P27138 (TFDB_CUPPJ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2,4-dichlorophenol 6-monooxygenase
EC=1.14.13.20

Alternative name(s):
2,4-dichlorophenol hydroxylase
Short name=2,4-DCP hydroxylase

Gene names

Name:	tfdB
Synonyms:	tfdBI
Ordered Locus Names:	Reut_D6462

Encoded on

Plasmid pJP4 Ref.1 Ref.2
Plasmid pReut1 Ref.3

Organism

Cupriavidus pinatubonensis (strain JMP134 / LMG 1197) (Alcaligenes eutrophus) (Ralstonia eutropha) [Complete proteome] [HAMAP]

Taxonomic identifier

264198 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length	598 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Transforms 2,4-dichlorophenol (2,4-DCP) into 3,5-dichlorocatechol.
Catalytic activity	2,4-dichlorophenol + NADPH + O2 = 3,5-dichlorocatechol + NADP+ + H2O.
Cofactor	FAD.
Pathway	Xenobiotic degradation; (2,4-dichlorophenoxy)acetate degradation.
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the pheA/tfdB FAD monooxygenase family.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	FAD Flavoprotein NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome Plasmid
Gene Ontology (GO)
Biological process	2,4-dichlorophenoxyacetic acid catabolic process Non-traceable author statement Ref.1. Source: UniProtKB aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2,4-dichlorophenol 6-monooxygenase activity Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 598	598	2,4-dichlorophenol 6-monooxygenase		PRO_0000214049
Regions
	Nucleotide binding	8 – 37	30	FAD Potential
	Nucleotide binding	301 – 311	11	FAD Potential

Sequences

	Sequence		Length	Mass (Da)
	P27138 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: A1E552E5A34B832F	FASTA	598	65,380
	10 20 30 40 50 60 MALTIETDVL VVGTGPAGAS AGALLARYGV RTMLINKYNW TAPTPRAHIT NQRTMEILRD 70 80 90 100 110 120 LGLEAEARLY AAPNDLMGEN TICASLAGEE FGRIRTWGTD VRRRADYDEC SPTSMCDLPQ 130 140 150 160 170 180 NYLEPILVKS AALDGCKVRF DTEYLGHEQD ADGVSSRLRD RLNGEEFTVR SKYLIGADGA 190 200 210 220 230 240 NSRVVSDLDL PLEGTMGKSG SINLLFEADL DRYVAHRPSV LYWVIQPGSD IGGLGIGVVR 250 260 270 280 290 300 MVRPWNKWLA IWGYDVEQGP PEISESFARR IVHNLIGDDS VPLKIEGIST WTVNDMYATR 310 320 330 340 350 360 LQQGRVFCAG DAVHRHPPTN GLGSNTSIQD SFNLAWKIAM VLNGTADESL LDTYTIERAP 370 380 390 400 410 420 IAKQVVCRAN KSLEDFPPIA MALGLPQAKS ADEMKSNMAR RKEPGPEAQA QRTRLREAIA 430 440 450 460 470 480 GTNYVYNAHG VEMNQRYDSP AIVADNSPDE VFRDVELYHQ ASTRPGAPMP HVWVYASGDG 490 500 510 520 530 540 HRISTKDLCG KGNFTLFTGI GGAAWQDAAA AVSRQLGVAV TVRIIGPGQA YEDHYGDFAR 550 560 570 580 590 ISEIIDTGAI LVRPDFHVAY RATSLPADAA GDLVSAMRRI LGRQSERSSA LRVTSRAI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase and dichlorocatechol oxidative operons of plasmid pJP4." Perkins E.J., Gordon M.P., Caceres O., Lurquin P.F. J. Bacteriol. 172:2351-2359(1990) [PubMed: 2185214] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genetic organization of the catabolic plasmid pJP4 from Ralstonia eutropha JMP134 (pJP4) reveals mechanisms of adaptation to chloroaromatic pollutants and evolution of specialized chloroaromatic degradation pathways." Trefault N., De la Iglesia R., Molina A.M., Manzano M., Ledger T., Perez-Pantoja D., Sanchez M.A., Stuardo M., Gonzalez B. Environ. Microbiol. 6:655-668(2004) [PubMed: 15186344] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Complete sequence of plasmid 1 of Ralstonia eutropha JMP134." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JMP134 / LMG 1197.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M35097 Genomic DNA. Translation: AAA98266.1. AY365053 Genomic DNA. Translation: AAR31035.1. CP000093 Genomic DNA. Translation: AAZ65760.1.
PIR	E35255.
RefSeq	YP_025383.1. NC_005912.1. YP_293617.1. NC_007337.1.
3D structure databases
ProteinModelPortal	P27138.
ModBase	Search...
Protein-protein interaction databases
STRING	P27138.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2847394. 3607953.
GenomeReviews	Gene locus Reut_D6462 in contig CP000093_GR.
KEGG	reu:Reut_D6462.
PATRIC	20225302. VBIRalEut24049_0530.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG569405.
OMA	ITKYRWT.
ProtClustDB	CLSK926385.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-14385. REUT264198:REUT_D6462-MONOMER.
Family and domain databases
InterPro	IPR002938. mOase_FAD-bd. IPR003042. Rng_hydrolase-like. [Graphical view]
KO	K10676.
Pfam	PF01494. FAD_binding_3. 1 hit. [Graphical view]
PRINTS	PR00420. RNGMNOXGNASE.
ProtoNet	Search...

Entry information

Entry name

TFDB_CUPPJ

Accession

Primary (citable) accession number: P27138
Secondary accession number(s): Q46M70

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	January 25, 2012
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program