KEGG   PATHWAY: reu00361
Entry
reu00361                    Pathway                                
Name
Chlorocyclohexane and chlorobenzene degradation - Cupriavidus pinatubonensis JMP134
Class
Metabolism; Xenobiotics biodegradation and metabolism
Pathway map
reu00361  Chlorocyclohexane and chlorobenzene degradation
reu00361

Module
reu_M00548  Benzene degradation, benzene => catechol [PATH:reu00361]
Other DBs
UMBBD: hch ghch dcz 2,4-d pcp 2,4,5-t tcb
Organism
Cupriavidus pinatubonensis JMP134 [GN:reu]
Gene
Reut_A1699  phenol 2-monooxygenase P0 subunit [KO:K16249]
Reut_B5680  phenol 2-monooxygenase P0 subunit [KO:K16249]
Reut_B5681  phenol 2-monooxygenase P1 subunit [KO:K16243] [EC:1.14.13.244 1.14.13.243]
Reut_A1700  phenol 2-monooxygenase P1 subunit [KO:K16243] [EC:1.14.13.244 1.14.13.243]
Reut_A1701  phenol 2-monooxygenase P2 subunit [KO:K16244] [EC:1.14.13.244 1.14.13.243]
Reut_B5682  phenol 2-monooxygenase P2 subunit [KO:K16244] [EC:1.14.13.244 1.14.13.243]
Reut_B5683  phenol 2-monooxygenase P3 subunit [KO:K16242] [EC:1.14.13.244 1.14.13.243]
Reut_A1702  phenol 2-monooxygenase P3 subunit [KO:K16242] [EC:1.14.13.244 1.14.13.243]
Reut_A1703  phenol 2-monooxygenase P4 subunit [KO:K16245] [EC:1.14.13.244 1.14.13.243]
Reut_B5684  phenol 2-monooxygenase P4 subunit [KO:K16245] [EC:1.14.13.244 1.14.13.243]
Reut_A1704  phenol 2-monooxygenase P5 subunit [KO:K16246] [EC:1.14.13.244 1.14.13.243]
Reut_B5685  phenol 2-monooxygenase P5 subunit [KO:K16246] [EC:1.14.13.244 1.14.13.243]
Reut_B4402  Catechol dioxygenase, N-terminal [KO:K03381] [EC:1.13.11.1]
Reut_A1705  Catechol dioxygenase, N-terminal [KO:K03381] [EC:1.13.11.1]
Reut_D6465  muconate cycloisomerase [KO:K01860] [EC:5.5.1.7]
Reut_D6474  muconate cycloisomerase [KO:K01860] [EC:5.5.1.7]
Reut_A0875  Twin-arginine translocation pathway signal [KO:K01061] [EC:3.1.1.45]
Reut_A3180  Carboxymethylenebutenolidase [KO:K01061] [EC:3.1.1.45]
Reut_B5771  Carboxymethylenebutenolidase [KO:K01061] [EC:3.1.1.45]
Reut_C6316  Carboxymethylenebutenolidase [KO:K01061] [EC:3.1.1.45]
Reut_C6385  Carboxymethylenebutenolidase [KO:K01061] [EC:3.1.1.45]
Reut_D6464  Carboxymethylenebutenolidase [KO:K01061] [EC:3.1.1.45]
Reut_D6472  Carboxymethylenebutenolidase [KO:K01061] [EC:3.1.1.45]
Reut_B5577  Carboxymethylenebutenolidase [KO:K01061] [EC:3.1.1.45]
Reut_A1585  4-hydroxyphenylacetate 3-hydroxylase [KO:K24293] [EC:1.14.14.172 1.14.14.173]
Reut_A1584  Flavin reductase-like, FMN-binding protein [KO:K15245] [EC:1.5.1.37]
Reut_B3579  Ferredoxin:Oxidoreductase FAD/NAD(P)-binding:Oxidoreductase FAD-binding region [KO:K21607] [EC:1.1.1.404]
Reut_B4797  Ferredoxin:Oxidoreductase FAD/NAD(P)-binding:Oxidoreductase FAD-binding region [KO:K21607] [EC:1.1.1.404]
Reut_B5777  Phthalate 4,5-dioxygenase [KO:K21607] [EC:1.1.1.404]
Reut_D6463  Iron-containing alcohol dehydrogenase [KO:K00217] [EC:1.3.1.32]
Reut_D6471  Iron-containing alcohol dehydrogenase [KO:K00217] [EC:1.3.1.32]
Reut_B4694  maleylacetate reductase [KO:K00217] [EC:1.3.1.32]
Reut_B4129  maleylacetate reductase [KO:K00217] [EC:1.3.1.32]
Reut_A1589  maleylacetate reductase [KO:K00217] [EC:1.3.1.32]
Reut_B4137  hydroxyquinol 1,2-dioxygenase [KO:K04098] [EC:1.13.11.37]
Reut_A1587  catechol 1,2-dioxygenase [KO:K04098] [EC:1.13.11.37]
Reut_D6479  Taurine catabolism dioxygenase TauD/TfdA [KO:K06912] [EC:1.14.11.-]
Reut_D6470  Monooxygenase, FAD-binding [KO:K10676] [EC:1.14.13.20]
Reut_D6462  Monooxygenase, FAD-binding [KO:K10676] [EC:1.14.13.20]
Reut_B4679  Monooxygenase, FAD-binding protein [KO:K10676] [EC:1.14.13.20]
Reut_B4400  muconate cycloisomerase [KO:K01856] [EC:5.5.1.1]
Reut_A1689  muconate cycloisomerase [KO:K01856] [EC:5.5.1.1]
Reut_B5687  catechol 2,3-dioxygenase [KO:K00446] [EC:1.13.11.2]
Reut_B5807  Glyoxalase/bleomycin resistance protein/dioxygenase [KO:K00446] [EC:1.13.11.2]
Reut_D6473  Catechol dioxygenase, N-terminal [KO:K15253] [EC:1.13.11.-]
Reut_D6466  chlorocatechol 1,2-dioxygenase [KO:K15253] [EC:1.13.11.-]
Reut_B5659  Haloacid dehalogenase, type II:HAD-superfamily hydrolase, subfamily IA, variant 2 [KO:K01560] [EC:3.8.1.2]
Reut_B5662  Haloacid dehalogenase, type II:HAD-superfamily hydrolase, subfamily IA, variant 2 [KO:K01560] [EC:3.8.1.2]
Reut_A1952  Haloacid dehalogenase, type II:HAD-superfamily hydrolase, subfamily IA, variant 2 [KO:K01560] [EC:3.8.1.2]
Reut_A0165  Alpha/beta hydrolase fold protein [KO:K01561] [EC:3.8.1.3]
Compound
C00011  CO2
C00042  Succinate
C00090  Catechol
C00146  Phenol
C00160  Glycolate
C00530  Hydroquinone
C00682  2-Hydroxymuconate semialdehyde
C01407  Benzene
C02124  4-Chlorophenol
C02222  2-Maleylacetate
C02375  4-Chlorocatechol
C02575  Pentachlorophenol
C02625  2,4-Dichlorophenol
C02814  Benzene-1,2,4-triol
C02933  3,5-Dichlorocatechol
C03434  Tetrachlorohydroquinone
C03572  2-Chloro-cis,cis-muconate
C03585  3-Chloro-cis,cis-muconate
C03664  2,4-Dichlorophenoxyacetate
C03918  2,4-Dichloro-cis,cis-muconate
C04091  cis-1,2-Dihydrobenzene-1,2-diol
C04431  cis-4-Carboxymethylenebut-2-en-4-olide
C04522  2-Chloro-2,5-dihydro-5-oxofuran-2-acetate
C04706  cis-2-Chloro-4-carboxymethylenebut-2-en-1,4-olide
C04729  trans-2-Chloro-4-carboxymethylenebut-2-en-1,4-olide
C05618  3-Chlorocatechol
C06328  6-Chlorobenzene-1,2,4-triol
C06329  2-Chloromaleylacetate
C06594  1,2,4-Trichlorobenzene
C06596  gamma-Pentachlorocyclohexene
C06597  1,3,4,6-Tetrachloro-1,4-cyclohexadiene
C06598  2,4,5-Trichloro-2,5-cyclohexadiene-1-ol
C06599  2,5-Dichloro-2,5-cyclohexadiene-1,4-diol
C06600  2,5-Dichlorohydroquinone
C06601  Chlorohydroquinone
C06602  2,5-Dichlorophenol
C06603  cis,cis-4-Hydroxymuconic semialdehyde
C06755  Chloroacetic acid
C06988  beta-1,2,3,4,5,6-Hexachlorocyclohexane
C06989  delta-3,4,5,6-Tetrachlorocyclohexene
C06990  Chlorobenzene
C07075  Lindane
C07088  4-Chlorophenoxyacetate
C07089  5-Chloro-2-hydroxymuconic semialdehyde
C07090  Protoanemonin
C07091  cis-Acetylacrylate
C07092  1,4-Dichlorobenzene
C07093  3,6-Dichloro-cis-1,2-dihydroxycyclohexa-3,5-diene
C07094  3,6-Dichlorocatechol
C07095  2,5-Dichloro-cis,cis-muconate
C07096  2,6-Dichlorophenol
C07097  2,6-Dichlorohydroquinone
C07098  2,4,6-Trichlorophenol
C07099  2,3,6-Trichlorohydroquinone
C07100  2,4,5-Trichlorophenoxyacetic acid
C07101  2,4,5-Trichlorophenol
C07102  5-Chloro-1,2,4-trihydroxybenzene
C07103  2-Hydroxy-1,4-benzoquinone
C11352  5,6-Dichloro-1,3-cyclohexadiene
C12831  3,4,6-Trichlorocatechol
C12832  3,4,6-Trichloro-cis-1,2-dihydroxycyclohexa-3,5-diene
C12833  2,3,5-Trichloro-cis,cis-muconate
C12834  2,5-Dichloro-carboxymethylenebut-2-en-4-olide
C12835  2,5-Dichloro-4-oxohex-2-enedioate
C12836  2-Chloro-3-oxoadipate
C12837  3-Chloro-cis-1,2-dihydroxycyclohexa-3,5-diene
C12838  trans-4-Carboxymethylenebut-2-en-4-olide
C14419  2,4-Dichloroaniline
C14450  4-Chloroaniline
C16181  beta-2,3,4,5,6-Pentachlorocyclohexanol
C16182  beta-2,3,5,6-Tetrachloro-1,4-cyclohexanediol
C16266  3-Chloro-2-hydroxymuconic semialdehyde
C18236  1,2,3,4-Tetrachlorobenzene
C18238  cis-Chlorobenzene dihydrodiol
C18240  Tetrachlorocatechol
C18241  Tetrachloro-cis,cis-muconate
C18242  2,3,5-Trichlorodienelactone
C18243  2,3,5-Trichloromaleylacetate
C18244  2,4-Dichloro-3-oxoadipate
C18933  Chloranil
C21103  2,6-Dichloro-p-benzoquinone
C21104  2,5-Dichloro-p-benzoquinone
C21105  5-Chloro-2-hydroxy-p-benzoquinone
Reference
  Authors
Xun L, Bohuslavek J, Cai M.
  Title
Characterization of 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA) of Sphingomonas chlorophenolica ATCC 39723.
  Journal
Biochem Biophys Res Commun 266:322-5 (1999)
DOI:10.1006/bbrc.1999.1805
Reference
PMID:1987135
  Authors
van der Meer JR, van Neerven AR, de Vries EJ, de Vos WM, Zehnder AJ.
  Title
Cloning and characterization of plasmid-encoded genes for the degradation of 1,2-dichloro-, 1,4-dichloro-, and 1,2,4-trichlorobenzene of Pseudomonas sp. strain P51.
  Journal
J Bacteriol 173:6-15 (1991)
DOI:10.1128/jb.173.1.6-15.1991
Reference
  Authors
Nagata Y, Futamura A, Miyauchi K, Takagi M.
  Title
Two different types of dehalogenases, LinA and LinB, involved in gamma-hexachlorocyclohexane degradation in Sphingomonas paucimobilis UT26 are localized in the periplasmic space without molecular processing.
  Journal
J Bacteriol 181:5409-13 (1999)
DOI:10.1128/JB.181.17.5409-5413.1999
Reference
  Authors
Nagata Y, Miyauchi K, Takagi M.
  Title
Complete analysis of genes and enzymes for gamma-hexachlorocyclohexane degradation in Sphingomonas paucimobilis UT26.
  Journal
J Ind Microbiol Biotechnol 23:380-390 (1999)
DOI:10.1038/sj/jim/2900736
Reference
  Authors
Dogra C, Raina V, Pal R, Suar M, Lal S, Gartemann KH, Holliger C, van der Meer JR, Lal R.
  Title
Organization of lin genes and IS6100 among different strains of hexachlorocyclohexane-degrading Sphingomonas paucimobilis: evidence for horizontal gene transfer.
  Journal
J Bacteriol 186:2225-35 (2004)
DOI:10.1128/JB.186.8.2225-2235.2004
Reference
  Authors
Nagata Y, Prokop Z, Marvanova S, Sykorova J, Monincova M, Tsuda M, Damborsky J.
  Title
Reconstruction of mycobacterial dehalogenase Rv2579 by cumulative mutagenesis of haloalkane dehalogenase LinB.
  Journal
Appl Environ Microbiol 69:2349-55 (2003)
DOI:10.1128/AEM.69.4.2349-2355.2003
Reference
  Authors
Vedler E, Vahter M, Heinaru A.
  Title
The completely sequenced plasmid pEST4011 contains a novel IncP1 backbone and a catabolic transposon harboring tfd genes for 2,4-dichlorophenoxyacetic acid degradation.
  Journal
J Bacteriol 186:7161-74 (2004)
DOI:10.1128/JB.186.21.7161-7174.2004
Reference
PMID:9148781
  Authors
Sommer C, Gorisch H.
  Title
Enzymology of the degradation of (di)chlorobenzenes by Xanthobacter flavus 14p1.
  Journal
Arch Microbiol 167:384-91 (1997)
DOI:10.1007/s002030050459
Reference
  Authors
Laemmli CM, Schonenberger R, Suter M, Zehnder AJ, van der Meer JR.
  Title
TfdD(II), one of the two chloromuconate cycloisomerases of Ralstonia eutropha JMP134 (pJP4), cannot efficiently convert 2-chloro- cis, cis-muconate to trans-dienelactone to allow growth on 3-chlorobenzoate.
  Journal
Arch Microbiol 178:13-25 (2002)
DOI:10.1007/s00203-002-0417-3
Reference
  Authors
Wu J, Hong Q, Han P, He J, Li S.
  Title
A gene linB2 responsible for the conversion of beta-HCH and 2,3,4,5,6-pentachlorocyclohexanol in Sphingomonas sp. BHC-A.
  Journal
Appl Microbiol Biotechnol 73:1097-105 (2007)
DOI:10.1007/s00253-006-0579-z
Reference
PMID:9758802
  Authors
Potrawfke T, Timmis KN, Wittich RM
  Title
Degradation of 1,2,3,4-tetrachlorobenzene by pseudomonas chlororaphis RW71
  Journal
Appl Environ Microbiol 64:3798-806 (1998)
DOI:10.1128/AEM.64.10.3798-3806.1998
Reference
  Authors
Potrawfke T, Armengaud J, Wittich RM
  Title
Chlorocatechols substituted at positions 4 and 5 are substrates of the broad-spectrum chlorocatechol 1,2-dioxygenase of Pseudomonas chlororaphis RW71.
  Journal
J Bacteriol 183:997-1011 (2001)
DOI:10.1128/JB.183.3.997-1011.2001
Related
pathway
reu00020  Citrate cycle (TCA cycle)
reu00362  Benzoate degradation
reu00630  Glyoxylate and dicarboxylate metabolism
KO pathway
ko00361   
LinkDB

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