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Conserved domains on  [gi|170658146|gb|ACB27201|]
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Glyoxalase/bleomycin resistance protein/dioxygenase [Methylobacterium radiotolerans JCM 2831]

Protein Classification

VOC and VOC_BsCatE_like_C domain-containing protein( domain architecture ID 11675445)

VOC and VOC_BsCatE_like_C domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VOC super family cl14632
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 36-158 2.04e-45

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.


The actual alignment was detected with superfamily member cd07255:

Pssm-ID: 472697  Cd Length: 124  Bit Score: 150.15  E-value: 2.04e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146  36 RVGSVALVVRDLDGLARFYRDTLGLATISRKSDTLRLGV-GATVLLEL--RHDAAAQPWSpqRAGLFHTAFLLPSRGHLG 112
Cdd:cd07255    2 RIGRVTLKVADLERQSAFYQNVIGLSVLKQNASRAYLGVdGKQVLLVLeaIPDAVLAPRS--TTGLYHFAILLPDRKALG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 170658146 113 AWLAYAAERKIqLSGAADHLVSEAVYLTDPEGNGIEVYVDRPSSEW 158
Cdd:cd07255   80 RALAHLAEHGP-LIGAADHGVSEAIYLSDPEGNGIEIYADRPREQW 124
VOC_BsCatE_like_C cd16359
C-terminal of Bacillus subtilis CatE like protein, a vicinal oxygen chelate subfamily; ...
 196-304 2.87e-32

C-terminal of Bacillus subtilis CatE like protein, a vicinal oxygen chelate subfamily; Uncharacterized subfamily of vicinal oxygen chelate (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: 319966  Cd Length: 110  Bit Score: 115.54  E-value: 2.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146 196 GHVHLQVGALDTAERFYADLLGFDVMCRYPGATFLGAGGYHHQLATNIWNSRGAPVRPAGMAGLAEVELQI-DTGTLAKV 274
Cdd:cd16359    1 GHIHLRVSDLKAASHFYHQVLGFDIKSRRPGALFLSAGGYHHHIGLNTWAGRGLPLPPEDATGLAYFTIVLpDQEALAAI 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 170658146 275 RGRCLESGSAMTDDDGATVLHDPWGTRLRL 304
Cdd:cd16359   81 LERLDLAGYDVEALDDGLELTDPWGITVKF 110
 
Name Accession Description Interval E-value
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 36-158 2.04e-45

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: 150.15  E-value: 2.04e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146  36 RVGSVALVVRDLDGLARFYRDTLGLATISRKSDTLRLGV-GATVLLEL--RHDAAAQPWSpqRAGLFHTAFLLPSRGHLG 112
Cdd:cd07255    2 RIGRVTLKVADLERQSAFYQNVIGLSVLKQNASRAYLGVdGKQVLLVLeaIPDAVLAPRS--TTGLYHFAILLPDRKALG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 170658146 113 AWLAYAAERKIqLSGAADHLVSEAVYLTDPEGNGIEVYVDRPSSEW 158
Cdd:cd07255   80 RALAHLAEHGP-LIGAADHGVSEAIYLSDPEGNGIEIYADRPREQW 124
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
36-158 4.75e-37

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 128.92  E-value: 4.75e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146  36 RVGSVALVVRDLDGLARFYRDTLGLATISRKSDTLRLGV-GATVLLELRHDAAAQPwSPQRAGLFHTAFLLPSRGHLGAW 114
Cdd:COG2514    3 RLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRAdGGEHLLVLEEAPGAPP-RPGAAGLDHVAFRVPSRADLDAA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 170658146 115 LAYAAERKIQLSGAADHLVSEAVYLTDPEGNGIEVYVDRPSSEW 158
Cdd:COG2514   82 LARLAAAGVPVEGAVDHGVGESLYFRDPDGNLIELYTDRPRFEH 125
VOC_BsCatE_like_C cd16359
C-terminal of Bacillus subtilis CatE like protein, a vicinal oxygen chelate subfamily; ...
 196-304 2.87e-32

C-terminal of Bacillus subtilis CatE like protein, a vicinal oxygen chelate subfamily; Uncharacterized subfamily of vicinal oxygen chelate (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: 319966  Cd Length: 110  Bit Score: 115.54  E-value: 2.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146 196 GHVHLQVGALDTAERFYADLLGFDVMCRYPGATFLGAGGYHHQLATNIWNSRGAPVRPAGMAGLAEVELQI-DTGTLAKV 274
Cdd:cd16359    1 GHIHLRVSDLKAASHFYHQVLGFDIKSRRPGALFLSAGGYHHHIGLNTWAGRGLPLPPEDATGLAYFTIVLpDQEALAAI 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 170658146 275 RGRCLESGSAMTDDDGATVLHDPWGTRLRL 304
Cdd:cd16359   81 LERLDLAGYDVEALDDGLELTDPWGITVKF 110
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
194-305 4.66e-10

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 56.89  E-value: 4.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146 194 RVGHVHLQVGALDTAERFYADLLGFDVMCRYPGATFLGAGGYHHQLatNIWNSRGAPVRPAGmAGLAEVELQIDT-GTLA 272
Cdd:COG2514    3 RLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEHLL--VLEEAPGAPPRPGA-AGLDHVAFRVPSrADLD 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 170658146 273 KVRGRCLESG---SAMTDDDGATVL--HDPWGTRLRLV 305
Cdd:COG2514   80 AALARLAAAGvpvEGAVDHGVGESLyfRDPDGNLIELY 117
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
36-149 1.88e-08

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 51.68  E-value: 1.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146   36 RVGSVALVVRDLDGLARFYRDTLGLATISRKSDTLRLGVGATVL------LELRHDAAAQPwSPQRAGLFHTAFLLPSRG 109
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFlaggrvLELLLNETPPP-AAAGFGGHHIAFIAFSVD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 170658146  110 HLGAWLAYAAERKIQLSGAADHLVSE--AVYLTDPEGNGIEV 149
Cdd:pfam00903  80 DVDAAYDRLKAAGVEIVREPGRHGWGgrYSYFRDPDGNLIEL 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
194-304 1.48e-03

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 37.81  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146  194 RVGHVHLQVGALDTAERFYADLLGFDV-------MCRYPGATFLGAGGYHHQLATNiWNSRGAPVRP--AGMAGLAEVEL 264
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLveetdagEEGGLRSAFFLAGGRVLELLLN-ETPPPAAAGFggHHIAFIAFSVD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 170658146  265 QIDtGTLAKVR---GRCLESGSAMTDDDGATVLHDPWGTRLRL 304
Cdd:pfam00903  80 DVD-AAYDRLKaagVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 36-158 2.04e-45

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: 150.15  E-value: 2.04e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146  36 RVGSVALVVRDLDGLARFYRDTLGLATISRKSDTLRLGV-GATVLLEL--RHDAAAQPWSpqRAGLFHTAFLLPSRGHLG 112
Cdd:cd07255    2 RIGRVTLKVADLERQSAFYQNVIGLSVLKQNASRAYLGVdGKQVLLVLeaIPDAVLAPRS--TTGLYHFAILLPDRKALG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 170658146 113 AWLAYAAERKIqLSGAADHLVSEAVYLTDPEGNGIEVYVDRPSSEW 158
Cdd:cd07255   80 RALAHLAEHGP-LIGAADHGVSEAIYLSDPEGNGIEIYADRPREQW 124
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
36-158 4.75e-37

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 128.92  E-value: 4.75e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146  36 RVGSVALVVRDLDGLARFYRDTLGLATISRKSDTLRLGV-GATVLLELRHDAAAQPwSPQRAGLFHTAFLLPSRGHLGAW 114
Cdd:COG2514    3 RLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRAdGGEHLLVLEEAPGAPP-RPGAAGLDHVAFRVPSRADLDAA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 170658146 115 LAYAAERKIQLSGAADHLVSEAVYLTDPEGNGIEVYVDRPSSEW 158
Cdd:COG2514   82 LARLAAAGVPVEGAVDHGVGESLYFRDPDGNLIELYTDRPRFEH 125
VOC_BsCatE_like_C cd16359
C-terminal of Bacillus subtilis CatE like protein, a vicinal oxygen chelate subfamily; ...
 196-304 2.87e-32

C-terminal of Bacillus subtilis CatE like protein, a vicinal oxygen chelate subfamily; Uncharacterized subfamily of vicinal oxygen chelate (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: 319966  Cd Length: 110  Bit Score: 115.54  E-value: 2.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146 196 GHVHLQVGALDTAERFYADLLGFDVMCRYPGATFLGAGGYHHQLATNIWNSRGAPVRPAGMAGLAEVELQI-DTGTLAKV 274
Cdd:cd16359    1 GHIHLRVSDLKAASHFYHQVLGFDIKSRRPGALFLSAGGYHHHIGLNTWAGRGLPLPPEDATGLAYFTIVLpDQEALAAI 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 170658146 275 RGRCLESGSAMTDDDGATVLHDPWGTRLRL 304
Cdd:cd16359   81 LERLDLAGYDVEALDDGLELTDPWGITVKF 110
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 36-155 2.85e-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: 60.01  E-value: 2.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146  36 RVGSVALVVRDLDGLARFYRDTLGLATISR------KSDTLRLGVGATVLLELRHDAAAQPwSPQRAGLFHTAFLLPSrg 109
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRtdfgdgGFGHAFLRLGDGTELELFEAPGAAP-APGGGGLHHLAFRVDD-- 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 170658146 110 hLGAWLAYAAERKIQLSGA-ADHLVSE-AVYLTDPEGNGIEVYVDRPS 155
Cdd:COG0346   79 -LDAAYARLRAAGVEIEGEpRDRAYGYrSAYFRDPDGNLIELVEPPPG 125
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 39-149 7.09e-11

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: 58.31  E-value: 7.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146  39 SVALVVRDLDGLARFYRDTLGLATISRKSD----TLRLGVGATVLLelrhDAAAQPWSPQRAGLFHTAFLLPSRGHLGAW 114
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGggfaFLRLGPGLRLAL----LEGPEPERPGGGGLFHLAFEVDDVDEVDER 76

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 170658146 115 LAYAAERKIQLS-GAADHLVSEAVYLTDPEGNGIEV 149
Cdd:cd06587   77 LREAGAEGELVApPVDDPWGGRSFYFRDPDGNLIEF 112
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
194-305 4.66e-10

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 56.89  E-value: 4.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146 194 RVGHVHLQVGALDTAERFYADLLGFDVMCRYPGATFLGAGGYHHQLatNIWNSRGAPVRPAGmAGLAEVELQIDT-GTLA 272
Cdd:COG2514    3 RLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEHLL--VLEEAPGAPPRPGA-AGLDHVAFRVPSrADLD 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 170658146 273 KVRGRCLESG---SAMTDDDGATVL--HDPWGTRLRLV 305
Cdd:COG2514   80 AALARLAAAGvpvEGAVDHGVGESLyfRDPDGNLIELY 117
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
36-149 1.88e-08

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 51.68  E-value: 1.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146   36 RVGSVALVVRDLDGLARFYRDTLGLATISRKSDTLRLGVGATVL------LELRHDAAAQPwSPQRAGLFHTAFLLPSRG 109
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFlaggrvLELLLNETPPP-AAAGFGGHHIAFIAFSVD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 170658146  110 HLGAWLAYAAERKIQLSGAADHLVSE--AVYLTDPEGNGIEV 149
Cdd:pfam00903  80 DVDAAYDRLKAAGVEIVREPGRHGWGgrYSYFRDPDGNLIEL 121
BphC2-C3-RGP6_C_like cd08348
The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus ...
 86-153 3.29e-07

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: 48.67  E-value: 3.29e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170658146  86 AAAQPWSPQRAGLFHTAFLLPSRGHLGAWLAYAAERKIQLSGAADHLVSEAVYLTDPEGNGIEVYVDR 153
Cdd:cd08348   57 AQPPDKRPTRVGLAHIAFTYASLDDLARNYAQLKERGIKPVWPVNHGVTTSIYYRDPDGNMLEMQVDN 124
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 40-124 5.61e-06

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: 44.84  E-value: 5.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146  40 VALVVRDLDGLARFYRDTLGLATIS------RKSDTLRLGVGaTVLLEL--RHDAAAQPWSPQRAGLFHTAFLLPsrgHL 111
Cdd:cd08352    6 IAIICSDYEKSKDFYVDKLGFEIIRehyrpeRNDIKLDLALG-GYQLELfiKPDAPARPSYPEALGLRHLAFKVE---DV 81

                         90
                 ....*....|...
gi 170658146 112 GAWLAYAAERKIQ 124
Cdd:cd08352   82 EATVAELKSLGIE 94
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 38-160 1.27e-05

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: 43.84  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146  38 GSVALVVRDLDGLARFYRDTLGLatisRKSDTLRL-GVGATVLLELR-----HDAAAQPwsPQRAGLFHTAFLLPS---- 107
Cdd:cd08343    1 GHVVLCSPDVEASRDFYTDVLGF----RVSDRIVDpGVDGGAFLHCDrgtdhHTVALAG--GPHPGLHHVAFEVHDlddv 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 170658146 108 -RGHlgAWLAyAAERKIqLSGAADHLVSEAV--YLTDPEGNGIEVYVD--RPSSEWPR 160
Cdd:cd08343   75 gRGH--DRLR-EKGYKI-EWGPGRHGLGSQVfdYWFDPSGNRVEYYTDgdLVDDDWPP 128
PcpA_C_like cd08347
C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 36-154 3.34e-05

C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins; The C-terminal domain of Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins. PcpA is a key enzyme in the pentachlorophenol (PCP) degradation pathway, catalyzing the conversion of 2,6-dichloro-p-hydroquinone to 2-chloromaleylacetate. This domain 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.


Pssm-ID: 319935  Cd Length: 157  Bit Score: 43.39  E-value: 3.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146  36 RVGSVALVVRDLDGLARFYRDTLGLATISRKSDTLRL-----GVGATVLLELRHDAAAqpWSPQRAGLFHTAFLLPSRGH 110
Cdd:cd08347    1 GLHGVTLTVREPEETDAFLTNVFGFTEVGEEGDLVRLfaggnGSGGVVDVLDDPDLPS--AQQGYGTVHHVAFRVADDEE 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 170658146 111 LGAWLAYAAERKIQLSGAADHLVSEAVYLTDPEGNGIEVYVDRP 154
Cdd:cd08347   79 QAAWKERLEELGFDNSGIVDRFYFESLYFREPGGVLFEIATDGP 122
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 194-299 5.55e-05

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: 41.91  E-value: 5.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146 194 RVGHVHLQVGALDTAERFYADLLGFDVMCRYPGATFLGAGGyhHQLATNIWNSRGAPVRPAGMAGLAEVELQIDTGT-LA 272
Cdd:cd07255    2 RIGRVTLKVADLERQSAFYQNVIGLSVLKQNASRAYLGVDG--KQVLLVLEAIPDAVLAPRSTTGLYHFAILLPDRKaLG 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 170658146 273 KVRGRCLESGSAMTDDD----GATVLHDPWG 299
Cdd:cd07255   80 RALAHLAEHGPLIGAADhgvsEAIYLSDPEG 110
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 197-304 1.39e-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: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146 197 HVHLQVGALDTAERFYADLLGFDV--MCRYPGATFLGAGGyHHQLATNIWNSRGAPVRPaGMAGLA-EVELQIDTGTLAK 273
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVvsRNEGGGFAFLRLGP-GLRLALLEGPEPERPGGG-GLFHLAfEVDDVDEVDERLR 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 170658146 274 VRGRCLESGSAMTDDDGAT---VLHDPWGTRLRL 304
Cdd:cd06587   79 EAGAEGELVAPPVDDPWGGrsfYFRDPDGNLIEF 112
VOC_BsYyaH cd07241
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal ...
 40-149 1.23e-03

vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; 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: 319905  Cd Length: 125  Bit Score: 38.16  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146  40 VALVVRDLDGLARFYRDTLGlAT-----ISRKSDT----LRLGVGATVLLELRHDAAAQPWSPQRAGLFHTAFLLPSRGH 110
Cdd:cd07241    5 VALWTNDLERMKDFYVKYFG-AEsndiyHNKKKGFrsyfLTFDSGARLELMSRPDVTDPDKEVERTGLAHIAFSVGSKEA 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 170658146 111 LGAWLAYAAERKIQLSGAADHL---VSEAVYLtDPEGNGIEV 149
Cdd:cd07241   84 VDELTERLRADGYAVVGGPRTTgdgYYESVIL-DPEGNRIEI 124
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
194-304 1.48e-03

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 37.81  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146  194 RVGHVHLQVGALDTAERFYADLLGFDV-------MCRYPGATFLGAGGYHHQLATNiWNSRGAPVRP--AGMAGLAEVEL 264
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLveetdagEEGGLRSAFFLAGGRVLELLLN-ETPPPAAAGFggHHIAFIAFSVD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 170658146  265 QIDtGTLAKVR---GRCLESGSAMTDDDGATVLHDPWGTRLRL 304
Cdd:pfam00903  80 DVD-AAYDRLKaagVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 194-305 1.96e-03

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: 37.66  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146 194 RVGHVHLQVGALDTAERFYADLLGFDVMCRYP------GATFLGAGGyHHQLATNIWNSRGAPVRPAGMAGLAevelqID 267
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDfgdggfGHAFLRLGD-GTELELFEAPGAAPAPGGGGLHHLA-----FR 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 170658146 268 TGTLAKVRGRCLESGSAMTDDDG-------ATVLHDPWGTRLRLV 305
Cdd:COG0346   76 VDDLDAAYARLRAAGVEIEGEPRdraygyrSAYFRDPDGNLIELV 120
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 41-149 2.70e-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: 319942  Cd Length: 122  Bit Score: 36.96  E-value: 2.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146  41 ALVVRDLDGLARFYRDTLGLATISR--KSDTLRLGVGATVLLELRHDAAAQPWSP----QRAGLFHTAFLLPSRgHLGAW 114
Cdd:cd08354    5 CLYADDLDAAEAFYEDVLGLKPMLRsgRHAFFRLGPQVLLVFDPGATSKDVRTGEvpghGASGHGHFAFAVPTE-ELAAW 83

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 170658146 115 LAYAAERKIQLSGAADHLV-SEAVYLTDPEGNGIEV 149
Cdd:cd08354   84 EARLEAKGVPIESYTQWPEgGKSLYFRDPAGNLVEL 119
THT_oxygenase_C cd07257
The C-terminal domain of 2,4,5-trihydroxytoluene (THT) oxygenase; This subfamily contains the ...
 36-152 3.00e-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: 37.70  E-value: 3.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146  36 RVGSVALVVRDLDGLARFYRDTLGLatisRKSDTLRLGVGATVLLELRHDAAAQP--------WSPQRAGLFHTAF---- 103
Cdd:cd07257    1 KLGHVGLEVNDFEATFDWYTKTFGL----KPSDVIYLPDGKTVGSFLHLDRGSEYvdhhsfffAQGPRPKVHHAAFevhd 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 170658146 104 ---------LLPSRGHLGAWlayaaerkiqlsGAADHLVSEAV--YLTDPEGNGIEVYVD 152
Cdd:cd07257   77 fdsqvlghdWLREKGYKHVW------------GVGRHILGSQIfdYWFDPSGFIVEHYTD 124
 
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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