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Conserved domains on  [gi|492089737|ref|WP_005744922|]
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MULTISPECIES: VOC family protein [Pseudomonas]

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 ...
 7-131 7.79e-44

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 cd08354:

Pssm-ID: 472697  Cd Length: 122  Bit Score: 139.81  E-value: 7.79e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737   7 IIETALYVENLAKARDFYSDTLELEVMFESPTLVAFNVGGvSTLLLFKCGASlqTQYLSGGEIPPHDAQGRIHVCFAINA 86
Cdd:cd08354    1 ILETCLYADDLDAAEAFYEDVLGLKPMLRSGRHAFFRLGP-QVLLVFDPGAT--SKDVRTGEVPGHGASGHGHFAFAVPT 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 492089737  87 DQMQPWSDRLAQAKVAIEGRTEWPRGGSSIYFRDPDENLVELLTP 131
Cdd:cd08354   78 EELAAWEARLEAKGVPIESYTQWPEGGKSLYFRDPAGNLVELASA 122
 
Name Accession Description Interval E-value
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-131 7.79e-44

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


Pssm-ID: 319942  Cd Length: 122  Bit Score: 139.81  E-value: 7.79e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737   7 IIETALYVENLAKARDFYSDTLELEVMFESPTLVAFNVGGvSTLLLFKCGASlqTQYLSGGEIPPHDAQGRIHVCFAINA 86
Cdd:cd08354    1 ILETCLYADDLDAAEAFYEDVLGLKPMLRSGRHAFFRLGP-QVLLVFDPGAT--SKDVRTGEVPGHGASGHGHFAFAVPT 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 492089737  87 DQMQPWSDRLAQAKVAIEGRTEWPRGGSSIYFRDPDENLVELLTP 131
Cdd:cd08354   78 EELAAWEARLEAKGVPIESYTQWPEGGKSLYFRDPAGNLVELASA 122
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
4-132 5.22e-23

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 87.32  E-value: 5.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737   4 LNKIIETALYVENLAKARDFYSDTLELEVMFESPTLVAFNV-GGVSTLLLFKcgaslqtqylSGGEIPPHDAQGRIHVCF 82
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRAdGGEHLLVLEE----------APGAPPRPGAAGLDHVAF 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 492089737  83 AI-NADQMQPWSDRLAQAKVAIEGRTEwPRGGSSIYFRDPDENLVELLTPG 132
Cdd:COG2514   71 RVpSRADLDAALARLAAAGVPVEGAVD-HGVGESLYFRDPDGNLIELYTDR 120
PRK04101 PRK04101
metallothiol transferase FosB;
14-130 1.19e-12

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 60.73  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737  14 VENLAKARDFYSDTLELEVMFESPTLVAFNVGGVstlllfkcgaslqtqYLSGGE---IPPHDA-QGRIHVCFAINADQM 89
Cdd:PRK04101  12 VSNLEKSIEFYEKVLGAKLLVKGRKTAYFDLNGL---------------WIALNEekdIPRNEIhQSYTHIAFSIEEEDF 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 492089737  90 QPWSDRLAQAKVAI-EGRTEWPRGGSSIYFRDPDENLVELLT 130
Cdd:PRK04101  77 DHWYQRLKENDVNIlPGRERDERDKKSIYFTDPDGHKFEFHT 118
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
6-128 5.97e-12

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 58.61  E-value: 5.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737    6 KIIETALYVENLAKARDFYSDTLELEV-------MFESPTLVAFNVGGvSTLLLFKCGAslqtqylSGGEIPPHDAQGRI 78
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLveetdagEEGGLRSAFFLAGG-RVLELLLNET-------PPPAAAGFGGHHIA 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 492089737   79 HvcFAINADQMQPWSDRLAQAKVAIE---GRTEWprGGSSIYFRDPDENLVEL 128
Cdd:pfam00903  73 F--IAFSVDDVDAAYDRLKAAGVEIVrepGRHGW--GGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-131 7.79e-44

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


Pssm-ID: 319942  Cd Length: 122  Bit Score: 139.81  E-value: 7.79e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737   7 IIETALYVENLAKARDFYSDTLELEVMFESPTLVAFNVGGvSTLLLFKCGASlqTQYLSGGEIPPHDAQGRIHVCFAINA 86
Cdd:cd08354    1 ILETCLYADDLDAAEAFYEDVLGLKPMLRSGRHAFFRLGP-QVLLVFDPGAT--SKDVRTGEVPGHGASGHGHFAFAVPT 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 492089737  87 DQMQPWSDRLAQAKVAIEGRTEWPRGGSSIYFRDPDENLVELLTP 131
Cdd:cd08354   78 EELAAWEARLEAKGVPIESYTQWPEGGKSLYFRDPAGNLVELASA 122
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
4-132 5.22e-23

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 87.32  E-value: 5.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737   4 LNKIIETALYVENLAKARDFYSDTLELEVMFESPTLVAFNV-GGVSTLLLFKcgaslqtqylSGGEIPPHDAQGRIHVCF 82
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRAdGGEHLLVLEE----------APGAPPRPGAAGLDHVAF 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 492089737  83 AI-NADQMQPWSDRLAQAKVAIEGRTEwPRGGSSIYFRDPDENLVELLTPG 132
Cdd:COG2514   71 RVpSRADLDAALARLAAAGVPVEGAVD-HGVGESLYFRDPDGNLIELYTDR 120
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-132 1.26e-21

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: 83.50  E-value: 1.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737   6 KIIETALYVENLAKARDFYSDTLELEVMFESP------TLVAFNVGGVSTLLLFKcgaslqtqylSGGEIPPHDAQGRIH 79
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDfgdggfGHAFLRLGDGTELELFE----------APGAAPAPGGGGLHH 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492089737  80 VCFAinADQMQPWSDRLAQAKVAIE-GRTEWPRGGSSIYFRDPDENLVELLTPG 132
Cdd:COG0346   72 LAFR--VDDLDAAYARLRAAGVEIEgEPRDRAYGYRSAYFRDPDGNLIELVEPP 123
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 10-128 2.03e-14

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: 64.47  E-value: 2.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737  10 TALYVENLAKARDFYSDTLELEV--MFESPTLVAFNVGGVSTLLLFkcgaslqtqylSGGEIPPHDAQGRIHVCFAI-NA 86
Cdd:cd06587    2 VALRVPDLDASVAFYEEVLGFEVvsRNEGGGFAFLRLGPGLRLALL-----------EGPEPERPGGGGLFHLAFEVdDV 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 492089737  87 DQMQPWSDRLAQAKVAIEGRTEWPRGGSSIYFRDPDENLVEL 128
Cdd:cd06587   71 DEVDERLREAGAEGELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
PRK04101 PRK04101
metallothiol transferase FosB;
14-130 1.19e-12

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 60.73  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737  14 VENLAKARDFYSDTLELEVMFESPTLVAFNVGGVstlllfkcgaslqtqYLSGGE---IPPHDA-QGRIHVCFAINADQM 89
Cdd:PRK04101  12 VSNLEKSIEFYEKVLGAKLLVKGRKTAYFDLNGL---------------WIALNEekdIPRNEIhQSYTHIAFSIEEEDF 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 492089737  90 QPWSDRLAQAKVAI-EGRTEWPRGGSSIYFRDPDENLVELLT 130
Cdd:PRK04101  77 DHWYQRLKENDVNIlPGRERDERDKKSIYFTDPDGHKFEFHT 118
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
6-128 5.97e-12

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 58.61  E-value: 5.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737    6 KIIETALYVENLAKARDFYSDTLELEV-------MFESPTLVAFNVGGvSTLLLFKCGAslqtqylSGGEIPPHDAQGRI 78
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLveetdagEEGGLRSAFFLAGG-RVLELLLNET-------PPPAAAGFGGHHIA 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 492089737   79 HvcFAINADQMQPWSDRLAQAKVAIE---GRTEWprGGSSIYFRDPDENLVEL 128
Cdd:pfam00903  73 F--IAFSVDDVDAAYDRLKAAGVEIVrepGRHGW--GGRYSYFRDPDGNLIEL 121
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 14-130 8.87e-12

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: 58.13  E-value: 8.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737  14 VENLAKARDFYSDTLELEVMFESPTLVAFNVGGVSTLLlfkcgaSLQTQylsggeIPPHD-AQGRIHVCFAINADQMQPW 92
Cdd:cd08363    8 VSNLNKSIAFYKDVLDAKLLVLGEKTAYFDLNGLWLAL------NVQED------IPRNEiSHSYTHIAFSIDEEDLDAF 75

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 492089737  93 SDRLAQAKVAI-EGRTEWPRGGSSIYFRDPDENLVELLT 130
Cdd:cd08363   76 KERLKDNGVNIlEGRKRDILEGQSIYFTDPDGHLFELHT 114
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 12-128 3.21e-10

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: 53.77  E-value: 3.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737  12 LYVENLAKARDFYSDTLELEVMFESPTLVAFNVGGVSTLLLFKcgaslqtqylsGGEIPPHDAQ---GRIHVCFAINA-- 86
Cdd:cd07253    9 LTVKDIERTIDFYTKVLGMTVVTFKEGRKALRFGNQKINLHQK-----------GKEFEPKASAptpGSADLCFITETpi 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 492089737  87 DQMQpwsDRLAQAKVAIEGRTEwPRGGS-----SIYFRDPDENLVEL 128
Cdd:cd07253   78 DEVL---EHLEACGVTIEEGPV-KRTGAlgpilSIYFRDPDGNLIEL 120
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 10-131 6.17e-09

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: 50.41  E-value: 6.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737  10 TALYVENLAKARDFYSDTLELEVMFESPTlvafnvGGVSTLLLFKCGASLQTQYLSGGEIPPHDAQGRIHVCFaiNADQM 89
Cdd:cd07264    4 IVLYVDDFAASLRFYRDVLGLPPRFLHEE------GEYAEFDTGETKLALFSRKEMARSGGPDRRGSAFELGF--EVDDV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 492089737  90 QPWSDRLAQAKVAIEG---RTEWprGGSSIYFRDPDENLVELLTP 131
Cdd:cd07264   76 EATVEELVERGAEFVRepaNKPW--GQTVAYVRDPDGNLIEICEP 118
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-129 8.42e-09

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 50.21  E-value: 8.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737   1 MLRLNKIIetaLYVENLAKARDFYSD-TLELEVMFESPTLVAFNVGGVSTLLLFKcGASLQTqyLSGGEIPphDAQGRIH 79
Cdd:COG3607    1 MPRIIFVN---LPVADLERSRAFYEAlGFTFNPQFSDEGAACFVLGEGIVLMLLP-REKFAT--FTGKPIA--DATGFTE 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 492089737  80 VCFAINA------DQMQpwsDRLAQAKVAIEGRTEWPRGGSSIYFRDPDENLVELL 129
Cdd:COG3607   73 VLLALNVesreevDALV---AKALAAGGTVLKPPQDVGGMYSGYFADPDGHLWEVA 125
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 11-128 1.10e-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: 49.62  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737  11 ALYVENLAKARDFYSDTLELEVMfESPTLVA-----FNVGGVSTLLLfkcgasLQTQYLSGGEIPPHDAQGRiHVCFAI- 84
Cdd:cd07245    5 ALACPDLERARRFYTDVLGLEEV-PRPPFLKfggawLYLGGGQQIHL------VVEQNPSELPRPEHPGRDR-HPSFSVp 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 492089737  85 NADQMQpwsDRLAQAKVAIEGRTEWPRGGSSIYFRDPDENLVEL 128
Cdd:cd07245   77 DLDALK---QRLKEAGIPYTESTSPGGGVTQLFFRDPDGNRLEF 117
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 5-131 1.22e-08

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 49.63  E-value: 1.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737   5 NKIIETALYVENLAKARDFYSDTLELEVMFESP---TLVAFNVGGVSTLLLFKcgaslqtqylsggeIPPHDAQGRIHVC 81
Cdd:COG3324    3 GTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGpggDYAEFDTDGGQVGGLMP--------------GAEEPGGPGWLLY 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 492089737  82 FAI-NADQMQpwsDRLAQAKVAIE-GRTEWPRGGSSIYFRDPDENLVELLTP 131
Cdd:COG3324   69 FAVdDLDAAV---ARVEAAGGTVLrPPTDIPPWGRFAVFRDPEGNRFGLWQP 117
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 11-128 3.89e-06

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: 43.07  E-value: 3.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737  11 ALYVENLAKARDFYSDTLELEVMFESPTLVAFNVGGVSTLLLFkcgaslqTQYLSGGEiPPHDAQGRIHVCFAI-NADQM 89
Cdd:cd07255    7 TLKVADLERQSAFYQNVIGLSVLKQNASRAYLGVDGKQVLLVL-------EAIPDAVL-APRSTTGLYHFAILLpDRKAL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 492089737  90 QPWSDRLAQAKVAIegrtewprGGS------SIYFRDPDENLVEL 128
Cdd:cd07255   79 GRALAHLAEHGPLI--------GAAdhgvseAIYLSDPEGNGIEI 115
EhpR_like cd07261
phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter ...
 10-88 5.03e-06

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: 42.77  E-value: 5.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737  10 TALYVENLAKARDFYSDTLELEVMFESPTLVAFNVGGVSTLLLFkcgaslqtqylSGGEIPPHDAQ--GRIHVCFAINAD 87
Cdd:cd07261    2 VILYVDNPERSTEFYRFLLGKEPVESSPTFASFVLSGGAKLGLW-----------SSEEVEPKVAVtgGGAELSFMVPSG 70


                 .
gi 492089737  88 Q 88
Cdd:cd07261   71 E 71
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 12-128 6.75e-06

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: 42.27  E-value: 6.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737  12 LYVENLAKARDFYSDTLELevmfespTLVAFnvggvstlllFKCGAslqtqYLSGGEI--------PPHDAQGRIHVCFA 83
Cdd:cd07244    7 LAVSDLERSLAFYVDLLGF-------KPHVR----------WDKGA-----YLTAGDLwlclsldpAAEPSPDYTHIAFT 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 492089737  84 INADQMQPWSDRLAQAKVAI--EGRTEwprgGSSIYFRDPDENLVEL 128
Cdd:cd07244   65 VSEEDFEELSERLRAAGVKIwqENSSE----GDSLYFLDPDGHKLEL 107
Glyoxalase_2 pfam12681
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 12-128 8.71e-06

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


Pssm-ID: 403776  Cd Length: 118  Bit Score: 42.01  E-value: 8.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737   12 LYVENLAKARDFYSDTLELEVMFESPTLVAFNVggvstlllfkcGASLQTQYLSGGEIPPHDAQGRIHVCFAINADQMQP 91
Cdd:pfam12681   6 LVVKDINISRKFYEDVLDQKIKLDFGENVSFEG-----------GFAIQSDFKELIGIDLSIAEQSNNFELYFEVADVDA 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 492089737   92 WSDRLAQAKVA--IEGRTEWPRGGSSIYFRDPDENLVEL 128
Cdd:pfam12681  75 FLQKIKEIGNIeyLHELKEQPWGQRVFRFYDPDGHIIEI 113
VOC_BsYyaH cd07241
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal ...
 6-128 9.64e-05

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: 39.31  E-value: 9.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737   6 KIIETALYVENLAKARDFYSDTLELEV--MFESPTlVAFNvggvSTLLLFKCGASLQTqyLSGGEIPPHDAQ----GRIH 79
Cdd:cd07241    1 KIEHVALWTNDLERMKDFYVKYFGAESndIYHNKK-KGFR----SYFLTFDSGARLEL--MSRPDVTDPDKEvertGLAH 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492089737  80 VCFAINA----DQMqpwSDRLAQAKVAIEGRTEWPRGGssiYF----RDPDENLVEL 128
Cdd:cd07241   74 IAFSVGSkeavDEL---TERLRADGYAVVGGPRTTGDG---YYesviLDPEGNRIEI 124
FosX cd08364
fosfomycin resistant protein subfamily FosX; This subfamily family contains FosX, a fosfomycin ...
 79-130 2.24e-04

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: 38.41  E-value: 2.24e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 492089737  79 HVCFAINADQMQPWSDRLAQAKVAI-EGRTEWPRGGSSIYFRDPDENLVELLT 130
Cdd:cd08364   68 HIAFKVSEGDLDEYRARIKKLGLEIrPPRSRVQGEGRSLYFYDFDNHLFELHT 120
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 12-130 3.18e-04

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: 37.92  E-value: 3.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737  12 LYVENLAKARDFYSDTLELEVMFESPT-------LVAFNVGGVstlllfkcgaslqtqYLSGGEIPPHDAQGRIHVCFAI 84
Cdd:cd08345    4 LIVRDLEKSTAFLQDIFGAREVYSSGDktfslskEKFFLLGGL---------------WIALMEGESLQERSYTHIAFQI 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 492089737  85 NADQMQPWSDRLAQAKVAI-EGRTEWPRGGSSIYFRDPDENLVELLT 130
Cdd:cd08345   69 QSEDFDRYAERLGALGVEMrPPRPRVEGEGRSIYFYDPDNHLFELHT 115
MhqB_like_N cd08344
N-terminal domain of MhqB, a type I extradiol dioxygenase, and similar proteins; This ...
 7-128 3.25e-04

N-terminal domain of MhqB, a type I extradiol dioxygenase, and similar proteins; This subfamily contains the N-terminal, non-catalytic, domain of Burkholderia sp. NF100 MhqB and similar proteins. MhqB is a type I extradiol dioxygenase involved in the catabolism of methylhydroquinone, an intermediate in the degradation of fenitrothion. The purified enzyme has shown extradiol ring cleavage activity toward 3-methylcatechol. Fe2+ was suggested as a cofactor, the same as most other enzymes in the family. Burkholderia sp. NF100 MhqB is encoded on the plasmid pNF1. The type I family of extradiol dioxygenases contains two structurally homologous barrel-shaped domains at the N- and C-terminal. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism.


Pssm-ID: 319932  Cd Length: 112  Bit Score: 37.78  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089737   7 IIETALYVENLAKARDFYsDTLELEVMFESPTLVAFNVGGVSTLLLFKCGASLQTQYLSggeipphdaqgrihvcFAINA 86
Cdd:cd08344    3 IDHFALEVPDLEVARRFY-EAFGLDVRETGEDLELRAPGNDHVWARLIQGARKRLAYLS----------------FGIFG 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 492089737  87 DQMQPWSDRLAQAKVAiegRTEWPRGG--SSIYFRDPDENLVEL 128
Cdd:cd08344   66 DDLARFAAHLDAAGVA---LIAAPPGAdpDGVWFEDPDGNLLQV 106
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 10-37 3.31e-03

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


Pssm-ID: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 34.97  E-value: 3.31e-03
                         10        20
                 ....*....|....*....|....*...
gi 492089737  10 TALYVENLAKARDFYSDTLELEVMFESP 37
Cdd:cd07263    2 VMLYVDDQDKALDFYVEKLGFEVVEDVP 29
ChaP_like cd08351
ChaP, an enzyme involved in the biosynthesis of the antitumor agent chartreusin (cha), and ...
 65-130 4.50e-03

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: 34.79  E-value: 4.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492089737  65 SGGEIPPHdaqgriHVCFAINADQMQPWSDRLAQAKVAI--------EGRTEWPRGGSSIYFRDPDENLVELLT 130
Cdd:cd08351   51 PRGEIAPQ------HYAFLVSDDEFDAILARIRARGLEYwadpqhrePGEINHNDGGRGVYFRDPDGHLLEILT 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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