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Conserved domains on  [gi|495463412|ref|WP_008188104|]
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MULTISPECIES: VOC family protein [Moorena]

Protein Classification

VOC family protein( domain architecture ID 10001243)

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
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 18-152 9.65e-20

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: 79.27  E-value: 9.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  18 RRVHHIALNVKDIQASRHFYGTLLGLHELTGEEVPSTLRSLVEagkvtnFVTPDGIVVDLFSEPDLSPPDPDphrgfTRV 97
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAF------LRLGDGTELELFEAPGAAPAPGG-----GGL 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495463412  98 NHLAFDIDPqlFDQAVEVLKQNQIPIDHGPVTRPTG-RGIYFYDPDGFIVEIRCDP 152
Cdd:COG0346   70 HHLAFRVDD--LDAAYARLRAAGVEIEGEPRDRAYGyRSAYFRDPDGNLIELVEPP 123
 
Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 18-152 9.65e-20

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: 79.27  E-value: 9.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  18 RRVHHIALNVKDIQASRHFYGTLLGLHELTGEEVPSTLRSLVEagkvtnFVTPDGIVVDLFSEPDLSPPDPDphrgfTRV 97
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAF------LRLGDGTELELFEAPGAAPAPGG-----GGL 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495463412  98 NHLAFDIDPqlFDQAVEVLKQNQIPIDHGPVTRPTG-RGIYFYDPDGFIVEIRCDP 152
Cdd:COG0346   70 HHLAFRVDD--LDAAYARLRAAGVEIEGEPRDRAYGyRSAYFRDPDGNLIELVEPP 123
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 22-148 1.32e-15

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: 68.32  E-value: 1.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  22 HIALNVKDIQASRHFYGTLLGLHELtgeevpstlrSLVEAGKVTNFVTPDGIVVDLFSEPDLSPpdpdphRGFTRVNHLA 101
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVV----------SRNEGGGFAFLRLGPGLRLALLEGPEPER------PGGGGLFHLA 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 495463412 102 FDI-DPQLFDQAVEVLKQNQIPIDHGPVTRPTGRGIYFYDPDGFIVEI 148
Cdd:cd06587   65 FEVdDVDEVDERLREAGAEGELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
19-148 2.08e-14

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 65.16  E-value: 2.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412   19 RVHHIALNVKDIQASRHFYGTLLGLHELTGEEVPstlrslVEAGKVTNFVTPDGIVVDLFSEPDLSPPDPDPHRGFTRvn 98
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAG------EEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIA-- 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 495463412   99 HLAFDIDPqlFDQAVEVLKQNQIPIDHGPVTRPTGRG-IYFYDPDGFIVEI 148
Cdd:pfam00903  73 FIAFSVDD--VDAAYDRLKAAGVEIVREPGRHGWGGRySYFRDPDGNLIEL 121
PRK11478 PRK11478
VOC family protein;
17-148 1.04e-06

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 45.27  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  17 LRRVHHIALNVKDIQASRHFYGTLLG---LHELTGEEVPSTLRSLVEAGKVtnfvtpdgiVVDLFSEPDLSPPDPDPHRG 93
Cdd:PRK11478   4 LKQVHHIAIIATDYAVSKAFYCDILGftlQSEVYREARDSWKGDLALNGQY---------VIELFSFPFPPERPSRPEAC 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495463412  94 FTRvnHLAFDIDPqlFDQAVEVLKQNQI---PIDHGPVTRPtgRGIYFYDPDGFIVEI 148
Cdd:PRK11478  75 GLR--HLAFSVDD--IDAAVAHLESHNVkceAIRVDPYTQK--RFTFFNDPDGLPLEL 126
catechol_2_3 TIGR03211
catechol 2,3 dioxygenase; Members of this family all are enzymes active as catechol 2,3 ...
 96-147 1.19e-03

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: 37.99  E-value: 1.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 495463412   96 RVNHLAFDID-PQLFDQAVEVLKQNQIPIDHGP----VTRptGRGIYFYDPDGFIVE 147
Cdd:TIGR03211 207 KLHHVSFFLDsWEDVLKAADVMSKNDVSIDIGPtrhgITR--GQTIYFFDPSGNRNE 261
 
Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 18-152 9.65e-20

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: 79.27  E-value: 9.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  18 RRVHHIALNVKDIQASRHFYGTLLGLHELTGEEVPSTLRSLVEagkvtnFVTPDGIVVDLFSEPDLSPPDPDphrgfTRV 97
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAF------LRLGDGTELELFEAPGAAPAPGG-----GGL 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495463412  98 NHLAFDIDPqlFDQAVEVLKQNQIPIDHGPVTRPTG-RGIYFYDPDGFIVEIRCDP 152
Cdd:COG0346   70 HHLAFRVDD--LDAAYARLRAAGVEIEGEPRDRAYGyRSAYFRDPDGNLIELVEPP 123
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
17-152 6.71e-19

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 77.31  E-value: 6.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  17 LRRVHHIALNVKDIQASRHFYGTLLGLHELTGEEVPSTLRSLVEAGKVTNFVTPDGIvvdlfsepdlsppdpdPHRGFTR 96
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEHLLVLEEAPGAP----------------PRPGAAG 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495463412  97 VNHLAFDI-DPQLFDQAVEVLKQNQIPIDhGPVTRPTGRGIYFYDPDGFIVEIRCDP 152
Cdd:COG2514   65 LDHVAFRVpSRADLDAALARLAAAGVPVE-GAVDHGVGESLYFRDPDGNLIELYTDR 120
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 22-148 1.32e-15

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: 68.32  E-value: 1.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  22 HIALNVKDIQASRHFYGTLLGLHELtgeevpstlrSLVEAGKVTNFVTPDGIVVDLFSEPDLSPpdpdphRGFTRVNHLA 101
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVV----------SRNEGGGFAFLRLGPGLRLALLEGPEPER------PGGGGLFHLA 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 495463412 102 FDI-DPQLFDQAVEVLKQNQIPIDHGPVTRPTGRGIYFYDPDGFIVEI 148
Cdd:cd06587   65 FEVdDVDEVDERLREAGAEGELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
19-148 2.08e-14

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 65.16  E-value: 2.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412   19 RVHHIALNVKDIQASRHFYGTLLGLHELTGEEVPstlrslVEAGKVTNFVTPDGIVVDLFSEPDLSPPDPDPHRGFTRvn 98
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAG------EEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIA-- 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 495463412   99 HLAFDIDPqlFDQAVEVLKQNQIPIDHGPVTRPTGRG-IYFYDPDGFIVEI 148
Cdd:pfam00903  73 FIAFSVDD--VDAAYDRLKAAGVEIVREPGRHGWGGRySYFRDPDGNLIEL 121
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 18-148 1.05e-09

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: 52.93  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  18 RRVHHIALNVKDIQASRHFYGTLLGLhELTGEevpsTLRSLVEAGKVTnfVTPDGIVVDLFS-EPDLSPPDPDPHRGFtr 96
Cdd:cd08352    1 KKIHHIAIICSDYEKSKDFYVDKLGF-EIIRE----HYRPERNDIKLD--LALGGYQLELFIkPDAPARPSYPEALGL-- 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495463412  97 vNHLAF---DIdpqlfDQAVEVLKQNQIPIDHGPVTRPTGRGI-YFYDPDGFIVEI 148
Cdd:cd08352   72 -RHLAFkveDV-----EATVAELKSLGIETEPIRVDDFTGKKFtFFFDPDGLPLEL 121
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 20-148 4.52e-08

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: 48.47  E-value: 4.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  20 VHHIALNVKDIQASRHFYGTLLGLheltgEEVPstlRSLVEAGKVTNFVTPDGIVVDLFSEPDLSPPDPDPHRGftRVNH 99
Cdd:cd07245    1 LDHVALACPDLERARRFYTDVLGL-----EEVP---RPPFLKFGGAWLYLGGGQQIHLVVEQNPSELPRPEHPG--RDRH 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495463412 100 LAFDIDPqlFDQAVEVLKQNQIPI--DHGPVTRPTgrGIYFYDPDGFIVEI 148
Cdd:cd07245   71 PSFSVPD--LDALKQRLKEAGIPYteSTSPGGGVT--QLFFRDPDGNRLEF 117
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 17-149 1.80e-07

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: 47.22  E-value: 1.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  17 LRRVHHIALNVKDIQASRHFYGTLLGLHELTGEEVPSTLR------SLVEAGKvtNFVTPDgivvdlfsepdlsppdpdp 90
Cdd:cd07253    1 IKRLDHLVLTVKDIERTIDFYTKVLGMTVVTFKEGRKALRfgnqkiNLHQKGK--EFEPKA------------------- 59

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495463412  91 HRGFTRVNHLAFDIDPQLfDQAVEVLKQNQIPIDHGPVTRPTGRG----IYFYDPDGFIVEIR 149
Cdd:cd07253   60 SAPTPGSADLCFITETPI-DEVLEHLEACGVTIEEGPVKRTGALGpilsIYFRDPDGNLIELS 121
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 20-148 2.94e-07

fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin resistant protein. FosB is a Mg(2+)-dependent L-cysteine thiol transferase. Fosfomycin inhibits the enzyme UDP-nacetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosB catalyzes the Mg(II) dependent addition of L-cysteine to the epoxide ring of fosfomycin, (1R,2S)-epoxypropylphosphonic acid, rendering it inactive. FosB is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319951 [Multi-domain]  Cd Length: 131  Bit Score: 46.58  E-value: 2.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  20 VHHIALNVKDIQASRHFYGTLLglheltgeevpstLRSLVEAGKVTNFVTPDGIVVDLFSEPDLSPPDPdpHRGFTrvnH 99
Cdd:cd08363    1 INHITFSVSNLNKSIAFYKDVL-------------DAKLLVLGEKTAYFDLNGLWLALNVQEDIPRNEI--SHSYT---H 62

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495463412 100 LAFDIDPQLFDQAVEVLKQNQIPIDHGpvtRP----TGRGIYFYDPDGFIVEI 148
Cdd:cd08363   63 IAFSIDEEDLDAFKERLKDNGVNILEG---RKrdilEGQSIYFTDPDGHLFEL 112
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 22-151 7.97e-07

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: 45.39  E-value: 7.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  22 HIALNVKDIQASRHFYGTLLGLheltgeevpstlrslveagKVTNFVTPDGIVVDLFsepDLSPPDPDPHRGF------T 95
Cdd:cd08343    2 HVVLCSPDVEASRDFYTDVLGF-------------------RVSDRIVDPGVDGGAF---LHCDRGTDHHTVAlaggphP 59

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495463412  96 RVNHLAF---DIDPQLfdQAVEVLKQNQIPIDHGPVTRPTGRGIYFY--DPDGFIVEIRCD 151
Cdd:cd08343   60 GLHHVAFevhDLDDVG--RGHDRLREKGYKIEWGPGRHGLGSQVFDYwfDPSGNRVEYYTD 118
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 19-148 8.33e-07

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 45.21  E-value: 8.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  19 RVHHIALNVKDIQASRHFYgTLLGLheltgeevpsTLRSLVEAGKVTNFVTPDGIVVDLFSEPD---LSPPDPDPHRGFT 95
Cdd:COG3607    3 RIIFVNLPVADLERSRAFY-EALGF----------TFNPQFSDEGAACFVLGEGIVLMLLPREKfatFTGKPIADATGFT 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495463412  96 RVnHLAF------DIDpQLFDQAVE----VLKQnqiPIDHGPvtrptGRGIYFYDPDGFIVEI 148
Cdd:COG3607   72 EV-LLALnvesreEVD-ALVAKALAaggtVLKP---PQDVGG-----MYSGYFADPDGHLWEV 124
PRK11478 PRK11478
VOC family protein;
17-148 1.04e-06

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 45.27  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  17 LRRVHHIALNVKDIQASRHFYGTLLG---LHELTGEEVPSTLRSLVEAGKVtnfvtpdgiVVDLFSEPDLSPPDPDPHRG 93
Cdd:PRK11478   4 LKQVHHIAIIATDYAVSKAFYCDILGftlQSEVYREARDSWKGDLALNGQY---------VIELFSFPFPPERPSRPEAC 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495463412  94 FTRvnHLAFDIDPqlFDQAVEVLKQNQI---PIDHGPVTRPtgRGIYFYDPDGFIVEI 148
Cdd:PRK11478  75 GLR--HLAFSVDD--IDAAVAHLESHNVkceAIRVDPYTQK--RFTFFNDPDGLPLEL 126
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 22-147 1.44e-06

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: 44.47  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  22 HIALNVKDIQASRHFYGTLLGlheltGEEVPSTLRSLVEAGKVTNFVTpDGIVVDLFSEPDLSPPDpdphrgftrVNHLA 101
Cdd:cd08345    1 HITLIVRDLEKSTAFLQDIFG-----AREVYSSGDKTFSLSKEKFFLL-GGLWIALMEGESLQERS---------YTHIA 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 495463412 102 FDIDPQLFDQAVEVLKQNQIPIDHG-PVTRPTGRGIYFYDPDGFIVE 147
Cdd:cd08345   66 FQIQSEDFDRYAERLGALGVEMRPPrPRVEGEGRSIYFYDPDNHLFE 112
PRK04101 PRK04101
metallothiol transferase FosB;
99-150 1.55e-06

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 44.94  E-value: 1.55e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495463412  99 HLAFDIDPQLFDQAVEVLKQNQIPIDHGpvtRP----TGRGIYFYDPDGFIVEIRC 150
Cdd:PRK04101  66 HIAFSIEEEDFDHWYQRLKENDVNILPG---RErderDKKSIYFTDPDGHKFEFHT 118
VOC_like cd08357
uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and ...
 21-149 2.10e-06

uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and type I ring-cleaving dioxygenases; 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: 319945 [Multi-domain]  Cd Length: 124  Bit Score: 44.30  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  21 HHIALNVKDIQASRHFYGTLLGLHEltgeevpstLRSlveagkvtnfvTPDGIVVDLFSEPDLSPPDPDPHRGFTR---- 96
Cdd:cd08357    1 FHLAIPVRDLEAARDFYGDVLGCPE---------GRS-----------SETWIDFNFFGHQVVAHLVPNYASTSTNavdg 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495463412  97 ----VNH--LAFDIDPqlFDQAVEVLKQNQIPIDHGPVTRPTG-----RGIYFYDPDGFIVEIR 149
Cdd:cd08357   61 hsvpVPHfgLALTVDD--FDALAERLKAAGVKFYIEPYVRFEGepgeqWTMFLLDPSGNALEFK 122
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 19-148 1.77e-05

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 41.54  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  19 RVHHIALNVKDIQASRHFYGTLLGLHELTGEEVPstlrslveaGKVTNFVTPDGIVVDLFSEPDLSPpdpdphrgfTRVN 98
Cdd:COG3324    4 TIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPG---------GDYAEFDTDGGQVGGLMPGAEEPG---------GPGW 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495463412  99 HLAFDIDPqlFDQAVEVLKQNQIPIDHGPVT-RPTGRGIYFYDPDGFIVEI 148
Cdd:COG3324   66 LLYFAVDD--LDAAVARVEAAGGTVLRPPTDiPPWGRFAVFRDPEGNRFGL 114
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 22-148 2.18e-05

fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin resistant protein. FosA is a Mn(II) and K(+)-dependent glutathione transferase. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosA, catalyzes the addition of glutathione to the antibiotic fosfomycin, (1R,2S)-epoxypropylphosphonic acid, making it inactive. FosA is a Mn(II) dependent enzyme. It is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319908 [Multi-domain]  Cd Length: 121  Bit Score: 41.50  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  22 HIALNVKDIQASRHFYGTLLGLheltgeevpstlRSLV--------EAGkvtnfvtpdGIVVDLFSEPDLSPpdpdpHRG 93
Cdd:cd07244    4 HITLAVSDLERSLAFYVDLLGF------------KPHVrwdkgaylTAG---------DLWLCLSLDPAAEP-----SPD 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495463412  94 FTrvnHLAFDIDPQLFDQAVEVLKQNQIPI---DHGPvtrptGRGIYFYDPDGFIVEI 148
Cdd:cd07244   58 YT---HIAFTVSEEDFEELSERLRAAGVKIwqeNSSE-----GDSLYFLDPDGHKLEL 107
HPCD_N_class_II cd07266
N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 19-147 3.44e-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: 40.85  E-value: 3.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  19 RVHHIALNVKDIQASRHFYGTLLGLHELTGEEVPSTLRSLVEAGKVTNFVTPDGIvvdlfsepdlsppdpdphrgfTRVN 98
Cdd:cd07266    4 RLAHAELVVTDLAASREFYVDTLGLHVTDEDDNAIYLRGVEEFIHHTLVLRKAPE---------------------AAVG 62

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495463412  99 HLAFDI-DPQLFDQAVEVLKQNQIPidHGPVTRP-TGRGIYFYDPDGFIVE 147
Cdd:cd07266   63 HLGFRVrDEADLDKAAAFYKELGLP--TEWREEPgQGRTLRVEDPFGFPIE 111
ChaP_like cd08351
ChaP, an enzyme involved in the biosynthesis of the antitumor agent chartreusin (cha), and ...
 22-148 3.49e-05

ChaP, an enzyme involved in the biosynthesis of the antitumor agent chartreusin (cha), and similar proteins; ChaP is an enzyme involved in the biosynthesis of the potent antitumor agent chartreusin (cha). Cha is an aromatic polyketide glycoside produced by Streptomyces chartreusis. ChaP may play a role as a meta-cleavage dioxygenase in the oxidative rearrangement of the anthracyclic polyketide. ChaP 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: 319939  Cd Length: 118  Bit Score: 40.95  E-value: 3.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  22 HIALNVKDIQASRHFYGTLLGLheltgeEVPstlrslVEAGKVTNFVTPDGIVVDlFSEPdlsppdpdphRGFTRVNHLA 101
Cdd:cd08351    5 HTIVPARDKEASARFLAEILGL------PAP------PPWGPFAPVRLNNGLTLD-FADP----------RGEIAPQHYA 61

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495463412 102 FDIDPQLFDQAVEVLKQNQIPIDHGPVTRPT--------GRGIYFYDPDGFIVEI 148
Cdd:cd08351   62 FLVSDDEFDAILARIRARGLEYWADPQHREPgeinhndgGRGVYFRDPDGHLLEI 116
Glyoxalase_2 pfam12681
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 23-154 3.61e-05

Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.


Pssm-ID: 403776  Cd Length: 118  Bit Score: 40.86  E-value: 3.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412   23 IALNVKDIQASRHFYGTLLGLheltgeevpstlRSLVEAGKVTNFVTPDGIVVDLFSEPDLSPPDPDPHRGFtrvnHLAF 102
Cdd:pfam12681   4 PLLVVKDINISRKFYEDVLDQ------------KIKLDFGENVSFEGGFAIQSDFKELIGIDLSIAEQSNNF----ELYF 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 495463412  103 DIDPqlFDQAVEVLKQN-QIPIDHGPVTRPTG-RGIYFYDPDGFIVEIrCDPIE 154
Cdd:pfam12681  68 EVAD--VDAFLQKIKEIgNIEYLHELKEQPWGqRVFRFYDPDGHIIEI-GESME 118
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 17-151 4.57e-05

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: 40.70  E-value: 4.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  17 LRRVHHIALNVKDIQASRHFYGTLLGLHEltgeevpstlrslveagkvtnfVTPDGIVVDLFSEPDLSPPDPDPHRGFTR 96
Cdd:cd08362    1 VTHLRYVALGVPDLAAEREFYTEVWGLEE----------------------VAEDDDVVYLRAEGSEHHVLRLRQSDENR 58

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 495463412  97 VNHLAFD-IDPQLFDQAVEVLKQNQIPIDH--GPVTRPT-GRGIYFYDPDGFIVEIRCD 151
Cdd:cd08362   59 LDLIAFAaATRADVDALAARLAAAGVRILSepGPLDDPGgGYGFRFFDPDGRTIEVSAD 117
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 19-154 9.01e-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: 39.99  E-value: 9.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  19 RVHHIALNVKDIQASRHFYGTLLGLheltgeevpstlrSLVEAGKVTNFVTPDGIVVDLFSEPDLSPPDPDphRGFTRVN 98
Cdd:cd07255    2 RIGRVTLKVADLERQSAFYQNVIGL-------------SVLKQNASRAYLGVDGKQVLLVLEAIPDAVLAP--RSTTGLY 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495463412  99 HLAFDI-DPQLFDQAVEVLKQNQIPI---DHGpvtrpTGRGIYFYDPDGFIVEIRCD-PIE 154
Cdd:cd07255   67 HFAILLpDRKALGRALAHLAEHGPLIgaaDHG-----VSEAIYLSDPEGNGIEIYADrPRE 122
BphC2-C3-RGP6_C_like cd08348
The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus ...
 122-151 1.05e-04

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


Pssm-ID: 319936  Cd Length: 137  Bit Score: 39.81  E-value: 1.05e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 495463412 122 PIDHGPVTrptgrGIYFYDPDGFIVEIRCD 151
Cdd:cd08348   99 PVNHGVTT-----SIYYRDPDGNMLEMQVD 123
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 23-148 1.89e-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: 319914 [Multi-domain]  Cd Length: 120  Bit Score: 38.81  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  23 IALNVKDIQASRHFYGTLlglheltGEEvpstlRSLVEAGKVTNFVTPDGIV----VDLFSEPDLSPPDPDPHRGFTrvn 98
Cdd:cd07251    2 ITLGVRDLERSARFYEAL-------GWK-----PNLDPNDGVVFFQLGGTVLalypRDALAEDAGVSVTGAGFSGVT--- 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  99 hLAF------DIDpQLFDQAVE----VLKQNQiPIDHGpvtrptGRGIYFYDPDGFIVEI 148
Cdd:cd07251   67 -LAHnvrsreEVD-QLLAKAVAaggkILKPPQ-EVFWG------GYSGYFADPDGHIWEV 117
PpCmtC_C cd07258
C-terminal domain of 2,3-dihydroxy-p-cumate-3,4-dioxygenase (PpCmtC); This subfamily contains ...
 93-147 2.10e-04

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: 39.10  E-value: 2.10e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495463412  93 GFTRVNHLAFDIDPQLfdQAVEVLKQNQIPIDHGPVTRPT--GRGIYFYDPDGFIVE 147
Cdd:cd07258   53 GIQHINHQVTSIDDVL--RSYYRLKEHDVPIVFGPGRHPTsgARFLYFKGPDGMTFE 107
VOC_like cd09011
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 27-148 2.15e-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: 319953  Cd Length: 122  Bit Score: 38.61  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  27 VKDIQASRHFYGTLLGLheltgeevpstlRSLVEAGKvtNFVTPDGIVVDLFSEPDLSPPDPDPHRGFTRVN-HLAFDID 105
Cdd:cd09011   10 VKDIEKSKKFYEDVLGQ------------KILLDFGE--NVVFEGGFALQEKKSWLETIIISDLSIKQQSNNfELYFEVD 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 495463412 106 PqlFDQAVEVLKQNQ-IPIDHGPVTRPTG-RGIYFYDPDGFIVEI 148
Cdd:cd09011   76 D--FDAFFEKLNPHKdIEFIHPILEHPWGqRVFRFYDPDGHIIEI 118
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 22-148 7.74e-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: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 37.31  E-value: 7.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  22 HIALNVKDIQASRHFYGTLLGLheltgeevpsTLRSLVEAGKVTNFVTpDGIVVDLFSEPDLSPPDPDPHRGFTRvnHLA 101
Cdd:cd07264    3 YIVLYVDDFAASLRFYRDVLGL----------PPRFLHEEGEYAEFDT-GETKLALFSRKEMARSGGPDRRGSAF--ELG 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 495463412 102 FDIDPqlFDQAVEVLKQNQIPIDHGPVTRPTG-RGIYFYDPDGFIVEI 148
Cdd:cd07264   70 FEVDD--VEATVEELVERGAEFVREPANKPWGqTVAYVRDPDGNLIEI 115
COG3565 COG3565
Predicted dioxygenase of extradiol dioxygenase family [General function prediction only];
22-45 7.86e-04

Predicted dioxygenase of extradiol dioxygenase family [General function prediction only];


Pssm-ID: 442786  Cd Length: 139  Bit Score: 37.46  E-value: 7.86e-04
                         10        20
                 ....*....|....*....|....
gi 495463412  22 HIALNVKDIQASRHFYGTLLGLHE 45
Cdd:COG3565    7 HLAFPVTDLDAARRFYGDVLGCEE 30
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 20-148 8.24e-04

Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) interconverts (2R)-methylmalonyl-CoA and (2S)-methylmalonyl-CoA. MMCE has been found in bacteria, archaea, and in animals. In eukaryotes, MMCE is an essential enzyme in a pathway that converts propionyl-CoA to succinyl-CoA, and is important in the breakdown of odd-chain length fatty acids, branched-chain amino acids, and other metabolites. In bacteria, MMCE participates in the reverse pathway for propionate fermentation, glyoxylate regeneration, and the biosynthesis of polyketide antibiotics. MMCE is closely related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319912 [Multi-domain]  Cd Length: 127  Bit Score: 37.17  E-value: 8.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  20 VHHIALNVKDIQASRHFYGTLLGLHELTGEEVPstlrslvEAGKVTNFVTPDGIVVDL---FSEPDLSPPDPDPHRGftR 96
Cdd:cd07249    1 LDHIGIAVPDLDEALKFYEDVLGVKVSEPEELE-------EQGVRVAFLELGNTQIELlepLGEDSPIAKFLDKKGG--G 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495463412  97 VNHLAFDIDPqlFDQAVEVLKQNQI-PIDHGPVTRPTGRGIYFYDPD---GFIVEI 148
Cdd:cd07249   72 LHHIAFEVDD--IDAAVEELKAQGVrLLSEGPRIGAHGKRVAFLHPKdtgGVLIEL 125
catechol_2_3 TIGR03211
catechol 2,3 dioxygenase; Members of this family all are enzymes active as catechol 2,3 ...
 96-147 1.19e-03

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: 37.99  E-value: 1.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 495463412   96 RVNHLAFDID-PQLFDQAVEVLKQNQIPIDHGP----VTRptGRGIYFYDPDGFIVE 147
Cdd:TIGR03211 207 KLHHVSFFLDsWEDVLKAADVMSKNDVSIDIGPtrhgITR--GQTIYFFDPSGNRNE 261
VOC_BsYqjT cd07242
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; The vicinal ...
 20-148 1.80e-03

vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; 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: 319906  Cd Length: 126  Bit Score: 36.31  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  20 VHHIALNVKDIQASRHFYGTLLGLHELTGEEVPSTLRSLVEAGKVTNFVTPDGIVVDLFsepdlsppdpdpHRGFTRVNH 99
Cdd:cd07242    2 VSHVELAVSDLHRSFKWFEWILGLGWKEYDTWSFGPSWKLSGGSLLVVQQTDEFATPEF------------DRARVGLNH 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 495463412 100 LAFDIDPQL-FDQAVEVLKQNQIPI----DHGPVTRPTGRGIYFYDPDGFIVEI 148
Cdd:cd07242   70 LAFHAESREaVDELTEKLAKIGGVRtygdRHPFAGGPPHYAAFCEDPDGIKLEL 123
BphC-JF8_C_like cd09014
C-terminal, catalytic domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase); 2, ...
 16-152 2.71e-03

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: 36.20  E-value: 2.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  16 SLRRVHHIALNVKDIQASRHFYGTLLGLHelTGEEVPSTLRslVEAG---KVTNFVTPDGIVVDLFSEpdlsppdpdphR 92
Cdd:cd09014    3 PVRRIDHLNLLASDVTANRQFMSDTLGFR--LREQIRDNNG--GEAGawmSVSSLVHDVAVMRDGKGE-----------P 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495463412  93 GftRVNHLAFDID-PQLFDQAVEVLKQNQIPIDHGPVTRPTGRG--IYFYDPDGFIVEIRCDP 152
Cdd:cd09014   68 G--RLHHLAYWYGtPEDLLRAADIFREHGIQIEAGPGKHGISQAffLYVYEPGGNRVELFGGA 128
FosX cd08364
fosfomycin resistant protein subfamily FosX; This subfamily family contains FosX, a fosfomycin ...
 98-148 3.83e-03

fosfomycin resistant protein subfamily FosX; This subfamily family contains FosX, a fosfomycin resistant protein. FosX is a Mn(II)-dependent fosfomycin-specific epoxide hydrolase. Fosfomycin inhibits the enzyme UDP-Nacetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosX catalyzes the addition of a water molecule to the C1 position of the antibiotic with inversion of the configuration at C1 in the presence of Mn(II). The hydrated fosfomycin loses the inhibition activity. FosX is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319952  Cd Length: 130  Bit Score: 35.33  E-value: 3.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495463412  98 NHLAFDIDPQLFDQAVEVLKQNQIPIDHGpvtRP----TGRGIYFYDPDGFIVEI 148
Cdd:cd08364   67 NHIAFKVSEGDLDEYRARIKKLGLEIRPP---RSrvqgEGRSLYFYDFDNHLFEL 118
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 22-148 3.89e-03

Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that prefers the divalent cation zinc as cofactor. Glyoxalase I (also known as lactoylglutathione lyase; EC 4.4.1.5) is part of the glyoxalase system, a two-step system for detoxifying methylglyoxal, a side product of glycolysis. This system is responsible for the conversion of reactive, acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids and involves 2 enzymes, glyoxalase I and II. Glyoxalase I catalyses an intramolecular redox reaction of the hemithioacetal (formed from methylglyoxal and glutathione) to form the thioester, S-D-lactoylglutathione. This reaction involves the transfer of two hydrogen atoms from C1 to C2 of the methylglyoxal, and proceeds via an ene-diol intermediate. Glyoxalase I has a requirement for bound metal ions for catalysis. Eukaryotic glyoxalase I prefers the divalent cation zinc as cofactor, whereas Escherichia coil and other prokaryotic glyoxalase I uses nickel. However, eukaryotic Trypanosomatid parasites also use nickel as a cofactor, which could possibly be explained by acquiring their GLOI gene by horizontal gene transfer. Human glyoxalase I is a two-domain enzyme and it has the structure of a domain-swapped dimer with two active sites located at the dimer interface. In yeast, in various plants, insects and Plasmodia, glyoxalase I is four-domain, possibly the result of a further gene duplication and an additional gene fusing event.


Pssm-ID: 319900 [Multi-domain]  Cd Length: 142  Bit Score: 35.77  E-value: 3.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  22 HIALNVKDIQASRHFYGTLLGLHELTGEEVPSTLRSLVEAG-KVTNFVTPDGIVVDLFS----------------EPDLS 84
Cdd:cd07233    3 HTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGyEDPKDIPKDPRTAWVFSregtlelthnwgtendEDPVY 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495463412  85 PPDPDPHRGFtrvNHLAFDIDPqlFDQAVEVLKQNQIPIdhgpVTRPTG---RGIYF-YDPDGFIVEI 148
Cdd:cd07233   83 HNGNSDPRGF---GHIGIAVDD--VYAACERFEELGVKF----KKKPDDgkmKGIAFiKDPDGYWIEI 141
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
21-138 4.71e-03

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 34.95  E-value: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412   21 HHIALNVKDIQASRHFYGTLLGLheltgeEVPSTLRSLVEAGKVTNFVTPDG-IVVDLFSepdLSPPDPDPHRGFTRVNH 99
Cdd:pfam13669   1 HHVGIAVPDLDRALALWGALLGL------GPEGDYRSEPQNVDLAFALLGDGpVEVELIQ---PLDGDSPLARHGPGLHH 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 495463412  100 LAFDIDPqlFDQAVEVLKQNQIP-IDHGPVTRPTGRGIYF 138
Cdd:pfam13669  72 LAYWVDD--LDAAVARLLDQGYRvAPKGPRAGAAGRRVAF 109
2_3_CTD_C cd07243
C-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the C-terminal, ...
 46-143 6.39e-03

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: 35.07  E-value: 6.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495463412  46 LTGEEVPSTLRSLVeagKVTNF------VTPDG---IVVDLFSEPDLSPPDPDPHRGFTRVNHLAFDIDP-QLFDQAVEV 115
Cdd:cd07243   12 LYGERIAETTRFFT---DVLGFyltervLDPDGgtrVGIFLSCSNKAHDIAFVGYPEDGKLHHTSFFLESwEDVLKAGDI 88

                         90       100       110
                 ....*....|....*....|....*....|..
gi 495463412 116 LKQNQIPIDHGP----VTRptGRGIYFYDPDG 143
Cdd:cd07243   89 ISKNDVSIDIGPtrhgITR--GQTIYFFDPSG 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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