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Conserved domains on  [gi|488997115|ref|WP_002907816|]
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MULTISPECIES: VOC family protein [Klebsiella]

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 ...
 2-126 1.07e-50

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 cd07241:

Pssm-ID: 472697  Cd Length: 125  Bit Score: 156.80  E-value: 1.07e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997115   2 KIAHIALWTQQLDVQARFWVDFFAASINEKYLSQTnPGFASYFVTIDDEVVIELMTKPGLQQASADNNHTGWAHLALSVG 81
Cdd:cd07241    1 KIEHVALWTNDLERMKDFYVKYFGAESNDIYHNKK-KGFRSYFLTFDSGARLELMSRPDVTDPDKEVERTGLAHIAFSVG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488997115  82 GAEQVDAIAQRAGAAGI-LISPPRTTGDGYYEAVIADPDGNLIEIV 126
Cdd:cd07241   80 SKEAVDELTERLRADGYaVVGGPRTTGDGYYESVILDPEGNRIEIT 125
 
Name Accession Description Interval E-value
VOC_BsYyaH cd07241
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal ...
 2-126 1.07e-50

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


Pssm-ID: 319905  Cd Length: 125  Bit Score: 156.80  E-value: 1.07e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997115   2 KIAHIALWTQQLDVQARFWVDFFAASINEKYLSQTnPGFASYFVTIDDEVVIELMTKPGLQQASADNNHTGWAHLALSVG 81
Cdd:cd07241    1 KIEHVALWTNDLERMKDFYVKYFGAESNDIYHNKK-KGFRSYFLTFDSGARLELMSRPDVTDPDKEVERTGLAHIAFSVG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488997115  82 GAEQVDAIAQRAGAAGI-LISPPRTTGDGYYEAVIADPDGNLIEIV 126
Cdd:cd07241   80 SKEAVDELTERLRADGYaVVGGPRTTGDGYYESVILDPEGNRIEIT 125
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-126 1.45e-23

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: 88.13  E-value: 1.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997115   1 MKIAHIALWTQQLDVQARFWVDFFAASINEKYlSQTNPGFASYFVTIDDEVVIELMTKPGlqqASADNNHTGWAHLALSV 80
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRT-DFGDGGFGHAFLRLGDGTELELFEAPG---AAPAPGGGGLHHLAFRV 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 488997115  81 ggaEQVDAIAQRAGAAGI-LISPPRTTGDGYYEAVIADPDGNLIEIV 126
Cdd:COG0346   77 ---DDLDAAYARLRAAGVeIEGEPRDRAYGYRSAYFRDPDGNLIELV 120
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-125 1.57e-14

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 64.78  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997115    2 KIAHIALWTQQLDVQARFWVDFFAASINEKYlSQTNPGFASYFVTIDDEVVIELMTKPGlqqASADNNHTGWAHLALSVG 81
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEET-DAGEEGGLRSAFFLAGGRVLELLLNET---PPPAAAGFGGHHIAFIAF 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 488997115   82 GAEQVDAIAQRAGAAGI-LISPPRTTGDGYYEAVIADPDGNLIEI 125
Cdd:pfam00903  77 SVDDVDAAYDRLKAAGVeIVREPGRHGWGGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
VOC_BsYyaH cd07241
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal ...
 2-126 1.07e-50

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


Pssm-ID: 319905  Cd Length: 125  Bit Score: 156.80  E-value: 1.07e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997115   2 KIAHIALWTQQLDVQARFWVDFFAASINEKYLSQTnPGFASYFVTIDDEVVIELMTKPGLQQASADNNHTGWAHLALSVG 81
Cdd:cd07241    1 KIEHVALWTNDLERMKDFYVKYFGAESNDIYHNKK-KGFRSYFLTFDSGARLELMSRPDVTDPDKEVERTGLAHIAFSVG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488997115  82 GAEQVDAIAQRAGAAGI-LISPPRTTGDGYYEAVIADPDGNLIEIV 126
Cdd:cd07241   80 SKEAVDELTERLRADGYaVVGGPRTTGDGYYESVILDPEGNRIEIT 125
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-126 1.45e-23

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: 88.13  E-value: 1.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997115   1 MKIAHIALWTQQLDVQARFWVDFFAASINEKYlSQTNPGFASYFVTIDDEVVIELMTKPGlqqASADNNHTGWAHLALSV 80
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRT-DFGDGGFGHAFLRLGDGTELELFEAPG---AAPAPGGGGLHHLAFRV 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 488997115  81 ggaEQVDAIAQRAGAAGI-LISPPRTTGDGYYEAVIADPDGNLIEIV 126
Cdd:COG0346   77 ---DDLDAAYARLRAAGVeIEGEPRDRAYGYRSAYFRDPDGNLIELV 120
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 5-125 6.42e-20

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: 78.34  E-value: 6.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997115   5 HIALWTQQLDVQARFWVDFFAAsinekYLSQTNPGFASYFVTIDDEVVIELMTKPGLQqasaDNNHTGWAHLALSVGGAE 84
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGF-----EVVSRNEGGGFAFLRLGPGLRLALLEGPEPE----RPGGGGLFHLAFEVDDVD 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 488997115  85 QVDAIAQRAGAAGILISPPRTTGDGYYEAVIADPDGNLIEI 125
Cdd:cd06587   72 EVDERLREAGAEGELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 21-126 1.57e-15

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 67.55  E-value: 1.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997115  21 VDFFAA---SINEKYlsqTNPGFAsyFVTIDDEVVIELMTKPGLQQ----ASADNNHTGWAHLALSVGGAEQVDAIAQRA 93
Cdd:COG3607   18 RAFYEAlgfTFNPQF---SDEGAA--CFVLGEGIVLMLLPREKFATftgkPIADATGFTEVLLALNVESREEVDALVAKA 92

                         90       100       110
                 ....*....|....*....|....*....|....
gi 488997115  94 GAAGI-LISPPRTTGDGYYeAVIADPDGNLIEIV 126
Cdd:COG3607   93 LAAGGtVLKPPQDVGGMYS-GYFADPDGHLWEVA 125
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
1-127 8.41e-15

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 66.13  E-value: 8.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997115   1 MKIAHIALWTQQLDVQARFWVDFFAASINEKYlsqtnPGFAsYFVTIDDEVVIELMTKPGlqqASADNNHTGWAHLALSV 80
Cdd:COG2514    2 TRLGHVTLRVRDLERSAAFYTDVLGLEVVERE-----GGRV-YLRADGGEHLLVLEEAPG---APPRPGAAGLDHVAFRV 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 488997115  81 GGAEQVDAIAQRAGAAGILISPPRTTGDGyyEAV-IADPDGNLIEIVA 127
Cdd:COG2514   73 PSRADLDAALARLAAAGVPVEGAVDHGVG--ESLyFRDPDGNLIELYT 118
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-125 1.57e-14

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 64.78  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997115    2 KIAHIALWTQQLDVQARFWVDFFAASINEKYlSQTNPGFASYFVTIDDEVVIELMTKPGlqqASADNNHTGWAHLALSVG 81
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEET-DAGEEGGLRSAFFLAGGRVLELLLNET---PPPAAAGFGGHHIAFIAF 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 488997115   82 GAEQVDAIAQRAGAAGI-LISPPRTTGDGYYEAVIADPDGNLIEI 125
Cdd:pfam00903  77 SVDDVDAAYDRLKAAGVeIVREPGRHGWGGRYSYFRDPDGNLIEL 121
VOC_BsYqjT cd07242
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; The vicinal ...
 3-127 1.06e-09

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: 52.49  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997115   3 IAHIALWTQQLDVQARFWVDFFAASINEkylSQTNPGFASYFVTIDDEVVIElmTKPGLQQASADNNHTGWAHLALSVGG 82
Cdd:cd07242    2 VSHVELAVSDLHRSFKWFEWILGLGWKE---YDTWSFGPSWKLSGGSLLVVQ--QTDEFATPEFDRARVGLNHLAFHAES 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488997115  83 AEQVDAIAQRAGAAGILISP----PRTTGDGYYEAVIADPDGNLIEIVA 127
Cdd:cd07242   77 REAVDELTEKLAKIGGVRTYgdrhPFAGGPPHYAAFCEDPDGIKLELVA 125
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-126 2.23e-09

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 51.17  E-value: 2.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997115   1 MKIAHIALWTQQLDVQARFWVDFFAASINEKYlsqtnpGFASYFVTIDDEVVIELmtkpGLQQASADNNHTGWaHLALSV 80
Cdd:COG3324    3 GTIVWVELPVDDLERAKAFYEEVFGWTFEDDA------GPGGDYAEFDTDGGQVG----GLMPGAEEPGGPGW-LLYFAV 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 488997115  81 ggaEQVDAIAQRAGAAGI-LISPPRTTGDGYYEAVIADPDGNLIEIV 126
Cdd:COG3324   72 ---DDLDAAVARVEAAGGtVLRPPTDIPPWGRFAVFRDPEGNRFGLW 115
BphC2-C3-RGP6_C_like cd08348
The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus ...
 2-125 2.06e-08

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: 49.06  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997115   2 KIAHIALWTQQLDVQA--RFWVDFFAASINEKylsqtNPGFAsyFVTIDDEV-VIELMTKPGLQQASADN-NHTGWAHLA 77
Cdd:cd08348    1 KLAHFVLRTNPEKFEAmvQWYLDILGARIVAR-----NAKGC--FLSFDEEHhRIAIFGAPGGAQPPDKRpTRVGLAHIA 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488997115  78 LSVGGAEQV-DAIAQRAgAAGILISPP----RTTGDGYYeaviaDPDGNLIEI 125
Cdd:cd08348   74 FTYASLDDLaRNYAQLK-ERGIKPVWPvnhgVTTSIYYR-----DPDGNMLEM 120
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 75-127 4.48e-07

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: 45.32  E-value: 4.48e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488997115  75 HLALSVGGAEQVDAIAQRAGAAGI-LISPPRTTGD--GYYEAVIADPDGNLIEIVA 127
Cdd:cd08362   61 LIAFAAATRADVDALAARLAAAGVrILSEPGPLDDpgGGYGFRFFDPDGRTIEVSA 116
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-125 3.55e-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: 319917 [Multi-domain]  Cd Length: 120  Bit Score: 42.83  E-value: 3.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997115   5 HIALWTQQLDVQARFWVDFFAASINEKYlsqtnPGFASYFVTiDDEVVIELMTKPGLQQASADnnhtgwaHLALSVGGAE 84
Cdd:cd07254    4 HLSLNVTDLERSIRFYSDLFGAEPAKRK-----ADYAKFMLE-DPPLNLALLVNDRKEPYGLN-------HLGIQVDSKE 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 488997115  85 QVDAIAQRAGAAGI-LISPPRTT-----GDGYYeavIADPDGNLIEI 125
Cdd:cd07254   71 EVAALKARAEAAGLpVRKEPRTTccyavQDKFW---LTDPDGNAWEF 114
VOC_like cd09012
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 47-126 5.00e-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: 319954  Cd Length: 127  Bit Score: 42.75  E-value: 5.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997115  47 IDDEVVIELMTKPGLQQ-----ASADNNHTGWAHLALSVGGAEQVDAIAQRAGAAGILISPPRTTGD--GYYEAVIADPD 119
Cdd:cd09012   39 VSDNIFVMLLAHDRFKTfipepIAVDAKKSTEVLLTLSAKSRQEVDAFVDKAVEAGGKADPYVNGGDegFMYGRSFEDLD 118


                 ....*..
gi 488997115 120 GNLIEIV 126
Cdd:cd09012  119 GHLWEVV 125
PsjN_like cd16356
Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme ...
 76-125 5.38e-06

Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme and similar proteins; Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme 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: 319963  Cd Length: 119  Bit Score: 42.41  E-value: 5.38e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488997115  76 LALSVGGAEQVDAIAQRAGAAG-ILISPPRTTGDGYYEAVIADPDGNLIEI 125
Cdd:cd16356   69 LTFDVDDVEAVDRLVPRAAALGaTLIKPPYDTYYGWYQAVLLDPEGNVFRI 119
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-125 2.01e-05

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


Pssm-ID: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 40.76  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997115   5 HIALWTQQLDVQARFWVDFFAASINEKYLSQTNPGfasYFVTIDDEVVIELMTKPGLQQASADnnHTGW--AHLALSVGG 82
Cdd:cd07245    3 HVALACPDLERARRFYTDVLGLEEVPRPPFLKFGG---AWLYLGGGQQIHLVVEQNPSELPRP--EHPGrdRHPSFSVPD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488997115  83 aeqVDAIAQRAGAAGILIsPPRTTGDGYYEAV-IADPDGNLIEI 125
Cdd:cd07245   78 ---LDALKQRLKEAGIPY-TESTSPGGGVTQLfFRDPDGNRLEF 117
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 49-125 2.25e-05

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


Pssm-ID: 319940 [Multi-domain]  Cd Length: 123  Bit Score: 40.99  E-value: 2.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997115  49 DEVVIELMTKPGLQQASADNNHTGWAHLALSVggaEQVDAIAQRAGAAGILISPPRT---TGDGYyeAVIADPDGNLIEI 125
Cdd:cd08352   47 GGYQLELFIKPDAPARPSYPEALGLRHLAFKV---EDVEATVAELKSLGIETEPIRVddfTGKKF--TFFFDPDGLPLEL 121
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
74-125 9.21e-05

Zn-dependent glyoxalase, PhnB family [Energy production and conversion];


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 39.07  E-value: 9.21e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488997115  74 AHLALSVggaEQVDAIAQRAGAAG-ILISPPRTTGDGYYEAVIADPDGNLIEI 125
Cdd:COG2764   66 VSLSLYV---DDVDALFARLVAAGaTVVMPLQDTFWGDRFGMVRDPFGVLWMI 115
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 74-126 1.25e-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: 319923 [Multi-domain]  Cd Length: 121  Bit Score: 38.75  E-value: 1.25e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488997115  74 AHLALSVGGAEQVDAIAQRAGAAG-ILISPP---RTTGDGYYEAVIADPDGNLIEIV 126
Cdd:cd07262   64 THVAFAAPSRAAVDAFHAAALAAGgTDNGAPglrPHYHPGYYAAYVRDPDGNKIEAV 120
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-125 1.85e-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: 38.47  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997115   3 IAHIALWTQQLDVQARFWVDFFAASINekylSQTNPGFASYFVTIddEVVIELMTKPGLQQASADNNHTGWAHLALSVgg 82
Cdd:cd07264    1 IAYIVLYVDDFAASLRFYRDVLGLPPR----FLHEEGEYAEFDTG--ETKLALFSRKEMARSGGPDRRGSAFELGFEV-- 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488997115  83 aEQVDAIAQRAGAAGILI-SPPRTTGDGYYEAVIADPDGNLIEI 125
Cdd:cd07264   73 -DDVEATVEELVERGAEFvREPANKPWGQTVAYVRDPDGNLIEI 115
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 61-126 2.19e-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: 38.04  E-value: 2.19e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488997115  61 LQQASADNNHTGWAhLALSVGGAEQVDAIAQRAGAAG-ILISPPRTTGDGYYEAVIADPDGNLIEIV 126
Cdd:cd07251   53 AGVSVTGAGFSGVT-LAHNVRSREEVDQLLAKAVAAGgKILKPPQEVFWGGYSGYFADPDGHIWEVA 118
EhpR_like cd07261
phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter ...
 72-127 2.84e-04

phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter agglomerans confers resistance by binding D-alanyl-griseoluteic acid and acting as a chaperone involved in exporting the antibiotic rather than by altering it chemically. EhpR is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319922  Cd Length: 114  Bit Score: 37.77  E-value: 2.84e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488997115  72 GWAHLALSVGGAEQVDAIAQRAGAAGILISPPRTTGDGYYEAVIADPDGNLIEIVA 127
Cdd:cd07261   59 GGAELSFMVPSGEQVDEVYAEWKAMGIPIIQEPTTMDFGYTFVATDPDGHRLRVCC 114
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 2-126 3.13e-03

vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; This subfamily of vicinal oxygen chelate (VOC) family protein includes Streptomyces hygroscopicus ValD protein and similar proteins. ValD protein functions in validamycin biosynthetic pathway. 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: 319968  Cd Length: 150  Bit Score: 35.38  E-value: 3.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997115   2 KIAHIALWTQQLDVQARFWVDFFAASIneKYLSQT------------NPGFASYFVTID-------DEVVIELMTKPGLQ 62
Cdd:cd16361    1 GVNHVGITVPDLDAAVEFYTDVLGAEV--VYRSTPlaegdrgggemrAAGFVPGFARARiamlrlgPGPGIELFEYKGPE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488997115  63 QASA--DNNHTGWAHLALSVggaEQVDAIAQR-AGAAGILISPPRTTGD-----GYYEAVIADPDGNLIEIV 126
Cdd:cd16361   79 QRAPvpRNSDVGIFHFALQV---DDVEAAAERlAAAGGKVLMGPREIPDggpgkGNRMVYLRDPWGTLIELV 147
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 82-127 8.49e-03

N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth disturbances caused by high osmolarity and a high concentration of A-factor, a microbial hormone, during the early growth phase in Streptomyces griseus. A-factor (2-isocapryloyl-3R-hydroxymethyl-gamma-butyrolactone) controls morphological differentiation and secondary metabolism in Streptomyces griseus. It is a chemical signaling molecule that at a very low concentration acts as a switch for yellow pigment production, aerial mycelium formation, streptomycin production, and streptomycin resistance. The structure and amino acid sequence of SgaA are closely related to a group of antibiotics resistance proteins, including bleomycin resistance protein, mitomycin resistance protein, and fosfomycin resistance proteins. SgaA might also function as a streptomycin resistance protein.


Pssm-ID: 319911 [Multi-domain]  Cd Length: 114  Bit Score: 33.78  E-value: 8.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 488997115  82 GAEQVDAIAQRAGAAG-ILISPPRTTGDGYYEAVIADPDGNLIEIVA 127
Cdd:cd07247   68 AVDDLDAALARVEAAGgKVVVPPTDIPGGGRFAVFADPEGNRFGLWS 114
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 1-125 8.55e-03

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


Pssm-ID: 319918  Cd Length: 124  Bit Score: 33.82  E-value: 8.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488997115   1 MKIAHIALWTQQLDVQARFWVDFFAASINEKYLSQTnpgfasYFVTIDDEVVIELMTKPGLQQAsaDNNHTGWAHLALSV 80
Cdd:cd07255    1 TRIGRVTLKVADLERQSAFYQNVIGLSVLKQNASRA------YLGVDGKQVLLVLEAIPDAVLA--PRSTTGLYHFAILL 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 488997115  81 GGAEQVDAIAQRAGAAGILISPprttGD-GYYEAVIA-DPDGNLIEI 125
Cdd:cd07255   73 PDRKALGRALAHLAEHGPLIGA----ADhGVSEAIYLsDPEGNGIEI 115
 
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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