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Conserved domains on  [gi|499315417|ref|WP_011005909|]
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MULTISPECIES: catechol 2,3-dioxygenase [Bacteria]

Protein Classification

catechol 2,3-dioxygenase( domain architecture ID 11496493)

catechol 2,3-dioxygenase initiates the meta-cleavage pathway of catechol degradation, catalyzing the oxidation of catechol to 2-hydroxymuconate-6-semialdehyde

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
catechol_2_3 TIGR03211
catechol 2,3 dioxygenase; Members of this family all are enzymes active as catechol 2,3 ...
 4-307 3.44e-175

catechol 2,3 dioxygenase; Members of this family all are enzymes active as catechol 2,3 dioxygenase (1.13.11.2), although some members have highly significant activity on catechol derivatives such as 3-methylcatechol, 3-chlorocatechol, and 4-chlorocatechol (see Mars, et al.). This enzyme is also called metapyrocatechase, as it performs a meta-cleavage (an extradiol ring cleavage), in contrast to the ortho-cleavage (intradiol ring cleavage)performed by catechol 1,2-dioxygenase (EC 1.13.11.1), also called pyrocatechase. [Energy metabolism, Other]


:

Pssm-ID: 274480 [Multi-domain]  Cd Length: 303  Bit Score: 486.37  E-value: 3.44e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417    4 GVMRPGHVQLRVLDMSKALEHYVELLGLIEMDRDDQgRVYLKAWTEVDKFSLVLREADEPGMDFMGFKVVDEDALRQLER 83
Cdd:TIGR03211   1 GVMRLGHVELRVLDLEESLKHYTDVLGLEETGRDGQ-RVYLKAWDEWDHYSVILTEADTAGLDHMAFKVESEADLERLVK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417   84 DLMAYGCAVEQLPAGELNSCGRRVRFQAPSGHHFELYADKEYTGkWGLNDVNPEAWPRDLKGMAAVRFDHALMYGDELPA 163
Cdd:TIGR03211  80 RLEAYGVGTGWIPAGELPGVGRRVRFTLPSGHTMELYAEKEYVG-ELVGGLNPDPWPDPLRGVGARRLDHCLLYGEDVAE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417  164 TYDLFTKVLGFYLAEQVLDE-NGTRVAQFLSLSTKAHDVAFIHHPEKGRLHHVSFHLETWEDLLRAADLISMTDTSIDIG 242
Cdd:TIGR03211 159 NTRFFTEVLGFRLTEQVVLGdGKEMAAAWLSVSNKAHDIAFVGDPEPGKLHHVSFFLDSWEDVLKAADVMSKNDVSIDIG 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499315417  243 PTRHGLTHGKTIYFFDPSGNRNEVFCGGDYNYPDHKPVTWTTDQLGKAIFYHDRILNERFMTVLT 307
Cdd:TIGR03211 239 PTRHGITRGQTIYFFDPSGNRNETFAGGYLAYPDWPPITWTEDELGRGIFYHGRVLNESFHTVGT 303
 
Name Accession Description Interval E-value
catechol_2_3 TIGR03211
catechol 2,3 dioxygenase; Members of this family all are enzymes active as catechol 2,3 ...
 4-307 3.44e-175

catechol 2,3 dioxygenase; Members of this family all are enzymes active as catechol 2,3 dioxygenase (1.13.11.2), although some members have highly significant activity on catechol derivatives such as 3-methylcatechol, 3-chlorocatechol, and 4-chlorocatechol (see Mars, et al.). This enzyme is also called metapyrocatechase, as it performs a meta-cleavage (an extradiol ring cleavage), in contrast to the ortho-cleavage (intradiol ring cleavage)performed by catechol 1,2-dioxygenase (EC 1.13.11.1), also called pyrocatechase. [Energy metabolism, Other]


Pssm-ID: 274480 [Multi-domain]  Cd Length: 303  Bit Score: 486.37  E-value: 3.44e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417    4 GVMRPGHVQLRVLDMSKALEHYVELLGLIEMDRDDQgRVYLKAWTEVDKFSLVLREADEPGMDFMGFKVVDEDALRQLER 83
Cdd:TIGR03211   1 GVMRLGHVELRVLDLEESLKHYTDVLGLEETGRDGQ-RVYLKAWDEWDHYSVILTEADTAGLDHMAFKVESEADLERLVK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417   84 DLMAYGCAVEQLPAGELNSCGRRVRFQAPSGHHFELYADKEYTGkWGLNDVNPEAWPRDLKGMAAVRFDHALMYGDELPA 163
Cdd:TIGR03211  80 RLEAYGVGTGWIPAGELPGVGRRVRFTLPSGHTMELYAEKEYVG-ELVGGLNPDPWPDPLRGVGARRLDHCLLYGEDVAE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417  164 TYDLFTKVLGFYLAEQVLDE-NGTRVAQFLSLSTKAHDVAFIHHPEKGRLHHVSFHLETWEDLLRAADLISMTDTSIDIG 242
Cdd:TIGR03211 159 NTRFFTEVLGFRLTEQVVLGdGKEMAAAWLSVSNKAHDIAFVGDPEPGKLHHVSFFLDSWEDVLKAADVMSKNDVSIDIG 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499315417  243 PTRHGLTHGKTIYFFDPSGNRNEVFCGGDYNYPDHKPVTWTTDQLGKAIFYHDRILNERFMTVLT 307
Cdd:TIGR03211 239 PTRHGITRGQTIYFFDPSGNRNETFAGGYLAYPDWPPITWTEDELGRGIFYHGRVLNESFHTVGT 303
2_3_CTD_C cd07243
C-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the C-terminal, ...
 145-287 2.33e-93

C-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the C-terminal, catalytic, domain of catechol 2,3-dioxygenase. Catechol 2,3-dioxygenase (2,3-CTD, catechol:oxygen 2,3-oxidoreductase) catalyzes an extradiol cleavage of catechol to form 2-hydroxymuconate semialdehyde with the insertion of two atoms of oxygen. The enzyme is a homotetramer and contains catalytically essential Fe(II) . The reaction proceeds by an ordered bi-unit mechanism. First, catechol binds to the enzyme, this is then followed by the binding of dioxygen to form a tertiary complex, and then the aromatic ring is cleaved to produce 2-hydroxymuconate semialdehyde. Catechol 2,3-dioxygenase belongs to the type I extradiol dioxygenase family. The subunit comprises the N- and C-terminal domains of similar structure fold, resulting from an ancient gene duplication. The active site is located in a funnel-shaped space of the C-terminal domain. This subfamily represents the C-terminal domain.


Pssm-ID: 319907  Cd Length: 144  Bit Score: 273.13  E-value: 2.33e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417 145 GMAAVRFDHALMYGDELPATYDLFTKVLGFYLAEQVLDE-NGTRVAQFLSLSTKAHDVAFIHHPEKGRLHHVSFHLETWE 223
Cdd:cd07243    1 GIAAHRLDHCLLYGERIAETTRFFTDVLGFYLTERVLDPdGGTRVGIFLSCSNKAHDIAFVGYPEDGKLHHTSFFLESWE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499315417 224 DLLRAADLISMTDTSIDIGPTRHGLTHGKTIYFFDPSGNRNEVFCGGDYNYPDHKPVTWTTDQL 287
Cdd:cd07243   81 DVLKAGDIISKNDVSIDIGPTRHGITRGQTIYFFDPSGNRNETFAGGYIAYPDMPVVTWTEDQL 144
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
5-124 2.66e-19

Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 82.31  E-value: 2.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417   5 VMRPGHVQLRVLDMSKALEHYVELLGLIEMDRDDqGRVYLKAWTevDKFSLVLREAD-------EPGMDFMGFKVVDEDA 77
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREG-GRVYLRADG--GEHLLVLEEAPgapprpgAAGLDHVAFRVPSRAD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 499315417  78 LRQLERDLMAYGCAVEqlpAGELNSCGRRVRFQAPSGHHFELYADKE 124
Cdd:COG2514   78 LDAALARLAAAGVPVE---GAVDHGVGESLYFRDPDGNLIELYTDRP 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
150-266 1.40e-16

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 74.41  E-value: 1.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417  150 RFDHALMYGDELPATYDLFTKVLGFYLAEQVLDE-----------NGTRVAQFLSLSTKAHDVAFIHHpekgrlHHVSFH 218
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGeegglrsafflAGGRVLELLLNETPPPAAAGFGG------HHIAFI 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 499315417  219 LETWEDLLRAADLISMTDTSIDIGPTRHGLTHGKTiYFFDPSGNRNEV 266
Cdd:pfam00903  75 AFSVDDVDAAYDRLKAAGVEIVREPGRHGWGGRYS-YFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
catechol_2_3 TIGR03211
catechol 2,3 dioxygenase; Members of this family all are enzymes active as catechol 2,3 ...
 4-307 3.44e-175

catechol 2,3 dioxygenase; Members of this family all are enzymes active as catechol 2,3 dioxygenase (1.13.11.2), although some members have highly significant activity on catechol derivatives such as 3-methylcatechol, 3-chlorocatechol, and 4-chlorocatechol (see Mars, et al.). This enzyme is also called metapyrocatechase, as it performs a meta-cleavage (an extradiol ring cleavage), in contrast to the ortho-cleavage (intradiol ring cleavage)performed by catechol 1,2-dioxygenase (EC 1.13.11.1), also called pyrocatechase. [Energy metabolism, Other]


Pssm-ID: 274480 [Multi-domain]  Cd Length: 303  Bit Score: 486.37  E-value: 3.44e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417    4 GVMRPGHVQLRVLDMSKALEHYVELLGLIEMDRDDQgRVYLKAWTEVDKFSLVLREADEPGMDFMGFKVVDEDALRQLER 83
Cdd:TIGR03211   1 GVMRLGHVELRVLDLEESLKHYTDVLGLEETGRDGQ-RVYLKAWDEWDHYSVILTEADTAGLDHMAFKVESEADLERLVK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417   84 DLMAYGCAVEQLPAGELNSCGRRVRFQAPSGHHFELYADKEYTGkWGLNDVNPEAWPRDLKGMAAVRFDHALMYGDELPA 163
Cdd:TIGR03211  80 RLEAYGVGTGWIPAGELPGVGRRVRFTLPSGHTMELYAEKEYVG-ELVGGLNPDPWPDPLRGVGARRLDHCLLYGEDVAE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417  164 TYDLFTKVLGFYLAEQVLDE-NGTRVAQFLSLSTKAHDVAFIHHPEKGRLHHVSFHLETWEDLLRAADLISMTDTSIDIG 242
Cdd:TIGR03211 159 NTRFFTEVLGFRLTEQVVLGdGKEMAAAWLSVSNKAHDIAFVGDPEPGKLHHVSFFLDSWEDVLKAADVMSKNDVSIDIG 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499315417  243 PTRHGLTHGKTIYFFDPSGNRNEVFCGGDYNYPDHKPVTWTTDQLGKAIFYHDRILNERFMTVLT 307
Cdd:TIGR03211 239 PTRHGITRGQTIYFFDPSGNRNETFAGGYLAYPDWPPITWTEDELGRGIFYHGRVLNESFHTVGT 303
2_3_CTD_C cd07243
C-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the C-terminal, ...
 145-287 2.33e-93

C-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the C-terminal, catalytic, domain of catechol 2,3-dioxygenase. Catechol 2,3-dioxygenase (2,3-CTD, catechol:oxygen 2,3-oxidoreductase) catalyzes an extradiol cleavage of catechol to form 2-hydroxymuconate semialdehyde with the insertion of two atoms of oxygen. The enzyme is a homotetramer and contains catalytically essential Fe(II) . The reaction proceeds by an ordered bi-unit mechanism. First, catechol binds to the enzyme, this is then followed by the binding of dioxygen to form a tertiary complex, and then the aromatic ring is cleaved to produce 2-hydroxymuconate semialdehyde. Catechol 2,3-dioxygenase belongs to the type I extradiol dioxygenase family. The subunit comprises the N- and C-terminal domains of similar structure fold, resulting from an ancient gene duplication. The active site is located in a funnel-shaped space of the C-terminal domain. This subfamily represents the C-terminal domain.


Pssm-ID: 319907  Cd Length: 144  Bit Score: 273.13  E-value: 2.33e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417 145 GMAAVRFDHALMYGDELPATYDLFTKVLGFYLAEQVLDE-NGTRVAQFLSLSTKAHDVAFIHHPEKGRLHHVSFHLETWE 223
Cdd:cd07243    1 GIAAHRLDHCLLYGERIAETTRFFTDVLGFYLTERVLDPdGGTRVGIFLSCSNKAHDIAFVGYPEDGKLHHTSFFLESWE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499315417 224 DLLRAADLISMTDTSIDIGPTRHGLTHGKTIYFFDPSGNRNEVFCGGDYNYPDHKPVTWTTDQL 287
Cdd:cd07243   81 DVLKAGDIISKNDVSIDIGPTRHGITRGQTIYFFDPSGNRNETFAGGYIAYPDMPVVTWTEDQL 144
2_3_CTD_N cd07265
N-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the N-terminal, ...
 4-125 7.48e-75

N-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the N-terminal, non-catalytic, domain of catechol 2,3-dioxygenase. Catechol 2,3-dioxygenase (2,3-CTD, catechol:oxygen 2,3-oxidoreductase) catalyzes an extradiol cleavage of catechol to form 2-hydroxymuconate semialdehyde with the insertion of two atoms of oxygen. The enzyme is a homotetramer and contains catalytically essential Fe(II) . The reaction proceeds by an ordered bi-unit mechanism. First, catechol binds to the enzyme, this is then followed by the binding of dioxygen to form a tertiary complex, and then the aromatic ring is cleaved to produce 2-hydroxymuconate semialdehyde. Catechol 2,3-dioxygenase belongs to the type I extradiol dioxygenase family. The subunit comprises the N- and C-terminal domains of similar structure fold, resulting from an ancient gene duplication. The active site is located in a funnel-shaped space of the C-terminal domain. This subfamily represents the N-terminal domain.


Pssm-ID: 319926  Cd Length: 122  Bit Score: 225.30  E-value: 7.48e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417   4 GVMRPGHVQLRVLDMSKALEHYVELLGLIEMDRDDQGRVYLKAWTEVDKFSLVLREADEPGMDFMGFKVVDEDALRQLER 83
Cdd:cd07265    1 GVLRPGHVQLRVLDLEEAIKHYREVLGLVETGRDDQGRVYLKAWDEYDHHSIILREADTAGLDFMGFKVLDDADLEQLEA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 499315417  84 DLMAYGCAVEQLPAGELNSCGRRVRFQAPSGHHFELYADKEY 125
Cdd:cd07265   81 RLQAYGVTVTRIPAGELPGVGRRVRFQLPSGHTMELYAEKEY 122
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 10-122 4.51e-44

N-terminal domain of type I, class II extradiol dioxygenases; This family contains the N-terminal non-catalytic domain of type I, class II extradiol dioxygenases. Dioxygenases catalyze the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms, resulting in the cleavage of aromatic rings. Two major groups of dioxygenases have been identified according to the cleavage site; extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon, whereas intradiol enzymes cleave the aromatic ring between two hydroxyl groups. Extradiol dioxygenases are classified into type I and type II enzymes. Type I extradiol dioxygenases include class I and class II enzymes. These two classes of enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. The extradiol dioxygenases represented in this family are type I, class II enzymes, and are composed of the N- and C-terminal domains of similar structure fold, resulting from an ancient gene duplication. The active site is located in a funnel-shaped space of the C-terminal domain. A catalytically essential metal, Fe(II) or Mn(II), presents in all the enzymes in this family.


Pssm-ID: 319967  Cd Length: 111  Bit Score: 146.31  E-value: 4.51e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417  10 HVQLRVLDMSKALEHYVELLGLIEMDRDdQGRVYLKAWtEVDKFSLVLREADEPGMDFMGFKVVDEDALRQLERDLMAYG 89
Cdd:cd16360    1 YAELGVPDLEKALEFYTDVLGLQVAKRD-GNSVYLRGY-EDEHHSLVLYEAPEAGLKHFAFEVASEEDLERAAASLTALG 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 499315417  90 CAVEQLPAGELNSCGRRVRFQAPSGHHFELYAD 122
Cdd:cd16360   79 CDVTWGPDGEVPGGGKGFRFQDPSGHLLELFVE 111
BphC-JF8_C_like cd09014
C-terminal, catalytic domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase); 2, ...
 145-291 3.24e-33

C-terminal, catalytic domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase); 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, a key step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). BphC belongs to the type I extradiol dioxygenase family, which requires a metal ion in the active site in its catalytic mechanism. Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. This subfamily of BphC is represented by the enzyme purified from the thermophilic biphenyl and naphthalene degrader, Bacillus sp. JF8. The members in this family of BphC enzymes may use either Mn(II) or Fe(II) as cofactors. The enzyme purified from Bacillus sp. JF8 is Mn(II)-dependent, however, the enzyme from Rhodococcus jostii RHAI has Fe(II) bound to it. BphC_JF8 is thermostable and its optimum activity is at 85 degrees C. The enzymes in this family have an internal duplication. This family represents the C-terminal repeat.


Pssm-ID: 319956  Cd Length: 167  Bit Score: 119.79  E-value: 3.24e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417 145 GMAAVRFDHALMYGDELPATYDLFTKVLGFYLAEQVLDENGTRVAQFLSLSTKAHDVAFIHHP--EKGRLHHVSFHLETW 222
Cdd:cd09014    1 GIPVRRIDHLNLLASDVTANRQFMSDTLGFRLREQIRDNNGGEAGAWMSVSSLVHDVAVMRDGkgEPGRLHHLAYWYGTP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499315417 223 EDLLRAADLISMTDTSIDIGPTRHGLTHGKTIYFFDPSGNRNEVFCGGDYNY--PDHKPVTWTTDQLGKAI 291
Cdd:cd09014   81 EDLLRAADIFREHGIQIEAGPGKHGISQAFFLYVYEPGGNRVELFGGAGYLIfdPDWEPVEWTEEDLDRGI 151
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 152-283 7.99e-29

C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family contains the C-terminal, catalytic domain of type I, class II extradiol dioxygenases. Dioxygenases catalyze the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms, resulting in the cleavage of aromatic rings. Two major groups of dioxygenases have been identified according to the cleavage site; extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon, whereas intradiol enzymes cleave the aromatic ring between two hydroxyl groups. Extradiol dioxygenases are classified into type I and type II enzymes. Type I extradiol dioxygenases include class I and class II enzymes. These two classes of enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. The extradiol dioxygenases represented in this family are type I, class II enzymes, and are composed of the N- and C-terminal domains of similar structure fold, resulting from an ancient gene duplication. The active site is located in a funnel-shaped space of the C-terminal domain. A catalytically essential metal, Fe(II) or Mn(II), presents in all the enzymes in this family.


Pssm-ID: 319931  Cd Length: 132  Bit Score: 107.40  E-value: 7.99e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417 152 DHALMYGDELPATYDLFTKVLGFYLAEqVLDENGTRVAQFLSLS--TKAHDVAFIHHPeKGRLHHVSFHLETWEDLLRAA 229
Cdd:cd08343    1 GHVVLCSPDVEASRDFYTDVLGFRVSD-RIVDPGVDGGAFLHCDrgTDHHTVALAGGP-HPGLHHVAFEVHDLDDVGRGH 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499315417 230 DLISMTDTSIDIGPTRHGLTHGKTIYFFDPSGNRNEVFCGGDYNYPDHKPVTWT 283
Cdd:cd08343   79 DRLREKGYKIEWGPGRHGLGSQVFDYWFDPSGNRVEYYTDGDLVDDDWPPKVHD 132
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
5-124 2.66e-19

Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 82.31  E-value: 2.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417   5 VMRPGHVQLRVLDMSKALEHYVELLGLIEMDRDDqGRVYLKAWTevDKFSLVLREAD-------EPGMDFMGFKVVDEDA 77
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREG-GRVYLRADG--GEHLLVLEEAPgapprpgAAGLDHVAFRVPSRAD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 499315417  78 LRQLERDLMAYGCAVEqlpAGELNSCGRRVRFQAPSGHHFELYADKE 124
Cdd:COG2514   78 LDAALARLAAAGVPVE---GAVDHGVGESLYFRDPDGNLIELYTDRP 121
HPCD_N_class_II cd07266
N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 5-121 2.98e-17

N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily contains the N-terminal, non-catalytic, domain of HPCD. HPCD catalyses the second step in the degradation of 4-hydroxyphenylacetate to succinate and pyruvate. The aromatic ring of 4-hydroxyphenylacetate is opened by this dioxygenase to yield the 3,4-diol product, 2-hydroxy-5-carboxymethylmuconate semialdehyde. HPCD is a homotetramer and each monomer contains two structurally homologous barrel-shaped domains at the N- and C-terminus. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism. Most extradiol dioxygenases contain Fe(II) in their active site, but HPCD can be activated by either Mn(II) or Fe(II). These enzymes belong to the type I class II family of extradiol dioxygenases. The class III 3,4-dihydroxyphenylacetate 2,3-dioxygenases belong to a different superfamily.


Pssm-ID: 319927  Cd Length: 118  Bit Score: 76.29  E-value: 2.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417   5 VMRPGHVQLRVLDMSKALEHYVELLGLIEMDRDDqGRVYLKAWTEVDKFSLVLREADEPGMDFMGFKVVDEDALRQLERD 84
Cdd:cd07266    2 IIRLAHAELVVTDLAASREFYVDTLGLHVTDEDD-NAIYLRGVEEFIHHTLVLRKAPEAAVGHLGFRVRDEADLDKAAAF 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 499315417  85 LMAYGCAVEQLpagELNSCGRRVRFQAPSGHHFELYA 121
Cdd:cd07266   81 YKELGLPTEWR---EEPGQGRTLRVEDPFGFPIEFYL 114
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
150-266 1.40e-16

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 74.41  E-value: 1.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417  150 RFDHALMYGDELPATYDLFTKVLGFYLAEQVLDE-----------NGTRVAQFLSLSTKAHDVAFIHHpekgrlHHVSFH 218
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGeegglrsafflAGGRVLELLLNETPPPAAAGFGG------HHIAFI 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 499315417  219 LETWEDLLRAADLISMTDTSIDIGPTRHGLTHGKTiYFFDPSGNRNEV 266
Cdd:pfam00903  75 AFSVDDVDAAYDRLKAAGVEIVREPGRHGWGGRYS-YFRDPDGNLIEL 121
HPCD_C_class_II cd07256
C-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 149-285 1.72e-16

C-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily contains the C-terminal, catalytic, domain of HPCD. HPCD catalyses the second step in the degradation of 4-hydroxyphenylacetate to succinate and pyruvate. The aromatic ring of 4-hydroxyphenylacetate is opened by this dioxygenase to yield the 3,4-diol product, 2-hydroxy-5-carboxymethylmuconate semialdehyde. HPCD is a homotetramer and each monomer contains two structurally homologous barrel-shaped domains at the N- and C-terminus. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism. Most extradiol dioxygenases contain Fe(II) in their active site, but HPCD can be activated by either Mn(II) or Fe(II). These enzymes belong to the type I class II family of extradiol dioxygenases. The class III 3,4-dihydroxyphenylacetate 2,3-dioxygenases belong to a different superfamily.


Pssm-ID: 319919  Cd Length: 160  Bit Score: 75.23  E-value: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417 149 VRFDHALMYGDELPATYDlFTKVLGFYLAEQVLDENGTRVAQFLSLSTKAHDVAFIhhpeKG---RLHHVSFHLETWEDL 225
Cdd:cd07256    2 LRIDHFNQRVPDVDAGLR-YYEDLGFRVSEYTEDDDGETWAAWMHRKGGVHDTALT----NGngpRLHHVAFWVPEPHNI 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499315417 226 LRAADLISMTDTS--IDIGPTRHGLTHGKTIYFFDPSGNRNEVFCgGDY--NYPDHKPVTWTTD 285
Cdd:cd07256   77 IQTCDLMAAARYSdrIERGPGRHGVSNAFFLYILDPDGHRIEIYT-SDYytVDPDNPPIKWDVH 139
BphC-JF8_N_like cd09013
N-terminal, non-catalytic, domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 9-125 5.94e-16

N-terminal, non-catalytic, domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase) from Bacillus sp. JF8, and similar proteins; 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, a key step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). BphC belongs to the type I extradiol dioxygenase family, which requires a metal ion in the active site in its catalytic mechanism. Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. This subfamily of BphC is represented by the enzyme purified from the thermophilic biphenyl and naphthalene degrader, Bacillus sp. JF8. The members in this family of BphC enzymes may use either Mn(II) or Fe(II) as cofactors. The enzyme purified from Bacillus sp. JF8 is Mn(II)-dependent, however, the enzyme from Rhodococcus jostii RHAI has Fe(II) bound to it. BphC_JF8 is thermostable and its optimum activity is at 85 degrees C. The enzymes in this family have an internal duplication. This family represents the N-terminal repeat.


Pssm-ID: 319955  Cd Length: 121  Bit Score: 72.77  E-value: 5.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417   9 GHVQLRVLDMSKALEHYVELLGLIEMDRDDQGrVYLKAWTEVDKFSLVLREADEPGMDFMGFKVVDEDALRQLERDLMAY 88
Cdd:cd09013    8 AHVELLTPKPEESLWFFTDVLGLEETHREGQS-VYLRAWGDWEHHTLKLTESPEAGLGHIAWRASSPEALERRVAALEAS 86

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 499315417  89 GCAVeQLPAGELNScGRRVRFQAPSGHHFELYADKEY 125
Cdd:cd09013   87 GVGI-GWIDGDLGQ-GPAYRFQSPDGHPMEIYWEVEK 121
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-124 3.59e-09

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 53.84  E-value: 3.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417   6 MRPGHVQLRVLDMSKALEHYVELLGLIEMDRDDQ--GRVYLKAWTEVDKFSLVLREADE-------PGMDFMGFKVvdeD 76
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFgdGGFGHAFLRLGDGTELELFEAPGaapapggGGLHHLAFRV---D 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 499315417  77 ALRQLERDLMAYGCAVEQLPaGELNSCGRRVRFQAPSGHHFELYADKE 124
Cdd:COG0346   78 DLDAAYARLRAAGVEIEGEP-RDRAYGYRSAYFRDPDGNLIELVEPPP 124
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
150-285 5.05e-09

Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 53.81  E-value: 5.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417 150 RFDHALMYGDELPATYDLFTKVLGFylaeQVLDENGTRVaqFLSLSTKAHDVAFIHHPE------KGRLHHVSFHLETWE 223
Cdd:COG2514    3 RLGHVTLRVRDLERSAAFYTDVLGL----EVVEREGGRV--YLRADGGEHLLVLEEAPGapprpgAAGLDHVAFRVPSRA 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499315417 224 DLLRAADLISMTDTSIDiGPTRHGltHGKTIYFFDPSGNRNEVFCggdynypDHKPVTWTTD 285
Cdd:COG2514   77 DLDAALARLAAAGVPVE-GAVDHG--VGESLYFRDPDGNLIELYT-------DRPRFEHVGD 128
BphC1-RGP6_N_like cd07252
N-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase; This subfamily contains the ...
 9-120 1.37e-07

N-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase; This subfamily contains the N-terminal, non-catalytic, domain of BphC1-RGP6 and similar proteins. BphC catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). This subfamily of BphCs belongs to the type I extradiol dioxygenase family, which require a metal in the active site in its catalytic mechanism. Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of 2,3-dihydroxybiphenyl 1,2-dioxygenases. For example, three types of BphC enzymes have been found in Rhodococcus globerulus (BphC1-RGP6 - BphC3-RGP6), all three enzymes are type I extradiol dioxygenases. BphC1-RGP6 has an internal duplication, it is a two-domain dioxygenase which forms octamers, and has Fe(II) at the catalytic site. Its N-terminal repeat is represented in this subfamily. BphC2-RGP6 and BphC3-RGP6 are one-domain dioxygenases, they belong to a different family, the ED_TypeI_classII_C (C-terminal domain of type I, class II extradiol dioxygenases) family.


Pssm-ID: 319915  Cd Length: 120  Bit Score: 49.52  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417   9 GHVQLRVLDMSKALEHYVELLGLIEMDRDDQGRVYLKawteVD--KFSLVLREADEPGMDFMGFKVVDEDALRQLERDLM 86
Cdd:cd07252    4 GYLGFEVSDLDAWREFATDVLGLQVADDGPDDALYLR----MDdrAHRIAVHPGEVDDLAYAGWEVADEAALDALAERLE 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 499315417  87 AYGCAVEQLPAGELNScgRRV----RFQAPSGHHFELY 120
Cdd:cd07252   80 AAGIEVTTGSAELAAE--RGVlgliKFTDPSGNPHEIF 115
PpCmtC_N cd08361
N-terminal domain of 2,3-dihydroxy-p-cumate-3,4-dioxygenase (PpCmtC); This subfamily contains ...
 11-127 2.14e-07

N-terminal domain of 2,3-dihydroxy-p-cumate-3,4-dioxygenase (PpCmtC); This subfamily contains the N-terminal, non-catalytic, domain of PpCmtC. 2,3-dihydroxy-p-cumate-3,4-dioxygenase (CmtC of Pseudomonas putida F1) is a dioxygenase involved in the eight-step catabolism pathway of p-cymene. CmtC acts upon the reaction intermediate 2,3-dihydroxy-p-cumate, yielding 2-hydroxy-3-carboxy-6-oxo-7-methylocta-2,4-dienoate. The CmtC belongs to the type I family of extradiol dioxygenases. Fe2+ was suggested as a cofactor, same as other enzymes in the family. The type I family of extradiol dioxygenases contains two structurally homologous barrel-shaped domains at the N- and C-terminal. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism.


Pssm-ID: 319949  Cd Length: 124  Bit Score: 48.75  E-value: 2.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417  11 VQLRVLDMSKALEHYVELLGLIEMDRDdQGRVYLKAwtevDK--FSLVLREADePGMDFMGFKVVDEDALRQLERDLMAY 88
Cdd:cd08361   10 VRLGTRDLEEAVRFATDILGLELVRRE-GGAAYFRS----DDrdHTLCYFEGD-PAEQTSGFEVRDPAELDAAAAELESA 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499315417  89 GCAVEqlpAGELNSCG-RRVR----FQAPSGHHFELYADKEYTG 127
Cdd:cd08361   84 GIAVR---RGTAEECEqRRVRafisFRDPSGNRIELVVRPHHSG 124
BphC5-RK37_C_like cd07239
C-terminal, catalytic domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase); 2, ...
 149-288 2.87e-07

C-terminal, catalytic domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase); 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). The enzyme contains a N-terminal and a C-terminal domain of similar structure fold, resulting from an ancient gene duplication. BphC belongs to the type I extradiol dioxygenase family, which requires a metal in the active site for its catalytic activity. Polychlorinated biphenyl degrading bacteria demonstrate multiplicity of BphCs. Bacterium Rhodococcus rhodochrous K37 has eight genes encoding BphC enzymes. This family includes the C-terminal domain of BphC5-RrK37. The crystal structure of the protein from Novosphingobium aromaticivorans has a Mn(II)in the active site, although most proteins of type I extradiol dioxygenases are activated by Fe(II).


Pssm-ID: 319904  Cd Length: 143  Bit Score: 49.12  E-value: 2.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417 149 VRFDHALMYGDELPATYDLFTKVLGFYLAEQVLDengtrVAQFLSLSTKAHDVAFIHHPEKGrLHHVSFHLETWEDLLRA 228
Cdd:cd07239    3 VKLSHVVLNSPDLDKTVAFYEDVLGFRVSDWLGD-----VMHFLRCNSQHHSIAIARGPHTS-LNHVAYEMRSVDEYMRG 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499315417 229 ADLISMTDTSIDIGPTRHGLTHGKTIYFFDPSGNRNEVFCGGD------YNYPDHKPVTWTTDQLG 288
Cdd:cd07239   77 SGRLIRSGARKIWGPGRHMAGDNTFSYFLDPHGNVVEYTSELElldedwHPHVVDFSEPEVTDQWG 142
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 150-271 2.93e-07

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 48.45  E-value: 2.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417 150 RFDHALMYGDELPATYDLFTKVLGFYLAEQV-LDENGTRVAqFLSLStKAHDVAFIHHP------EKGRLHHVSFH---L 219
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTdFGDGGFGHA-FLRLG-DGTELELFEAPgaapapGGGGLHHLAFRvddL 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499315417 220 ETWEDLLRAADLismtdtSIDIGPTRHGlTHGKTIYFFDPSGNRNEVFCGGD 271
Cdd:COG0346   80 DAAYARLRAAGV------EIEGEPRDRA-YGYRSAYFRDPDGNLIELVEPPP 124
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 153-266 3.75e-06

vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases.


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 45.21  E-value: 3.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417 153 HALMYGDELPATYDLFTKVLGFylaeQVLDENGTRVAQFLSLStKAHDVAFIHHPEK-----GRLHHVSFHLETWEDLLR 227
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGF----EVVSRNEGGGFAFLRLG-PGLRLALLEGPEPerpggGGLFHLAFEVDDVDEVDE 75

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 499315417 228 AADLISMTDTSIDIGPTRHGltHGKTIYFFDPSGNRNEV 266
Cdd:cd06587   76 RLREAGAEGELVAPPVDDPW--GGRSFYFRDPDGNLIEF 112
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 5-124 6.58e-05

Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function prediction only];


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 41.54  E-value: 6.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417   5 VMRPGHVQLRVLDMSKALEHYVELLGLIEMDRDDQGRVYLKAWTEVDKFSLVLREADEPGMDF--MGFKVVD-EDALRQL 81
Cdd:COG3324    2 PGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPGGDYAEFDTDGGQVGGLMPGAEEPGGPGwlLYFAVDDlDAAVARV 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 499315417  82 ErdlmAYGCAVEQLPAgELNSCGRRVRFQAPSGHHFELYADKE 124
Cdd:COG3324   82 E----AAGGTVLRPPT-DIPPWGRFAVFRDPEGNRFGLWQPAA 119
PpCmtC_C cd07258
C-terminal domain of 2,3-dihydroxy-p-cumate-3,4-dioxygenase (PpCmtC); This subfamily contains ...
 166-261 7.15e-05

C-terminal domain of 2,3-dihydroxy-p-cumate-3,4-dioxygenase (PpCmtC); This subfamily contains the C-terminal, catalytic, domain of PpCmtC. 2,3-dihydroxy-p-cumate-3,4-dioxygenase (CmtC of Pseudomonas putida F1) is a dioxygenase involved in the eight-step catabolism pathway of p-cymene. CmtC acts upon the reaction intermediate 2,3-dihydroxy-p-cumate, yielding 2-hydroxy-3-carboxy-6-oxo-7-methylocta-2,4-dienoate. The CmtC belongs to the type I family of extradiol dioxygenases. Fe2+ was suggested as a cofactor, same as for other enzymes in the family. The type I family of extradiol dioxygenases contains two structurally homologous barrel-shaped domains at the N- and C-terminal. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism.


Pssm-ID: 319921  Cd Length: 138  Bit Score: 42.19  E-value: 7.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417 166 DLFTKVLGFYLAEQVLDENGTRVAQFlslstkAHDVAFIHHPEKGrLHHVSFHLETWEDLLRAADLISMTDTSIDIGPTR 245
Cdd:cd07258   15 DFWTDVCNARVSDRIGDIFLMRVNAI------HHTFALGPASSSG-IQHINHQVTSIDDVLRSYYRLKEHDVPIVFGPGR 87

                         90
                 ....*....|....*.
gi 499315417 246 HGLTHGKTIYFFDPSG 261
Cdd:cd07258   88 HPTSGARFLYFKGPDG 103
BphC2-C3-RGP6_C_like cd08348
The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus ...
 159-268 1.01e-04

The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus globerulus P6 BphC2-RGP6 and BphC3-RGP6, and similar proteins. BphC catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, yielding 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid. This is the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). This subfamily of BphCs belongs to the type I extradiol dioxygenase family, which require a metal in the active site in its catalytic mechanism. Most type I extradiol dioxygenases are activated by Fe(II). Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. For example, three types of BphC enzymes have been found in Rhodococcus globerulus (BphC1-RGP6 - BphC3-RGP6), all three enzymes are type I extradiol dioxygenases. BphC2-RGP6 and BphC3-RGP6 are one-domain dioxygenases, which form hexamers. BphC1-RGP6 has an internal duplication, it is a two-domain dioxygenase which forms octamers, its two domains do not belong to this subfamily.


Pssm-ID: 319936  Cd Length: 137  Bit Score: 41.74  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417 159 DELPATYDLFTKVLGfylAEQVLDENGtrvAQFLSLSTKAHDVAFIHHPEKGR----------LHHVSFHLETWEDLLRA 228
Cdd:cd08348   12 EKFEAMVQWYLDILG---ARIVARNAK---GCFLSFDEEHHRIAIFGAPGGAQppdkrptrvgLAHIAFTYASLDDLARN 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 499315417 229 adLISMTDTSIDIG-PTRHGLTHGktIYFFDPSGNRNEVFC 268
Cdd:cd08348   86 --YAQLKERGIKPVwPVNHGVTTS--IYYRDPDGNMLEMQV 122
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 10-119 1.33e-04

vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases.


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 40.59  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417  10 HVQLRVLDMSKALEHYVELLGLIEMDRDDQGRVYLKAWTEVDKFSLV----LREADEPGMDFMGFKVVDEDALRQLERDL 85
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGFAFLRLGPGLRLALLegpePERPGGGGLFHLAFEVDDVDEVDERLREA 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 499315417  86 MAYGCAVEQLPAGELNscGRRVRFQAPSGHHFEL 119
Cdd:cd06587   81 GAEGELVAPPVDDPWG--GRSFYFRDPDGNLIEF 112
THT_oxygenase_C cd07257
The C-terminal domain of 2,4,5-trihydroxytoluene (THT) oxygenase; This subfamily contains the ...
 163-279 1.78e-04

The C-terminal domain of 2,4,5-trihydroxytoluene (THT) oxygenase; This subfamily contains the C-terminal, catalytic, domain of THT oxygenase. THT oxygenase is an extradiol dioxygenase in the 2,4-dinitrotoluene (DNT) degradation pathway. It catalyzes the conversion of 2,4,5-trihydroxytoluene to an unstable ring fission product, 2,4-dihydroxy-5-methyl-6-oxo-2,4-hexadienoic acid. The native protein was determined to be a dimer by gel filtration. The enzyme belongs to the type I family of extradiol dioxygenases which contains two structurally homologous barrel-shaped domains at the N- and C-terminus of each monomer. The active-site metal is located in the C-terminal barrel. Fe(II) is required for its catalytic activity.


Pssm-ID: 319920  Cd Length: 152  Bit Score: 41.17  E-value: 1.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417 163 ATYDLFTKVLGFYLAEQVLDENGTRVAQFLSLS-----TKAHDVAFIHHPeKGRLHHVSFHLETWEDLLRAADLISMTDT 237
Cdd:cd07257   14 ATFDWYTKTFGLKPSDVIYLPDGKTVGSFLHLDrgseyVDHHSFFFAQGP-RPKVHHAAFEVHDFDSQVLGHDWLREKGY 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499315417 238 SIDIGPTRHGLthGKTI--YFFDPSGNRNEVFCGGDYNYPDHKP 279
Cdd:cd07257   93 KHVWGVGRHIL--GSQIfdYWFDPSGFIVEHYTDGDLVNADTPI 134
BphC1-RGP6_C_like cd07237
C-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase; This subfamily contains the ...
 159-295 2.02e-04

C-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase; This subfamily contains the C-terminal, catalytic, domain of BphC1-RGP6 and similar proteins. BphC catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). This subfamily of BphCs belongs to the type I extradiol dioxygenase family, which require a metal in the active site in its catalytic mechanism. Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. For example, three types of BphC enzymes have been found in Rhodococcus globerulus (BphC1-RGP6 - BphC3-RGP6), all three enzymes are type I extradiol dioxygenases. BphC1-RGP6 has an internal duplication, it is a two-domain dioxygenase which forms octamers, and has Fe(II) at the catalytic site. Its C-terminal repeat is represented in this subfamily. BphC2-RGP6 and BphC3-RGP6 are one-domain dioxygenases, they belong to a different subfamily of the ED_TypeI_classII_C (C-terminal domain of type I, class II extradiol dioxygenases) family.


Pssm-ID: 319902  Cd Length: 153  Bit Score: 41.11  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417 159 DELPATYDLFTKVLGF----YLAEQVLDENGTRVAqFLSLSTKAHDVAFIHHPEKGRLHHVSFHLETWEDLLRAADL--- 231
Cdd:cd07237   18 PDVDEALAFYTDVLGFrlsdEIRIPLPPGVTARLH-FLHCNGRHHSLAFGAGPGPKRLHHLMLEVTSLDDVGRAYDRvrk 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499315417 232 ----ISMTdtsidIGptRHGLTHGKTIYFFDPSGNRNEVFCGGDYNYPDHKPVTWTTDqlgkAIFYHD 295
Cdd:cd07237   97 rgipIAMT-----LG--RHTNDKMLSFYVATPSGFLIEYGWGGRVVDEDWTVEEYDAP----SIWGHK 153
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 166-268 8.46e-04

N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC superfamily contains Bacillus subtilis CatE and similar proteins. CatE is proposed to function as Catechol-2,3-dioxygenase. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319918  Cd Length: 124  Bit Score: 38.45  E-value: 8.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417 166 DLFTKVLGFylaeQVLDENGTRVA------QFLSLSTKAHDVAFIHHPEKGrLHHVSFHLETWEDLLRAadLISMTDTSI 239
Cdd:cd07255   18 AFYQNVIGL----SVLKQNASRAYlgvdgkQVLLVLEAIPDAVLAPRSTTG-LYHFAILLPDRKALGRA--LAHLAEHGP 90

                         90       100
                 ....*....|....*....|....*....
gi 499315417 240 DIGPTRHGLTHGktIYFFDPSGNRNEVFC 268
Cdd:cd07255   91 LIGAADHGVSEA--IYLSDPEGNGIEIYA 117
THT_Oxygenase_N cd07267
N-terminal domain of 2,4,5-trihydroxytoluene (THT) oxygenase; This subfamily contains the ...
 5-119 1.53e-03

N-terminal domain of 2,4,5-trihydroxytoluene (THT) oxygenase; This subfamily contains the N-terminal, non-catalytic, domain of THT oxygenase. THT oxygenase is an extradiol dioxygenase in the 2,4-dinitrotoluene (DNT) degradation pathway. It catalyzes the conversion of 2,4,5-trihydroxytoluene to an unstable ring fission product, 2,4-dihydroxy-5-methyl-6-oxo-2,4-hexadienoic acid. The native protein was determined to be a dimer by gel filtration. The enzyme belongs to the type I family of extradiol dioxygenases which contains two structurally homologous barrel-shaped domains at the N- and C-terminus of each monomer. The active-site metal is located in the C-terminal barrel. Fe(II) is required for its catalytic activity.


Pssm-ID: 319928  Cd Length: 113  Bit Score: 37.64  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499315417   5 VMRPGHVQLRVLDMSKALEHYVELlGLIEMDRDDqGRVYLKAWTEvDKFSLVLREADEPGMDFMGFKVVDEDALRQLERd 84
Cdd:cd07267    1 LTRLAHVVYEHPDLEKAERFLTDF-GLIVAYRTG-EEIYYRGYGT-DPYVYVARKSSRSRFLGAAFVAASRADLEKAAT- 76

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 499315417  85 lmAYGC-AVEQL--PAGelnscGRRVRFQAPSGHHFEL 119
Cdd:cd07267   77 --LPGAsPIEDLeaPGG-----GKVVTLTDPDGFPVHL 107
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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