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Conserved domains on  [gi|616919741|gb|KAH10781|]
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hypothetical protein W800_02109 [Staphylococcus aureus VET1779S]

Protein Classification

VOC family protein( domain architecture ID 50733)

vicinal oxygen chelate (VOC) family protein uses a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms

CATH:  3.10.180.10
Gene Ontology:  GO:0046872|GO:0003824
PubMed:  21820381|11076500

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 ...
 9-132 1.93e-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: 149.00  E-value: 1.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741   9 TQVTNIELNVRDLDLMTTFYKNILGLPVKSSDDNTTVLSVGTGGHTLTLHLLEDGRQTSPREAGLFHIAFLLPTTEDLAN 88
Cdd:cd07255    1 TRIGRVTLKVADLERQSAFYQNVIGLSVLKQNASRAYLGVDGKQVLLVLEAIPDAVLAPRSTTGLYHFAILLPDRKALGR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 616919741  89 FLYFVAQKNMGIGAGDHLVSEALYFNDPEGNGIEVYRDRPSSSW 132
Cdd:cd07255   81 ALAHLAEHGPLIGAADHGVSEAIYLSDPEGNGIEIYADRPREQW 124
VOC super family cl14632
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 170-243 1.21e-18

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 cd16359:

Pssm-ID: 472697  Cd Length: 110  Bit Score: 78.95  E-value: 1.21e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616919741 170 GHLHLKTHDLDAAYQCYIEQLGFQHVSDFPRALFMSTNHYHHHIAANTWQSNQARQNNAQSYGLTHVDIYQPDA 243
Cdd:cd16359    1 GHIHLRVSDLKAASHFYHQVLGFDIKSRRPGALFLSAGGYHHHIGLNTWAGRGLPLPPEDATGLAYFTIVLPDQ 74
 
Name Accession Description Interval E-value
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 9-132 1.93e-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: 149.00  E-value: 1.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741   9 TQVTNIELNVRDLDLMTTFYKNILGLPVKSSDDNTTVLSVGTGGHTLTLHLLEDGRQTSPREAGLFHIAFLLPTTEDLAN 88
Cdd:cd07255    1 TRIGRVTLKVADLERQSAFYQNVIGLSVLKQNASRAYLGVDGKQVLLVLEAIPDAVLAPRSTTGLYHFAILLPDRKALGR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 616919741  89 FLYFVAQKNMGIGAGDHLVSEALYFNDPEGNGIEVYRDRPSSSW 132
Cdd:cd07255   81 ALAHLAEHGPLIGAADHGVSEAIYLSDPEGNGIEIYADRPREQW 124
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
9-144 5.70e-37

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 127.77  E-value: 5.70e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741   9 TQVTNIELNVRDLDLMTTFYKNILGLPVKSSDDNTTVLSVGTGGHTLTLHLLEDGRQtSPREAGLFHIAFLLPTTEDLAN 88
Cdd:COG2514    2 TRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEHLLVLEEAPGAPP-RPGAAGLDHVAFRVPSRADLDA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 616919741  89 FLYFVAQKNMGI-GAGDHLVSEALYFNDPEGNGIEVYRDRPSSSWEwqnGKVKMDTL 144
Cdd:COG2514   81 ALARLAAAGVPVeGAVDHGVGESLYFRDPDGNLIELYTDRPRFEHV---GDLETDVL 134
VOC_BsCatE_like_C cd16359
C-terminal of Bacillus subtilis CatE like protein, a vicinal oxygen chelate subfamily; ...
 170-243 1.21e-18

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: 78.95  E-value: 1.21e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616919741 170 GHLHLKTHDLDAAYQCYIEQLGFQHVSDFPRALFMSTNHYHHHIAANTWQSNQARQNNAQSYGLTHVDIYQPDA 243
Cdd:cd16359    1 GHIHLRVSDLKAASHFYHQVLGFDIKSRRPGALFLSAGGYHHHIGLNTWAGRGLPLPPEDATGLAYFTIVLPDQ 74
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
14-123 1.13e-08

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 52.07  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741   14 IELNVRDLDLMTTFYKNILGLPVKSSDDN-------TTVLSVGTGGHTLTlhlLEDGRQTSPREAGLFHIAFLLPTTEDL 86
Cdd:pfam00903   5 VALRVGDLEKSLDFYTDVLGFKLVEETDAgeegglrSAFFLAGGRVLELL---LNETPPPAAAGFGGHHIAFIAFSVDDV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 616919741   87 ANFLYFVAQKNMGI--GAGDHLVSE-ALYFNDPEGNGIEV 123
Cdd:pfam00903  82 DAAYDRLKAAGVEIvrEPGRHGWGGrYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 9-132 1.93e-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: 149.00  E-value: 1.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741   9 TQVTNIELNVRDLDLMTTFYKNILGLPVKSSDDNTTVLSVGTGGHTLTLHLLEDGRQTSPREAGLFHIAFLLPTTEDLAN 88
Cdd:cd07255    1 TRIGRVTLKVADLERQSAFYQNVIGLSVLKQNASRAYLGVDGKQVLLVLEAIPDAVLAPRSTTGLYHFAILLPDRKALGR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 616919741  89 FLYFVAQKNMGIGAGDHLVSEALYFNDPEGNGIEVYRDRPSSSW 132
Cdd:cd07255   81 ALAHLAEHGPLIGAADHGVSEAIYLSDPEGNGIEIYADRPREQW 124
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
9-144 5.70e-37

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 127.77  E-value: 5.70e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741   9 TQVTNIELNVRDLDLMTTFYKNILGLPVKSSDDNTTVLSVGTGGHTLTLHLLEDGRQtSPREAGLFHIAFLLPTTEDLAN 88
Cdd:COG2514    2 TRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEHLLVLEEAPGAPP-RPGAAGLDHVAFRVPSRADLDA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 616919741  89 FLYFVAQKNMGI-GAGDHLVSEALYFNDPEGNGIEVYRDRPSSSWEwqnGKVKMDTL 144
Cdd:COG2514   81 ALARLAAAGVPVeGAVDHGVGESLYFRDPDGNLIELYTDRPRFEHV---GDLETDVL 134
VOC_BsCatE_like_C cd16359
C-terminal of Bacillus subtilis CatE like protein, a vicinal oxygen chelate subfamily; ...
 170-243 1.21e-18

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: 78.95  E-value: 1.21e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616919741 170 GHLHLKTHDLDAAYQCYIEQLGFQHVSDFPRALFMSTNHYHHHIAANTWQSNQARQNNAQSYGLTHVDIYQPDA 243
Cdd:cd16359    1 GHIHLRVSDLKAASHFYHQVLGFDIKSRRPGALFLSAGGYHHHIGLNTWAGRGLPLPPEDATGLAYFTIVLPDQ 74
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 14-123 2.47e-12

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: 62.16  E-value: 2.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741  14 IELNVRDLDLMTTFYKNILGLPVKSSDDNTTVLSVGTGGHTlTLHLLEDGRQTSPREAGLFHIAFLLPTTEDLANFLYFV 93
Cdd:cd06587    2 VALRVPDLDASVAFYEEVLGFEVVSRNEGGGFAFLRLGPGL-RLALLEGPEPERPGGGGLFHLAFEVDDVDEVDERLREA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 616919741  94 AQKNMGIGAGDHLV--SEALYFNDPEGNGIEV 123
Cdd:cd06587   81 GAEGELVAPPVDDPwgGRSFYFRDPDGNLIEF 112
BphC2-C3-RGP6_C_like cd08348
The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus ...
 21-127 1.46e-10

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: 57.92  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741  21 LDLMTTFYKNILGLPVKSSDDNTTVLSVGTGGHTLTLHLLEDGRQTSPRE---AGLFHIAFLLPTTEDLA-NFLYFVAQK 96
Cdd:cd08348   14 FEAMVQWYLDILGARIVARNAKGCFLSFDEEHHRIAIFGAPGGAQPPDKRptrVGLAHIAFTYASLDDLArNYAQLKERG 93

                         90       100       110
                 ....*....|....*....|....*....|.
gi 616919741  97 NMGIGAGDHLVSEALYFNDPEGNGIEVYRDR 127
Cdd:cd08348   94 IKPVWPVNHGVTTSIYYRDPDGNMLEMQVDN 124
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 14-129 1.58e-09

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


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 54.61  E-value: 1.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741  14 IELNVRDLDLMTTFYKNILGLPVK----SSDDNTTVLSVGTGGHTlTLHLLE-DGRQTSPREAGLFHIAFllpTTEDLAN 88
Cdd:COG0346    6 VTLRVSDLEASLAFYTDVLGLELVkrtdFGDGGFGHAFLRLGDGT-ELELFEaPGAAPAPGGGGLHHLAF---RVDDLDA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 616919741  89 FLYFVAQKNMGI--GAGDHLVSE-ALYFNDPEGNGIEVYRDRPS 129
Cdd:COG0346   82 AYARLRAAGVEIegEPRDRAYGYrSAYFRDPDGNLIELVEPPPG 125
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
14-123 1.13e-08

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 52.07  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741   14 IELNVRDLDLMTTFYKNILGLPVKSSDDN-------TTVLSVGTGGHTLTlhlLEDGRQTSPREAGLFHIAFLLPTTEDL 86
Cdd:pfam00903   5 VALRVGDLEKSLDFYTDVLGFKLVEETDAgeegglrSAFFLAGGRVLELL---LNETPPPAAAGFGGHHIAFIAFSVDDV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 616919741   87 ANFLYFVAQKNMGI--GAGDHLVSE-ALYFNDPEGNGIEV 123
Cdd:pfam00903  82 DAAYDRLKAAGVEIvrEPGRHGWGGrYSYFRDPDGNLIEL 121
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 12-124 5.18e-06

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: 44.63  E-value: 5.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741  12 TNIELNVRDLDLMTTFYKNILGLPVKSSDDNTTVLSVGTGGHTLTL-------HLLEDGRQTSPREaglfhIAFllpTTE 84
Cdd:cd07264    2 AYIVLYVDDFAASLRFYRDVLGLPPRFLHEEGEYAEFDTGETKLALfsrkemaRSGGPDRRGSAFE-----LGF---EVD 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 616919741  85 DL-ANFLYFVAqknmgigAGDHLVSE---------ALYFNDPEGNGIEVY 124
Cdd:cd07264   74 DVeATVEELVE-------RGAEFVREpankpwgqtVAYVRDPDGNLIEIC 116
PcpA_C_like cd08347
C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 14-128 2.33e-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: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741  14 IELNVRDLDLMTTFYKNILGLPVKSSDDNTTVLSVGTGGHTLTLHLLEDGRQTSPREA--GLFHIAFLLPTTEDLAnfly 91
Cdd:cd08347    5 VTLTVREPEETDAFLTNVFGFTEVGEEGDLVRLFAGGNGSGGVVDVLDDPDLPSAQQGygTVHHVAFRVADDEEQA---- 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 616919741  92 FVAQKNMGIGAG-----DHLVSEALYFNDPEGNGIEVYRDRP 128
Cdd:cd08347   81 AWKERLEELGFDnsgivDRFYFESLYFREPGGVLFEIATDGP 122
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 16-123 3.24e-05

Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily of VOC family contains human glyoxalase domain-containing protein 5 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: 319916 [Multi-domain]  Cd Length: 123  Bit Score: 42.60  E-value: 3.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741  16 LNVRDLDLMTTFYKNILGLPVKSSDDNTTVLSVGTGG---HTLTLHLLEDGRQTSPreaGLFHIAFLlpTTEDLANFLYF 92
Cdd:cd07253    9 LTVKDIERTIDFYTKVLGMTVVTFKEGRKALRFGNQKinlHQKGKEFEPKASAPTP---GSADLCFI--TETPIDEVLEH 83

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 616919741  93 VAQKNMGI--------GAGDHLVSeaLYFNDPEGNGIEV 123
Cdd:cd07253   84 LEACGVTIeegpvkrtGALGPILS--IYFRDPDGNLIEL 120
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 14-124 7.04e-05

Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. The three types of fosfomycin resistance proteins, employ different mechanisms to render fosfomycin [(1R,2S)-epoxypropylphosphonic acid] inactive. FosB catalyzes the addition of L-cysteine to the epoxide ring of fosfomycin. FosX catalyzes the addition of a water molecule to the C1 position of the antibiotic with inversion of configuration at C1. FosA catalyzes the addition of glutathione to the antibiotic fosfomycin, making it inactive. Catalytic activities of both FosX and FosA are Mn(II)-dependent, but FosB is activated by Mg(II). Fosfomycin resistant proteins are evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319933  Cd Length: 118  Bit Score: 41.39  E-value: 7.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741  14 IELNVRDLDLMTTFYKNILG-LPVKSSDDNTTVLSVGT----GGHTLTLHlledgRQTSPREAGLFHIAFLLpTTEDLAN 88
Cdd:cd08345    2 ITLIVRDLEKSTAFLQDIFGaREVYSSGDKTFSLSKEKffllGGLWIALM-----EGESLQERSYTHIAFQI-QSEDFDR 75

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 616919741  89 FLYFVAQKNMGIGAGDHLVS---EALYFNDPEGNGIEVY 124
Cdd:cd08345   76 YAERLGALGVEMRPPRPRVEgegRSIYFYDPDNHLFELH 114
HPCD_N_class_II cd07266
N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 15-124 7.59e-05

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: 41.24  E-value: 7.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741  15 ELNVRDLDLMTTFYKNILGLPVKSSDDNTTVLSV--GTGGHTLTLhlledgrqTSPREAGLFHIAFLLPTTEDLANFLYF 92
Cdd:cd07266    9 ELVVTDLAASREFYVDTLGLHVTDEDDNAIYLRGveEFIHHTLVL--------RKAPEAAVGHLGFRVRDEADLDKAAAF 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 616919741  93 VAQKNM--------GIGagdhlvsEALYFNDPEGNGIEVY 124
Cdd:cd07266   81 YKELGLptewreepGQG-------RTLRVEDPFGFPIEFY 113
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 16-123 1.61e-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: 319942  Cd Length: 122  Bit Score: 40.43  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741  16 LNVRDLDLMTTFYKNILGLPVKSSDDNTTVLSVGTGghtlTLHLLeDGRQTSPREA----------GLFHIAFLLPtTED 85
Cdd:cd08354    6 LYADDLDAAEAFYEDVLGLKPMLRSGRHAFFRLGPQ----VLLVF-DPGATSKDVRtgevpghgasGHGHFAFAVP-TEE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 616919741  86 LANFLYFVAQKNMGI------GAGdhlvSEALYFNDPEGNGIEV 123
Cdd:cd08354   80 LAAWEARLEAKGVPIesytqwPEG----GKSLYFRDPAGNLVEL 119
BphC-JF8_N_like cd09013
N-terminal, non-catalytic, domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 10-126 6.32e-04

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: 38.87  E-value: 6.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741  10 QVTNIELNVRDLDLMTTFYKNILGLPVKSSDDNTTVLSvGTGG---HTLTLhlledgrqTSPREAGLFHIAFLLPTTEDL 86
Cdd:cd09013    6 QLAHVELLTPKPEESLWFFTDVLGLEETHREGQSVYLR-AWGDwehHTLKL--------TESPEAGLGHIAWRASSPEAL 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 616919741  87 ANFLYFVAQKNMGIG--AGDHLVSEALYFNDPEGNGIEVYRD 126
Cdd:cd09013   77 ERRVAALEASGVGIGwiDGDLGQGPAYRFQSPDGHPMEIYWE 118
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 14-123 6.91e-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: 38.45  E-value: 6.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741  14 IELNVRDLDLMTTFYKNILGL---PVKSSDDNTTV-LSVGTGGHtltLHLLE----DGRQTSPREAGLFHIAFLLPTTED 85
Cdd:cd07245    4 VALACPDLERARRFYTDVLGLeevPRPPFLKFGGAwLYLGGGQQ---IHLVVeqnpSELPRPEHPGRDRHPSFSVPDLDA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 616919741  86 LANFLY-----FVAQKNMGIGAgdhlvsEALYFNDPEGNGIEV 123
Cdd:cd07245   81 LKQRLKeagipYTESTSPGGGV------TQLFFRDPDGNRLEF 117
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 8-128 1.05e-03

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 38.08  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741   8 ATQVTNIELNVRDLDLMTTFYKNILGLPVKSSDDNT---TVLSVGtGGHTLTLHlledGRQTSPREAGlFHIAFllpTTE 84
Cdd:COG3324    2 PGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPGgdyAEFDTD-GGQVGGLM----PGAEEPGGPG-WLLYF---AVD 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 616919741  85 DLANFLYFVAQknmgigAGDHLVSEA---------LYFNDPEGNGIEVYRDRP 128
Cdd:COG3324   73 DLDAAVARVEA------AGGTVLRPPtdippwgrfAVFRDPEGNRFGLWQPAA 119
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 13-84 1.26e-03

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: 37.54  E-value: 1.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616919741  13 NIELNVRDLDLMTTFYKNILGLPVKSSDDNTTVLSVGTGGHTLTLHLLEDGRqtsPREAGLFHIAFLLPTTE 84
Cdd:cd16357    1 KVSLAVSDLEKSIDYWSDLLGMKVFEKSEKSALLGYGEDQAKLELVDIPEPV---DHGTAFGRIAFSCPADE 69
VOC_BsCatE_like_C cd16359
C-terminal of Bacillus subtilis CatE like protein, a vicinal oxygen chelate subfamily; ...
 14-123 1.87e-03

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: 36.96  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741  14 IELNVRDLDLMTTFYKNILGLPVKSSDDNTTVLSVGTGGHTLTLHLLEDGRQTSPRE--AGLFHIAFLLPTTEDLANFLY 91
Cdd:cd16359    3 IHLRVSDLKAASHFYHQVLGFDIKSRRPGALFLSAGGYHHHIGLNTWAGRGLPLPPEdaTGLAYFTIVLPDQEALAAILE 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 616919741  92 FVAQKNMGIGAGDHlvseALYFNDPEGNGIEV 123
Cdd:cd16359   83 RLDLAGYDVEALDD----GLELTDPWGITVKF 110
HPCD_C_class_II cd07256
C-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 66-136 4.48e-03

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: 37.10  E-value: 4.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741  66 TSPReagLFHIAFLLPTTEDLANFLYFVA----QKNMGIGAGDHLVSEA--LYFNDPEGNGIEVY--------RDRPSSS 131
Cdd:cd07256   59 NGPR---LHHVAFWVPEPHNIIQTCDLMAaarySDRIERGPGRHGVSNAffLYILDPDGHRIEIYtsdyytvdPDNPPIK 135


                 ....*
gi 616919741 132 WEWQN 136
Cdd:cd07256  136 WDVHD 140
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 16-126 6.87e-03

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: 35.76  E-value: 6.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616919741  16 LNVRDLDLMTTFYKNILGLPVksSDDNttVLSVGTGGHTLTLHLLEDGRQ---TSPREAGLFHIAFLLPTTEDLANFLYF 92
Cdd:cd08343    5 LCSPDVEASRDFYTDVLGFRV--SDRI--VDPGVDGGAFLHCDRGTDHHTvalAGGPHPGLHHVAFEVHDLDDVGRGHDR 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 616919741  93 VAQK--NMGIGAGDHLVSEA--LYFNDPEGNGIEVYRD 126
Cdd:cd08343   81 LREKgyKIEWGPGRHGLGSQvfDYWFDPSGNRVEYYTD 118
 
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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