Reviewed, UniProtKB/Swiss-Prot Q7WTJ2 (DMPP_ACICA)

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:

mphP

Organism

Acinetobacter calcoaceticus

Taxonomic identifier

471 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

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 By similarity. Probable electron transfer from NADPH, via FAD and the 2Fe-2S center, to the oxygenase activity site of the enzyme By similarity.
Catalytic activity	Phenol + NADPH + O(2) = catechol + NADP(+) + H(2)O.
Cofactor	Binds 1 FAD By similarity. Binds 1 2Fe-2S cluster By similarity.
Pathway	Aromatic compound metabolism; phenol degradation.
Subunit structure	The multicomponent enzyme phenol hydroxylase is formed by P0, P1, P2, P3, P4 and P5 polypeptides By similarity.
Induction	By phenol.
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
Gene Ontology (GO)
Biological process	aerobic phenol catabolic process Inferred from sequence or structural similarity. Source: UniProtKB electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	intracellular Non-traceable author statement. 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 Inferred from sequence or structural similarity. 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
	Chain	2 – 353	352	Phenol hydroxylase P5 protein		PRO_0000189406
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)
	Q7WTJ2-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: CFA97CFD40458549	FASTA	353	39,038
	10 20 30 40 50 60 MSYQVTIEPI GTTIEVEEDQ TILDAALRQG VWLPFACGHG TCGTCKVQVT DGFYDVGEAS 70 80 90 100 110 120 PFALMDIERD ENKVLACCCK PQSDMVIEAD VDEDPDFLGH LVQDYQATVI EIKDLSPTIK 130 140 150 160 170 180 GIRLQLDRPI EFQAGQYINV QFPNIEGTRA FSIANSPSEV GIVELHIRKV EGGAATTYVH 190 200 210 220 230 240 EQLATGDQLD ISGPYGQFFV RKSDDQNAIF IAGGSGLSSP QSMILDLLES GDSRTIYLFQ 250 260 270 280 290 300 GARDLAELYN RELFEQLVKD YPNFRYIPAL NAPKPEDQWT GFTGFVHEAV ADYFENRCGG 310 320 330 340 350 HKAYLCGPPI MIDSAISTLM QSRLFERDIH TERFLSAADG AAGQSRSALF KHI

References

[1]	"Genetic organization of genes encoding phenol hydroxylase, benzoate 1,2-dioxygenase alpha subunit and its regulatory proteins in Acinetobacter calcoaceticus PHEA-2." Xu Y., Chen M., Zhang W., Lin M. Curr. Microbiol. 46:235-240(2003) [PubMed: 12732969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: PHEA-2.
[2]	"Growth on phenol at chemostress levels amplifies the expression of the phenol degradation pathway in Acinetobacter calcoaceticus." Benndorf D., Loffhagen N., Hartig C., Babel W. Eng. Life Sci. 4:38-42(2004) Cited for: PROTEIN SEQUENCE OF 2-26, INDUCTION. Strain: 69-V.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ564846 Genomic DNA. Translation: CAD92316.1.
3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR012675. b-grasp_ferredoxin-like. IPR001041. Ferredoxin. IPR008333. OxRdtase_FAD-bd. IPR001433. OxRdtase_FAD/NAD_bd. IPR001221. Phe_hydroxylase. [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_ACICA

Accession

Primary (citable) accession number: Q7WTJ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 33 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)