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Conserved domains on  [gi|33356873|pdb|1F1X|A]
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Chain A, HOMOPROTOCATECHUATE 2,3-DIOXYGENASE

Protein Classification

HpaD family protein( domain architecture ID 11494141)

HpaD family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HpaD TIGR02295
3,4-dihydroxyphenylacetate 2,3-dioxygenase; This enzyme catalyzes the second step in the ...
 14-309 3.52e-180

3,4-dihydroxyphenylacetate 2,3-dioxygenase; This enzyme catalyzes the second step in the degradation of 4-hydroxyphenylacetate to succinate and pyruvate. 4-hydroxyphenylacetate arises from the degradation of tyrosine. The substrate, 3,4-dihydroxyphenylacetate (homoprotocatechuate) arises from the action of a hydroxylase on 4-hydroxyphenylacetate. The aromatic ring is opened by this dioxygenase exo to the 3,4-diol resulting in 2-hydroxy-5-carboxymethylmuconate semialdehyde. The enzyme from Bacillus brevis contains manganese.


:

Pssm-ID: 213698 [Multi-domain]  Cd Length: 294  Bit Score: 499.25  E-value: 3.52e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A         14 DILRCAYAELVVTDLAKSRNFYVDVLGLHVSYEDENQIYLRSFEEFIHHNLVLTKGPVAALKAMAFRVRTPEDVDKAEAY 93
Cdd:TIGR02295   1 NILRTGHVELRVTDLDKSREFYVDLLGFRETESDKEYIYLRGIEEFQHHSLVLTKAPSAALSYIGFRVSKEEDLDKAADF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A         94 YQELGCRTERRKDGFVKgigDALRVEDPLGFPYEFFFETTHVERLHMRYDLYSAGELVRLDHFNQVTPDVPRGRKYL-ED 172
Cdd:TIGR02295  81 FQKLGHPVRLVRDGGQP---EALRVEDPFGYPIEFYFEMEKVERLLRRYHRHRGVSPVRLDHFNVFVPDVQRALRFYkEE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A        173 LGFRVTEDIQDDEGTTYAAWMHRKGTVHDTALTGGNGPRLHHVAFSTHEKHNIIQICDKMGALRISDRIERGPGRHGVSN 252
Cdd:TIGR02295 158 LGFRVTEYTEDDEGNLAAAWLHRKGGVHDIALTNGNGPRLHHIAYWVHDPLNIIKACDILASAGLSDSIERGPGRHGVSN 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
1F1X_A        253 AFYLYILDPDNHRIEIYTQDYYTGDPDNPTITWNVHDNQRRDWWGNPVVPSWYTEAS 309
Cdd:TIGR02295 238 AFFLYLRDPDGHRIELYTGDYLTGDPDWPPIRWTLDDPQRQTLWGHPAPPSWFTEAS 294
 
Name Accession Description Interval E-value
HpaD TIGR02295
3,4-dihydroxyphenylacetate 2,3-dioxygenase; This enzyme catalyzes the second step in the ...
 14-309 3.52e-180

3,4-dihydroxyphenylacetate 2,3-dioxygenase; This enzyme catalyzes the second step in the degradation of 4-hydroxyphenylacetate to succinate and pyruvate. 4-hydroxyphenylacetate arises from the degradation of tyrosine. The substrate, 3,4-dihydroxyphenylacetate (homoprotocatechuate) arises from the action of a hydroxylase on 4-hydroxyphenylacetate. The aromatic ring is opened by this dioxygenase exo to the 3,4-diol resulting in 2-hydroxy-5-carboxymethylmuconate semialdehyde. The enzyme from Bacillus brevis contains manganese.


Pssm-ID: 213698 [Multi-domain]  Cd Length: 294  Bit Score: 499.25  E-value: 3.52e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A         14 DILRCAYAELVVTDLAKSRNFYVDVLGLHVSYEDENQIYLRSFEEFIHHNLVLTKGPVAALKAMAFRVRTPEDVDKAEAY 93
Cdd:TIGR02295   1 NILRTGHVELRVTDLDKSREFYVDLLGFRETESDKEYIYLRGIEEFQHHSLVLTKAPSAALSYIGFRVSKEEDLDKAADF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A         94 YQELGCRTERRKDGFVKgigDALRVEDPLGFPYEFFFETTHVERLHMRYDLYSAGELVRLDHFNQVTPDVPRGRKYL-ED 172
Cdd:TIGR02295  81 FQKLGHPVRLVRDGGQP---EALRVEDPFGYPIEFYFEMEKVERLLRRYHRHRGVSPVRLDHFNVFVPDVQRALRFYkEE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A        173 LGFRVTEDIQDDEGTTYAAWMHRKGTVHDTALTGGNGPRLHHVAFSTHEKHNIIQICDKMGALRISDRIERGPGRHGVSN 252
Cdd:TIGR02295 158 LGFRVTEYTEDDEGNLAAAWLHRKGGVHDIALTNGNGPRLHHIAYWVHDPLNIIKACDILASAGLSDSIERGPGRHGVSN 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
1F1X_A        253 AFYLYILDPDNHRIEIYTQDYYTGDPDNPTITWNVHDNQRRDWWGNPVVPSWYTEAS 309
Cdd:TIGR02295 238 AFFLYLRDPDGHRIELYTGDYLTGDPDWPPIRWTLDDPQRQTLWGHPAPPSWFTEAS 294
HPCD_C_class_II cd07256
C-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 150-309 2.17e-111

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: 319.83  E-value: 2.17e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A      150 LVRLDHFNQVTPDVPRGRKYLEDLGFRVTEDIQDDEGTTYAAWMHRKGTVHDTALTGGNGPRLHHVAFSTHEKHNIIQIC 229
Cdd:cd07256   1 LLRIDHFNQRVPDVDAGLRYYEDLGFRVSEYTEDDDGETWAAWMHRKGGVHDTALTNGNGPRLHHVAFWVPEPHNIIQTC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A      230 DKMGALRISDRIERGPGRHGVSNAFYLYILDPDNHRIEIYTQDYYTGDPDNPTITWNVHDNQRRDWWGNPVVPSWYTEAS 309
Cdd:cd07256  81 DLMAAARYSDRIERGPGRHGVSNAFFLYILDPDGHRIEIYTSDYYTVDPDNPPIKWDVHDPQRQTWWGAPVPRSWFEEAS 160
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
15-179 9.98e-20

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 83.85  E-value: 9.98e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A       15 ILRCAYAELVVTDLAKSRNFYVDVLGLHVSYEDENQIYLRSFEEfiHHNLVLTKGPVAALKA-------MAFRVRTPEDV 87
Cdd:COG2514   1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGG--EHLLVLEEAPGAPPRPgaagldhVAFRVPSRADL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A       88 DKAEAYYQELGCRTERRKDGFVkgiGDALRVEDPLGFPYEFFFETTHVERlhmrydlysagelvrldhfnqvTPDVPRgr 167
Cdd:COG2514  79 DAALARLAAAGVPVEGAVDHGV---GESLYFRDPDGNLIELYTDRPRFEH----------------------VGDLET-- 131

                       170
                ....*....|..
1F1X_A      168 kylEDLGFRVTE 179
Cdd:COG2514 132 ---DVLGFRLSD 140
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
152-268 7.37e-13

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 64.39  E-value: 7.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A        152 RLDHFNQVTPDVPRGRKYLED-LGFRVTEDI-QDDEGTTYAAWMHRKGTVHD-----TALTGGNGPRLHHVAFSTHEKHN 224
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDvLGFKLVEETdAGEEGGLRSAFFLAGGRVLElllneTPPPAAAGFGGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
1F1X_A        225 IIQICDKMGALRIsdRIERGPGRHGVSNAFYlYILDPDNHRIEI 268
Cdd:pfam00903  81 VDAAYDRLKAAGV--EIVREPGRHGWGGRYS-YFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
HpaD TIGR02295
3,4-dihydroxyphenylacetate 2,3-dioxygenase; This enzyme catalyzes the second step in the ...
 14-309 3.52e-180

3,4-dihydroxyphenylacetate 2,3-dioxygenase; This enzyme catalyzes the second step in the degradation of 4-hydroxyphenylacetate to succinate and pyruvate. 4-hydroxyphenylacetate arises from the degradation of tyrosine. The substrate, 3,4-dihydroxyphenylacetate (homoprotocatechuate) arises from the action of a hydroxylase on 4-hydroxyphenylacetate. The aromatic ring is opened by this dioxygenase exo to the 3,4-diol resulting in 2-hydroxy-5-carboxymethylmuconate semialdehyde. The enzyme from Bacillus brevis contains manganese.


Pssm-ID: 213698 [Multi-domain]  Cd Length: 294  Bit Score: 499.25  E-value: 3.52e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A         14 DILRCAYAELVVTDLAKSRNFYVDVLGLHVSYEDENQIYLRSFEEFIHHNLVLTKGPVAALKAMAFRVRTPEDVDKAEAY 93
Cdd:TIGR02295   1 NILRTGHVELRVTDLDKSREFYVDLLGFRETESDKEYIYLRGIEEFQHHSLVLTKAPSAALSYIGFRVSKEEDLDKAADF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A         94 YQELGCRTERRKDGFVKgigDALRVEDPLGFPYEFFFETTHVERLHMRYDLYSAGELVRLDHFNQVTPDVPRGRKYL-ED 172
Cdd:TIGR02295  81 FQKLGHPVRLVRDGGQP---EALRVEDPFGYPIEFYFEMEKVERLLRRYHRHRGVSPVRLDHFNVFVPDVQRALRFYkEE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A        173 LGFRVTEDIQDDEGTTYAAWMHRKGTVHDTALTGGNGPRLHHVAFSTHEKHNIIQICDKMGALRISDRIERGPGRHGVSN 252
Cdd:TIGR02295 158 LGFRVTEYTEDDEGNLAAAWLHRKGGVHDIALTNGNGPRLHHIAYWVHDPLNIIKACDILASAGLSDSIERGPGRHGVSN 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
1F1X_A        253 AFYLYILDPDNHRIEIYTQDYYTGDPDNPTITWNVHDNQRRDWWGNPVVPSWYTEAS 309
Cdd:TIGR02295 238 AFFLYLRDPDGHRIELYTGDYLTGDPDWPPIRWTLDDPQRQTLWGHPAPPSWFTEAS 294
HPCD_C_class_II cd07256
C-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 150-309 2.17e-111

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: 319.83  E-value: 2.17e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A      150 LVRLDHFNQVTPDVPRGRKYLEDLGFRVTEDIQDDEGTTYAAWMHRKGTVHDTALTGGNGPRLHHVAFSTHEKHNIIQIC 229
Cdd:cd07256   1 LLRIDHFNQRVPDVDAGLRYYEDLGFRVSEYTEDDDGETWAAWMHRKGGVHDTALTNGNGPRLHHVAFWVPEPHNIIQTC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A      230 DKMGALRISDRIERGPGRHGVSNAFYLYILDPDNHRIEIYTQDYYTGDPDNPTITWNVHDNQRRDWWGNPVVPSWYTEAS 309
Cdd:cd07256  81 DLMAAARYSDRIERGPGRHGVSNAFFLYILDPDGHRIEIYTSDYYTVDPDNPPIKWDVHDPQRQTWWGAPVPRSWFEEAS 160
HPCD_N_class_II cd07266
N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 14-134 6.43e-66

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: 203.02  E-value: 6.43e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A       14 DILRCAYAELVVTDLAKSRNFYVDVLGLHVSYEDENQIYLRSFEEFIHHNLVLTKGPVAALKAMAFRVRTPEDVDKAEAY 93
Cdd:cd07266   1 DIIRLAHAELVVTDLAASREFYVDTLGLHVTDEDDNAIYLRGVEEFIHHTLVLRKAPEAAVGHLGFRVRDEADLDKAAAF 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
1F1X_A       94 YQELGCRTERRkdgFVKGIGDALRVEDPLGFPYEFFFETTH 134
Cdd:cd07266  81 YKELGLPTEWR---EEPGQGRTLRVEDPFGFPIEFYLEMDH 118
catechol_2_3 TIGR03211
catechol 2,3 dioxygenase; Members of this family all are enzymes active as catechol 2,3 ...
 14-306 2.68e-63

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: 202.47  E-value: 2.68e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A         14 DILRCAYAELVVTDLAKSRNFYVDVLGLHVSYEDENQIYLRSFEEFIHHNLVLTKGPVAALKAMAFRVRTPEDVDKAEAY 93
Cdd:TIGR03211   1 GVMRLGHVELRVLDLEESLKHYTDVLGLEETGRDGQRVYLKAWDEWDHYSVILTEADTAGLDHMAFKVESEADLERLVKR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A         94 YQELGCRTERRKDGFVKGIGDALRVEDPLGFPYEFFFETTHVERLHMRY-------DLYSAGeLVRLDHFNQVTPDVPRG 166
Cdd:TIGR03211  81 LEAYGVGTGWIPAGELPGVGRRVRFTLPSGHTMELYAEKEYVGELVGGLnpdpwpdPLRGVG-ARRLDHCLLYGEDVAEN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A        167 RKYLED-LGFRVTEDIQDDEGTTYAA-WMHRKGTVHDTALTGGNGP-RLHHVAFSTHEKHNIIQICDKMGALRISdrIER 243
Cdd:TIGR03211 160 TRFFTEvLGFRLTEQVVLGDGKEMAAaWLSVSNKAHDIAFVGDPEPgKLHHVSFFLDSWEDVLKAADVMSKNDVS--IDI 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
1F1X_A        244 GPGRHGVSNAFYLYILDPDNHRIEIYTQDYYTgDPDNPTITWNVHDNQRRD-WWGNPVVPSWYT 306
Cdd:TIGR03211 238 GPTRHGITRGQTIYFFDPSGNRNETFAGGYLA-YPDWPPITWTEDELGRGIfYHGRVLNESFHT 300
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 20-131 2.09e-45

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: 150.16  E-value: 2.09e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A       20 YAELVVTDLAKSRNFYVDVLGLHVSYEDENQIYLRSFEeFIHHNLVLTKGPVAALKAMAFRVRTPEDVDKAEAYYQELGC 99
Cdd:cd16360   1 YAELGVPDLEKALEFYTDVLGLQVAKRDGNSVYLRGYE-DEHHSLVLYEAPEAGLKHFAFEVASEEDLERAAASLTALGC 79

                        90       100       110
                ....*....|....*....|....*....|..
1F1X_A      100 RTERRKDGFVKGIGDALRVEDPLGFPYEFFFE 131
Cdd:cd16360  80 DVTWGPDGEVPGGGKGFRFQDPSGHLLELFVE 111
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 154-285 1.49e-38

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: 133.21  E-value: 1.49e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A      154 DHFNQVTPDVPRGRKYLED-LGFRVTEDIqDDEGTTYAAWMHRKG--TVHDTALTGGNGPRLHHVAFSTHEKHNIIQICD 230
Cdd:cd08343   1 GHVVLCSPDVEASRDFYTDvLGFRVSDRI-VDPGVDGGAFLHCDRgtDHHTVALAGGPHPGLHHVAFEVHDLDDVGRGHD 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
1F1X_A      231 KMGALRIsdRIERGPGRHGVSNAFYLYILDPDNHRIEIYTQDYYTgDPDNPTITW 285
Cdd:cd08343  80 RLREKGY--KIEWGPGRHGLGSQVFDYWFDPSGNRVEYYTDGDLV-DDDWPPKVH 131
BphC-JF8_C_like cd09014
C-terminal, catalytic domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase); 2, ...
 152-306 1.93e-32

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: 118.25  E-value: 1.93e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A      152 RLDHFNQVTPDVPRGRKYLED-LGFRVTEDIQDDEGTTYAAWMHRKGTVHDTALT----GGNGpRLHHVAFSTHEKHNII 226
Cdd:cd09014   6 RIDHLNLLASDVTANRQFMSDtLGFRLREQIRDNNGGEAGAWMSVSSLVHDVAVMrdgkGEPG-RLHHLAYWYGTPEDLL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A      227 QICDKMGALRISdrIERGPGRHGVSNAFYLYILDPDNHRIEIYTQD-YYTGDPDNPTITWNVHDNQRRDWWGNPVVP-SW 304
Cdd:cd09014  85 RAADIFREHGIQ--IEAGPGKHGISQAFFLYVYEPGGNRVELFGGAgYLIFDPDWEPVEWTEEDLDRGIAWGGPTLPdSF 162


                ..
1F1X_A      305 YT 306
Cdd:cd09014 163 FT 164
2_3_CTD_N cd07265
N-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the N-terminal, ...
 15-133 2.14e-21

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: 87.79  E-value: 2.14e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A       15 ILRCAYAELVVTDLAKSRNFYVDVLGLH-VSYEDENQIYLRSFEEFIHHNLVLTKGPVAALKAMAFRVRTPEDVDKAEAY 93
Cdd:cd07265   2 VLRPGHVQLRVLDLEEAIKHYREVLGLVeTGRDDQGRVYLKAWDEYDHHSIILREADTAGLDFMGFKVLDDADLEQLEAR 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
1F1X_A       94 YQELGCRTERRKDGFVKGIGDALRVEDPLGFPYEFFFETT 133
Cdd:cd07265  82 LQAYGVTVTRIPAGELPGVGRRVRFQLPSGHTMELYAEKE 121
BphC-JF8_N_like cd09013
N-terminal, non-catalytic, domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 13-132 4.10e-20

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: 84.32  E-value: 4.10e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A       13 PDILRCAYAELVVTDLAKSRNFYVDVLGLHVSYEDENQIYLRSFEEFIHHNLVLTKGPVAALKAMAFRVRTPEDVDKAEA 92
Cdd:cd09013   2 FDLAQLAHVELLTPKPEESLWFFTDVLGLEETHREGQSVYLRAWGDWEHHTLKLTESPEAGLGHIAWRASSPEALERRVA 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
1F1X_A       93 YYQELGcrTERRKDGFVKGIGDALRVEDPLGFPYEFFFET 132
Cdd:cd09013  82 ALEASG--VGIGWIDGDLGQGPAYRFQSPDGHPMEIYWEV 119
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
15-179 9.98e-20

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 83.85  E-value: 9.98e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A       15 ILRCAYAELVVTDLAKSRNFYVDVLGLHVSYEDENQIYLRSFEEfiHHNLVLTKGPVAALKA-------MAFRVRTPEDV 87
Cdd:COG2514   1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGG--EHLLVLEEAPGAPPRPgaagldhVAFRVPSRADL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A       88 DKAEAYYQELGCRTERRKDGFVkgiGDALRVEDPLGFPYEFFFETTHVERlhmrydlysagelvrldhfnqvTPDVPRgr 167
Cdd:COG2514  79 DAALARLAAAGVPVEGAVDHGV---GESLYFRDPDGNLIELYTDRPRFEH----------------------VGDLET-- 131

                       170
                ....*....|..
1F1X_A      168 kylEDLGFRVTE 179
Cdd:COG2514 132 ---DVLGFRLSD 140
2_3_CTD_C cd07243
C-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the C-terminal, ...
 151-285 1.97e-18

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: 80.53  E-value: 1.97e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A      151 VRLDHFNQVTPDVPRGRKYLED-LGFRVTEDIQD-DEGTTYAAWMHRKGTVHDTALTGG-NGPRLHHVAFSTHEKHNIIQ 227
Cdd:cd07243   5 HRLDHCLLYGERIAETTRFFTDvLGFYLTERVLDpDGGTRVGIFLSCSNKAHDIAFVGYpEDGKLHHTSFFLESWEDVLK 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
1F1X_A      228 ICDKMGALRIsdRIERGPGRHGVSNAFYLYILDPDNHRIEIYTQDYYTgDPDNPTITW 285
Cdd:cd07243  85 AGDIISKNDV--SIDIGPTRHGITRGQTIYFFDPSGNRNETFAGGYIA-YPDMPVVTW 139
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
152-268 7.37e-13

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 64.39  E-value: 7.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A        152 RLDHFNQVTPDVPRGRKYLED-LGFRVTEDI-QDDEGTTYAAWMHRKGTVHD-----TALTGGNGPRLHHVAFSTHEKHN 224
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDvLGFKLVEETdAGEEGGLRSAFFLAGGRVLElllneTPPPAAAGFGGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
1F1X_A        225 IIQICDKMGALRIsdRIERGPGRHGVSNAFYlYILDPDNHRIEI 268
Cdd:pfam00903  81 VDAAYDRLKAAGV--EIVREPGRHGWGGRYS-YFRDPDGNLIEL 121
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 20-128 9.59e-12

N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from Rhodococcus rhodochrous K37, and similar proteins; 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 N-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: 319950 [Multi-domain]  Cd Length: 120  Bit Score: 61.11  E-value: 9.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A       20 YAELVVTDLAKSRNFYVDVLGLHVSYEDENQIYLRSFEEFiHHNLVLTKGPVAALKAMAFRVRTPEDVDKAEAYYQELGC 99
Cdd:cd08362   6 YVALGVPDLAAEREFYTEVWGLEEVAEDDDVVYLRAEGSE-HHVLRLRQSDENRLDLIAFAAATRADVDALAARLAAAGV 84

                        90       100       110
                ....*....|....*....|....*....|..
1F1X_A      100 RTERRK---DGFVKGIGdaLRVEDPLGFPYEF 128
Cdd:cd08362  85 RILSEPgplDDPGGGYG--FRFFDPDGRTIEV 114
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 152-270 1.11e-11

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: 61.16  E-value: 1.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A      152 RLDHFNQVTPDVPRGRK-YLEDLGFRVTEDIQDDEGTTYAAWMhRKGTVHDTALT-------GGNGPRLHHVAFSTHekh 223
Cdd:COG0346   2 GLHHVTLRVSDLEASLAfYTDVLGLELVKRTDFGDGGFGHAFL-RLGDGTELELFeapgaapAPGGGGLHHLAFRVD--- 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
1F1X_A      224 NIIQICDKMGALRIsdRIERGPGRHGvSNAFYLYILDPDNHRIEIYT 270
Cdd:COG0346  78 DLDAAYARLRAAGV--EIEGEPRDRA-YGYRSAYFRDPDGNLIELVE 121
PpCmtC_N cd08361
N-terminal domain of 2,3-dihydroxy-p-cumate-3,4-dioxygenase (PpCmtC); This subfamily contains ...
 19-103 9.34e-10

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: 55.68  E-value: 9.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A       19 AYAELVVTDLAKSRNFYVDVLGLHVSYEDENQIYLRSfeEFIHHNLVLTKGPvAALKAMAFRVRTPEDVDKAEAYYQELG 98
Cdd:cd08361   8 RYVRLGTRDLEEAVRFATDILGLELVRREGGAAYFRS--DDRDHTLCYFEGD-PAEQTSGFEVRDPAELDAAAAELESAG 84


                ....*
1F1X_A       99 CRTER 103
Cdd:cd08361  85 IAVRR 89
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 20-128 3.64e-08

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: 50.99  E-value: 3.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A       20 YAELVVTDLAKSRNFYVDVLGLHVSYEDENQIYLRsFEEFIHHNLVLTKGPVAALKA------MAFRVRTPEDVDKAEAY 93
Cdd:cd06587   1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGFAF-LRLGPGLRLALLEGPEPERPGggglfhLAFEVDDVDEVDERLRE 79

                        90       100       110
                ....*....|....*....|....*....|....*
1F1X_A       94 YQELGCRTERRKDGFvkGIGDALRVEDPLGFPYEF 128
Cdd:cd06587  80 AGAEGELVAPPVDDP--WGGRSFYFRDPDGNLIEF 112
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
150-270 5.79e-08

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 51.11  E-value: 5.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A      150 LVRLDHFNQVTPDVPRGRKYLED-LGFRVTEdiQDDEGTTYAAWmhrkGTVH-------DTALTGGNGPRLHHVAFSTHE 221
Cdd:COG2514   1 ITRLGHVTLRVRDLERSAAFYTDvLGLEVVE--REGGRVYLRAD----GGEHllvleeaPGAPPRPGAAGLDHVAFRVPS 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
1F1X_A      222 KHNIIQICDKMGALRISdriERGPGRHGVSNAFYLYilDPDNHRIEIYT 270
Cdd:COG2514  75 RADLDAALARLAAAGVP---VEGAVDHGVGESLYFR--DPDGNLIELYT 118
BphC1-RGP6_N_like cd07252
N-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase; This subfamily contains the ...
 19-133 2.36e-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: 48.75  E-value: 2.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A       19 AYAELVVTDLAKSRNFYVDVLGLHV-SYEDENQIYLRSFEEfiHHNLVLTKGPVAALKAMAFRVRTPEDVDKAEAYYQEL 97
Cdd:cd07252   4 GYLGFEVSDLDAWREFATDVLGLQVaDDGPDDALYLRMDDR--AHRIAVHPGEVDDLAYAGWEVADEAALDALAERLEAA 81

                        90       100       110
                ....*....|....*....|....*....|....*...
1F1X_A       98 GC--RTERRKDGFVKGIGDALRVEDPLGFPYEFFFETT 133
Cdd:cd07252  82 GIevTTGSAELAAERGVLGLIKFTDPSGNPHEIFYGPR 119
BphC5-RK37_C_like cd07239
C-terminal, catalytic domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase); 2, ...
 151-297 1.66e-06

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: 46.81  E-value: 1.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A      151 VRLDHFNQVTPDVPRGRKYLED-LGFRVTEDIQDdegttYAAWMHRKGTVHDTALTGGNGPRLHHVAFsthEKHNIIQIC 229
Cdd:cd07239   3 VKLSHVVLNSPDLDKTVAFYEDvLGFRVSDWLGD-----VMHFLRCNSQHHSIAIARGPHTSLNHVAY---EMRSVDEYM 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1F1X_A      230 DKMGALRISD-RIERGPGRHGVSNAFYLYILDPDNHRIEiYTQDYYTGDPDNPTITWNVHDNQRRDWWG 297
Cdd:cd07239  75 RGSGRLIRSGaRKIWGPGRHMAGDNTFSYFLDPHGNVVE-YTSELELLDEDWHPHVVDFSEPEVTDQWG 142
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 23-129 2.45e-06

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: 46.14  E-value: 2.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A       23 LVVTDLAKSRNFYVDVLGLHVSYE---DENQIYLRSFEEFIHHNLVLTKGPVAALKA-------MAFRVrtpEDVDKAEA 92
Cdd:COG0346   8 LRVSDLEASLAFYTDVLGLELVKRtdfGDGGFGHAFLRLGDGTELELFEAPGAAPAPgggglhhLAFRV---DDLDAAYA 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
1F1X_A       93 YYQELGCRTER----RKDGFvkgigDALRVEDPLGFPYEFF 129
Cdd:COG0346  85 RLRAAGVEIEGeprdRAYGY-----RSAYFRDPDGNLIELV 120
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 22-97 1.17e-05

Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance protein, confers Bm resistance by directly binding to Bm. Bm is a glycopeptide antibiotic produced naturally by actinomycetes. It is a potent anti-cancer drug, which acts as a strong DNA-cutting agent, thereby causing cell death. BLMA is produced by actinomycetes to protect themselves against their own lethal compound. BLMA has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMAs are dimers and each dimer binds to two Bm molecules at the Bm-binding pockets formed at the dimer interface; two Bm molecules are bound per dimer. BLMA belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. As for the larger superfamily, this family contains members with or without domain swapping.


Pssm-ID: 319937 [Multi-domain]  Cd Length: 114  Bit Score: 43.75  E-value: 1.17e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1F1X_A       22 ELVVTDLAKSRNFYVDVLGLHVSYEDENQIYLRSFEEFIHHNLVLTKGPVAALKAMAFRVRtpedVDKAEAYYQEL 97
Cdd:cd08349   3 ILPVRDIDKTLAFYVDVLGFEVDYERPPPGYAILSRGGVELHLFEHPGLDPAGSGVAAYIR----VEDIDALHAEL 74
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 23-130 2.14e-05

vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; uncharacterized subfamily of vicinal oxygen chelate (VOC) family contains Bacillus subtilis YwkD and similar proteins. 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 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: 319940 [Multi-domain]  Cd Length: 123  Bit Score: 43.30  E-value: 2.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A       23 LVVTDLAKSRNFYVDVLGLHVSYE---------------DENQIYLRSFEEFihhNLVLTKGPVAALKAMAFRVrtpEDV 87
Cdd:cd08352   8 IICSDYEKSKDFYVDKLGFEIIREhyrperndikldlalGGYQLELFIKPDA---PARPSYPEALGLRHLAFKV---EDV 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
1F1X_A       88 DKAEAYYQELGCRTErrkdgfvkgigdALRVEDPLGFPYEFFF 130
Cdd:cd08352  82 EATVAELKSLGIETE------------PIRVDDFTGKKFTFFF 112
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
19-128 2.15e-05

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 43.21  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A         19 AYAELVVTDLAKSRNFYVDVLGLHVSYEDENQIYLRSFEEFI-----HHNLVLTKGPVAALK-----AMAFRVRTPEDVD 88
Cdd:pfam00903   3 DHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFlaggrVLELLLNETPPPAAAgfgghHIAFIAFSVDDVD 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
1F1X_A         89 KAEAYYQELGCRterrkdgFVKGIGD------ALRVEDPLGFPYEF 128
Cdd:pfam00903  83 AAYDRLKAAGVE-------IVREPGRhgwggrYSYFRDPDGNLIEL 121
PpCmtC_C cd07258
C-terminal domain of 2,3-dihydroxy-p-cumate-3,4-dioxygenase (PpCmtC); This subfamily contains ...
 169-267 2.80e-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: 43.34  E-value: 2.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A      169 YLEDLGFRVTEDIQDdegttyaAWMHRKGTVHDT-ALTGGNGPRLHHVAFSTHEKHNIIQICDKMGALRIsdRIERGPGR 247
Cdd:cd07258  17 WTDVCNARVSDRIGD-------IFLMRVNAIHHTfALGPASSSGIQHINHQVTSIDDVLRSYYRLKEHDV--PIVFGPGR 87

                        90       100
                ....*....|....*....|
1F1X_A      248 HGVSNAFYLYILDPDNHRIE 267
Cdd:cd07258  88 HPTSGARFLYFKGPDGMTFE 107
THT_Oxygenase_N cd07267
N-terminal domain of 2,4,5-trihydroxytoluene (THT) oxygenase; This subfamily contains the ...
 15-128 2.82e-05

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: 42.65  E-value: 2.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A       15 ILRCAYAELVVTDLAKSRNFYVDvLGLHVSYEDENQIYLRSF--EEFIHhnlVLTKGPVAALKAMAFRVRTPEDVDKAEA 92
Cdd:cd07267   1 LTRLAHVVYEHPDLEKAERFLTD-FGLIVAYRTGEEIYYRGYgtDPYVY---VARKSSRSRFLGAAFVAASRADLEKAAT 76

                        90       100       110
                ....*....|....*....|....*....|....*.
1F1X_A       93 YyqeLGCRTerRKDGFVKGIGDALRVEDPLGFPYEF 128
Cdd:cd07267  77 L---PGASP--IEDLEAPGGGKVVTLTDPDGFPVHL 107
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 23-92 3.99e-05

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 42.51  E-value: 3.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A       23 LVVTDLAKSRNFYVDvLGL--HVSYEDEN--------QIYL-----RSFEEFIHHNLVLTKGPVAALkaMAFRVRTPEDV 87
Cdd:COG3607   9 LPVADLERSRAFYEA-LGFtfNPQFSDEGaacfvlgeGIVLmllprEKFATFTGKPIADATGFTEVL--LALNVESREEV 85


                ....*....
1F1X_A       88 D----KAEA 92
Cdd:COG3607  86 DalvaKALA 94
MhqB_like_C cd08360
C-terminal domain of Burkholderia sp. NF100 MhqB and similar proteins; This subfamily contains ...
 152-261 4.64e-05

C-terminal domain of Burkholderia sp. NF100 MhqB and similar proteins; This subfamily contains the C-terminal, catalytic, domain of Burkholderia sp. NF100 MhqB and similar proteins. MhqB is a type I extradiol dioxygenase involved in the catabolism of methylhydroquinone, an intermediate in the degradation of fenitrothion. The purified enzyme has shown extradiol ring cleavage activity toward 3-methylcatechol. Fe2+ was suggested as a cofactor, the same as most other enzymes in the family. Burkholderia sp. NF100 MhqB is encoded on the plasmid pNF1. 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: 319948  Cd Length: 134  Bit Score: 42.50  E-value: 4.64e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A      152 RLDHFNQVTPDVPRGRKYLED-LGFRVTEDIQDdegttYAAWMH--RKGTVHDTALTGGNGPRLHHVAFSTHEKHNIiqi 228
Cdd:cd08360   3 RLGHVLLFSPDVDRSVDFYRDlLGLKVSDRSFD-----IIAFMRgaAGSDHHLIAFAKSSATGLHHMSWDVSDVNEI--- 74

                        90       100       110
                ....*....|....*....|....*....|....*....
1F1X_A      229 cdKMGALRIsdrIERGP------GRHGVSNAFYLYILDP 261
Cdd:cd08360  75 --GIGASQL---LRAGYkdgwglGRHVLGSNYFHYVRDP 108
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 23-93 6.55e-05

C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. 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: 319964  Cd Length: 114  Bit Score: 41.77  E-value: 6.55e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1F1X_A       23 LVVTDLAKSRNFYVDVLGLHVSYEDENQIYLRSFEEFIHhnLVLtkgpvaalkamafrVRTPEDVDKAEAY 93
Cdd:cd16357   4 LAVSDLEKSIDYWSDLLGMKVFEKSEKSALLGYGEDQAK--LEL--------------VDIPEPVDHGTAF 58
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 153-268 1.65e-04

uncharacterized subfamily of 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 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: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 40.38  E-value: 1.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A      153 LDHFNQVTPDVPRGRKYLED-LGFRVTE--DIQDDEGttyaAWMH--RKGTVH-------DTALTGGNGPRLHHVAFSTH 220
Cdd:cd07245   1 LDHVALACPDLERARRFYTDvLGLEEVPrpPFLKFGG----AWLYlgGGQQIHlvveqnpSELPRPEHPGRDRHPSFSVP 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
1F1X_A      221 EKHNIIQICDKMGaLRISDRIERGPGRHGvsnafyLYILDPDNHRIEI 268
Cdd:cd07245  77 DLDALKQRLKEAG-IPYTESTSPGGGVTQ------LFFRDPDGNRLEF 117
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 19-273 3.58e-04

4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and metabolism, General function prediction only];


Pssm-ID: 442418 [Multi-domain]  Cd Length: 333  Bit Score: 41.80  E-value: 3.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A       19 AYAELVVTDLAKSRnFYVDVLGL-HVSYEDENQIYL-RSFEefIhhNLVLT---KGPVAA--------LKAMAFRVrtpE 85
Cdd:COG3185   5 EFVEFAVGDAEQLA-FLLEALGFtLVARHRSKAVTLyRQGD--I--NFVLNaepDSFAARfarehgpgVCAIAFRV---D 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A       86 DVDKAEAYYQELGCRTERRKDGF------VKGIGDAL-----RVEDPLGFPYEFFFETTHVERLHMRydlysageLVRLD 154
Cdd:COG3185  77 DAAAAYERALALGAEPFEGPGPGelripaIRGIGGSLhyfvdRYGYGGIYDPDFEPLPGDAAPAGAG--------LTRID 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A      155 HFNQVtpdVPRGR-----KYLED-LGFRVT--EDIQDDEG--TTYAAWmHRKGTVH---------DTA----LTGGNGPR 211
Cdd:COG3185 149 HIGIA---VPRGDldewvLFYEDvLGFEEIreEDIEDPYQgvRSAVLQ-SPDGKVRiplneptspDSQiaefLEKYRGEG 224

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1F1X_A      212 LHHVAFSThekHNIIQICDKMGA-----LRIS----DRIERGPGRHGVSNAF-----YLYILDPDNHRIEIYTQDY 273
Cdd:COG3185 225 IQHIAFAT---DDIEATVAALRArgvrfLDIPdnyyDDLEPRVGAHGEDVAFlhpkgILVDRDTGGVLLQIFTKPV 297
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 19-123 4.70e-04

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 39.23  E-value: 4.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A       19 AYAELVVTDLAKSRNFYVDVLGLHVSYEDENQIYLRSFEEFIHHNLVLTKGPVAALKAMA---FRVrtpEDVDKAEAYYQ 95
Cdd:COG3324   6 VWVELPVDDLERAKAFYEEVFGWTFEDDAGPGGDYAEFDTDGGQVGGLMPGAEEPGGPGWllyFAV---DDLDAAVARVE 82

                        90       100
                ....*....|....*....|....*...
1F1X_A       96 ELGCRTERRKDGfVKGIGDALRVEDPLG 123
Cdd:COG3324  83 AAGGTVLRPPTD-IPPWGRFAVFRDPEG 109
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 237-270 2.22e-03

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: 37.29  E-value: 2.22e-03
                        10        20        30
                ....*....|....*....|....*....|....
1F1X_A      237 ISDRIERGPGRHGVSNAFYLYilDPDNHRIEIYT 270
Cdd:cd07255  86 AEHGPLIGAADHGVSEAIYLS--DPEGNGIEIYA 117
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 19-98 2.45e-03

uncharacterized subfamily of 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 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: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 37.31  E-value: 2.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A       19 AYAELVVTDLAKSRNFYVDVLGLHVSYEDENQIY-----------LRSFEEfiHHNLVLTKGPVAALkAMAFRVrtpEDV 87
Cdd:cd07264   2 AYIVLYVDDFAASLRFYRDVLGLPPRFLHEEGEYaefdtgetklaLFSRKE--MARSGGPDRRGSAF-ELGFEV---DDV 75

                        90
                ....*....|.
1F1X_A       88 DKAEAYYQELG 98
Cdd:cd07264  76 EATVEELVERG 86
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 20-53 3.29e-03

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: 36.91  E-value: 3.29e-03
                        10        20        30
                ....*....|....*....|....*....|....
1F1X_A       20 YAELVVTDLAKSRNFYVDVLGLHVSYEDENQIYL 53
Cdd:cd07255   5 RVTLKVADLERQSAFYQNVIGLSVLKQNASRAYL 38
THT_oxygenase_C cd07257
The C-terminal domain of 2,4,5-trihydroxytoluene (THT) oxygenase; This subfamily contains the ...
 152-270 6.95e-03

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: 36.55  E-value: 6.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1F1X_A      152 RLDHFNQVTPDVPRGRK-YLEDLGFRVTEDIQDDEGTTYAAWMH-RKGTV----HDTALTGGNGPRLHHVAFSTHEKHNI 225
Cdd:cd07257   1 KLGHVGLEVNDFEATFDwYTKTFGLKPSDVIYLPDGKTVGSFLHlDRGSEyvdhHSFFFAQGPRPKVHHAAFEVHDFDSQ 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
1F1X_A      226 iqicdKMGALRISDR---IERGPGRHGVSNAFYLYILDPDNHRIEIYT 270
Cdd:cd07257  81 -----VLGHDWLREKgykHVWGVGRHILGSQIFDYWFDPSGFIVEHYT 123
 
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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