPEWQ GFKGFVHDAA KAHFDGRFGG 310 320 330 340 350 QKAYLCGPPP MIDAAITTLM QGRLFERDIF MERFYTAADG AGESSRSALF KRI

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]	"In vitro analysis of polypeptide requirements of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600." Powlowski J., Shingler V. J. Bacteriol. 172:6834-6840(1990) [PubMed: 2254259] [Abstract] Cited for: PROBABLE FUNCTION, PROTEIN SEQUENCE OF 2-5.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M60276 Genomic DNA. Translation: AAA25944.1.
3D structure databases
SMR	P19734. Positions 2-336.
ModBase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-12799.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR012675. b-grasp_ferredoxin-like. IPR017927. Fd_Rdtase_FAD-bd. IPR001041. Ferredoxin. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD_bd. IPR001221. Phe_hydroxylase. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
Gene3D	G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
Pfam	PF00970. FAD_binding_6. 1 hit. PF00111. Fer2. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00410. PHEHYDRXLASE.
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51384. FAD_FR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DMPP_PSEUF

Accession

Primary (citable) accession number: P19734

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 66 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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