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Conserved domains on  [gi|653730313|ref|WP_027668007|]
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MULTISPECIES: glyoxalase/bleomycin resistance/extradiol dioxygenase family protein [Rhizobium]

Protein Classification

VOC family protein( domain architecture ID 10006588)

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

CATH:  3.10.180.70
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
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
21-138 1.17e-46

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


:

Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 146.92  E-value: 1.17e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313  21 PYLTVDGAVKAAEFYKKAFGAEEAYLVPvDESGRTMHVHLYINGSSLMLSDAYPDygHPFKGHEGFAIQLIIDDIDFWWD 100
Cdd:COG2764    4 PYLVVDDAEEALEFYEDVFGFEVVFRMT-DPDGKIMHAELRIGGSVLMLSDAPPD--SPAAEGNGVSLSLYVDDVDALFA 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 653730313 101 RAVAAGAEVVMPVELMFWGDRYGQLRDPFGVLWGLNAP 138
Cdd:COG2764   81 RLVAAGATVVMPLQDTFWGDRFGMVRDPFGVLWMINTP 118
 
Name Accession Description Interval E-value
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
21-138 1.17e-46

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 146.92  E-value: 1.17e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313  21 PYLTVDGAVKAAEFYKKAFGAEEAYLVPvDESGRTMHVHLYINGSSLMLSDAYPDygHPFKGHEGFAIQLIIDDIDFWWD 100
Cdd:COG2764    4 PYLVVDDAEEALEFYEDVFGFEVVFRMT-DPDGKIMHAELRIGGSVLMLSDAPPD--SPAAEGNGVSLSLYVDDVDALFA 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 653730313 101 RAVAAGAEVVMPVELMFWGDRYGQLRDPFGVLWGLNAP 138
Cdd:COG2764   81 RLVAAGATVVMPLQDTFWGDRFGMVRDPFGVLWMINTP 118
VOC_like cd07246
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 21-138 5.68e-42

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: 319910 [Multi-domain]  Cd Length: 124  Bit Score: 135.12  E-value: 5.68e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313  21 PYLTVDGAVKAAEFYKKAFGAEEAYLVPvDESGRTMHVHLYINGSSLMLSDAYPDYGH--PFKGH-EGFAIQLIIDDIDF 97
Cdd:cd07246    5 PYLVVEDAAAAIAFYKKAFGAEELGRTT-QEDGRVGHAELRIGGTVVMVADENPERGAlsPTKLGgTPVIFHLYVEDVDA 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 653730313  98 WWDRAVAAGAEVVMPVELMFWGDRYGQLRDPFGVLWGLNAP 138
Cdd:cd07246   84 TFARAVAAGAVVVEPVEDQFWGDRVGKVKDPFGHVWWLATP 124
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
23-133 2.36e-20

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 80.18  E-value: 2.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313   23 LTVDGAVKAAEFYKKAFGAEEAYLVPVDESGRTMHVHLYINGSSLMLSDAY-PDYGHPFKGHEGFAIQLI-IDDIDFWWD 100
Cdd:pfam00903   7 LRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLNEtPPPAAAGFGGHHIAFIAFsVDDVDAAYD 86

                          90       100       110
                  ....*....|....*....|....*....|...
gi 653730313  101 RAVAAGAEVVMPVELMFWGDRYGQLRDPFGVLW 133
Cdd:pfam00903  87 RLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLI 119
PRK10148 PRK10148
VOC family metalloprotein YjdN;
19-137 4.20e-12

VOC family metalloprotein YjdN;


Pssm-ID: 236656  Cd Length: 147  Bit Score: 59.53  E-value: 4.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313  19 LLPYLTVDG-AVKAAEFYKKAFGAEEAYLVPVDE-------------SGRTM------HVHLYINGSSLMLSDAYPDygh 78
Cdd:PRK10148   3 LSPYLSFAGnCADAIAYYQQTLGAELLYKISFGEmpksaqdseegcpSGMQFpdtaiaHANVRIAGSDIMMSDAIPS--- 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 653730313  79 PFKGHEGFAIQLIIDDID---FWWDrAVAAGAEVVMPVELMFWGDRYGQLRDPFGVLWGLNA 137
Cdd:PRK10148  80 GKAHYSGFTLVLDTQDVEegkRWFD-NLAANGKIEMAWQETFWAHGFGKVTDKFGVPWMINV 140
 
Name Accession Description Interval E-value
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
21-138 1.17e-46

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 146.92  E-value: 1.17e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313  21 PYLTVDGAVKAAEFYKKAFGAEEAYLVPvDESGRTMHVHLYINGSSLMLSDAYPDygHPFKGHEGFAIQLIIDDIDFWWD 100
Cdd:COG2764    4 PYLVVDDAEEALEFYEDVFGFEVVFRMT-DPDGKIMHAELRIGGSVLMLSDAPPD--SPAAEGNGVSLSLYVDDVDALFA 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 653730313 101 RAVAAGAEVVMPVELMFWGDRYGQLRDPFGVLWGLNAP 138
Cdd:COG2764   81 RLVAAGATVVMPLQDTFWGDRFGMVRDPFGVLWMINTP 118
VOC_like cd07246
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 21-138 5.68e-42

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: 319910 [Multi-domain]  Cd Length: 124  Bit Score: 135.12  E-value: 5.68e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313  21 PYLTVDGAVKAAEFYKKAFGAEEAYLVPvDESGRTMHVHLYINGSSLMLSDAYPDYGH--PFKGH-EGFAIQLIIDDIDF 97
Cdd:cd07246    5 PYLVVEDAAAAIAFYKKAFGAEELGRTT-QEDGRVGHAELRIGGTVVMVADENPERGAlsPTKLGgTPVIFHLYVEDVDA 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 653730313  98 WWDRAVAAGAEVVMPVELMFWGDRYGQLRDPFGVLWGLNAP 138
Cdd:cd07246   84 TFARAVAAGAVVVEPVEDQFWGDRVGKVKDPFGHVWWLATP 124
PhnB_like cd06588
Escherichia coli PhnB and similar proteins; The Escherichia coli phnB gene is found next to an ...
 21-136 3.52e-26

Escherichia coli PhnB and similar proteins; The Escherichia coli phnB gene is found next to an operon of fourteen genes (phnC-to-phnP) related to the cleavage of carbon-phosphorus (C-P) bonds in unactivated alkylphosphonates, supporting bacterial growth on alkylphosphonates as the sole phosphorus source. It was originally considered part of that operon. PhnB appears to play no direct catalytic role in the usage of alkylphosphonate. Although many of the proteins in this family have been annotated as 3-demethylubiquinone-9 3-methyltransferase enzymes by automatic annotation programs, the experimental evidence for this assignment is lacking. In Escherichia coli, the gene coding 3-demethylubiquinone-9 3-methyltransferase enzyme is ubiG, which belongs to the AdoMet-MTase protein family. PhnB-like proteins adopt a structural fold similar to bleomycin resistance proteins, glyoxalase I, and type I extradiol dioxygenases.


Pssm-ID: 319899  Cd Length: 129  Bit Score: 95.42  E-value: 3.52e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313  21 PYLTVDG-AVKAAEFYKKAFGA----------EEAYLVPVDESGRTMHVHLYINGSSLMLSDAYPDygHPFKGHEGFAIQ 89
Cdd:cd06588    3 PYLWFNGnAEEALEFYAEVFPGgeilsltrygEGPPDFPEGDEGKVMHAEFTLGGQTLMASDDGPG--FPFTFGNAISLS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 653730313  90 LIIDD---IDFWWDrAVAAGAEVVMPVELMFWGDRYGQLRDPFGVLWGLN 136
Cdd:cd06588   81 VDCDSqeeADRLFE-KLSEGGEVLMPLQETFWGARYGWVKDKFGVSWQIN 129
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
23-133 2.36e-20

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 80.18  E-value: 2.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313   23 LTVDGAVKAAEFYKKAFGAEEAYLVPVDESGRTMHVHLYINGSSLMLSDAY-PDYGHPFKGHEGFAIQLI-IDDIDFWWD 100
Cdd:pfam00903   7 LRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLNEtPPPAAAGFGGHHIAFIAFsVDDVDAAYD 86

                          90       100       110
                  ....*....|....*....|....*....|...
gi 653730313  101 RAVAAGAEVVMPVELMFWGDRYGQLRDPFGVLW 133
Cdd:pfam00903  87 RLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLI 119
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 23-138 1.09e-14

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: 65.78  E-value: 1.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313  23 LTVDGAVKAAEFYKKAFGAEEAYLVPVDEsGRTMHVHLYI-NGSSLMLsdAYPDYGHPFKGHEGFA-IQLIIDDIDFWWD 100
Cdd:COG0346    8 LRVSDLEASLAFYTDVLGLELVKRTDFGD-GGFGHAFLRLgDGTELEL--FEAPGAAPAPGGGGLHhLAFRVDDLDAAYA 84

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 653730313 101 RAVAAGAEVVMPVELMFWGDRYGQLRDPFGVLWGLNAP 138
Cdd:COG0346   85 RLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVEP 122
TioX_like cd08355
Micromonospora sp. TioX and similar proteins; Micromonospora sp. TioX is encoded by a gene of ...
 19-133 1.75e-14

Micromonospora sp. TioX and similar proteins; Micromonospora sp. TioX is encoded by a gene of the thiocoraline biosynthetic gene cluster. Thiocoraline is a thiodepsipeptide with potent antitumor activity. TioX may be involved in thiocoraline resistance or secretion. TioX belongs to vicinal oxygen chelate (VOC) superfamily that 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: 319943  Cd Length: 123  Bit Score: 65.13  E-value: 1.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313  19 LLPYLTVDGAVKAAEFYKKAFGAEEAYLVPVDEsGRTMHVHLYINGSSLMLS----DAYPDYGHPFKGHEGFAIQLIIDD 94
Cdd:cd08355    1 VVPTLRYRDAVAAIDWLVEAFGFEERMVVPGDE-GTIHHAELTFGGGGVMVGsvrdEARPDRPADAGGHGTQSVYVAVAD 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 653730313  95 IDFWWDRAVAAGAEVVMPVELMFWGDRYGQLRDPFGVLW 133
Cdd:cd08355   80 PDAHYERARAAGAEIVMEPTDTDYGSRDYSARDPEGHLW 118
PRK10148 PRK10148
VOC family metalloprotein YjdN;
19-137 4.20e-12

VOC family metalloprotein YjdN;


Pssm-ID: 236656  Cd Length: 147  Bit Score: 59.53  E-value: 4.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313  19 LLPYLTVDG-AVKAAEFYKKAFGAEEAYLVPVDE-------------SGRTM------HVHLYINGSSLMLSDAYPDygh 78
Cdd:PRK10148   3 LSPYLSFAGnCADAIAYYQQTLGAELLYKISFGEmpksaqdseegcpSGMQFpdtaiaHANVRIAGSDIMMSDAIPS--- 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 653730313  79 PFKGHEGFAIQLIIDDID---FWWDrAVAAGAEVVMPVELMFWGDRYGQLRDPFGVLWGLNA 137
Cdd:PRK10148  80 GKAHYSGFTLVLDTQDVEegkRWFD-NLAANGKIEMAWQETFWAHGFGKVTDKFGVPWMINV 140
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 30-140 1.65e-10

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 54.64  E-value: 1.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313  30 KAAEFYKKAFGAEEAYLVPVDESGRTMHVHLYINGSsLMLSDAYPDYGHPfkghegfAIQLIIDDIDFWWDRAVAAGAEV 109
Cdd:COG3324   17 RAKAFYEEVFGWTFEDDAGPGGDYAEFDTDGGQVGG-LMPGAEEPGGPGW-------LLYFAVDDLDAAVARVEAAGGTV 88

                         90       100       110
                 ....*....|....*....|....*....|.
gi 653730313 110 VMPVELMFWGDRYGQLRDPFGVLWGLNAPSK 140
Cdd:COG3324   89 LRPPTDIPPWGRFAVFRDPEGNRFGLWQPAA 119
VOC_like cd08359
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 31-132 6.68e-07

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: 319947 [Multi-domain]  Cd Length: 119  Bit Score: 45.08  E-value: 6.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313  31 AAEFYKKAFGAEEAYlvpvdESGRTMHVHLYI-NGSSLMLSD----AYPDYGHPFKGheGFAIQLIIDDIDFWWDRAVAA 105
Cdd:cd08359   15 TAAFYVKHFGFRVIF-----DSDWYVSLRRAErHGFELAIMDgqhgAVPAASQTQSS--GLIINFEVDDADAEYERLTQA 87

                         90       100
                 ....*....|....*....|....*..
gi 653730313 106 GAEVVMPVELMFWGDRYGQLRDPFGVL 132
Cdd:cd08359   88 GLEFLEPPRDEPWGQRRFIVRDPNGVL 114
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 23-132 7.63e-07

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: 45.02  E-value: 7.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313  23 LTVDGAVKAAEFYKKAFGAEEAYLVPVDESGR--TMHVHLYINGSSLMLSDAYPDYGHPfkgheGFAIQLIIDDIDFWWD 100
Cdd:cd07264    6 LYVDDFAASLRFYRDVLGLPPRFLHEEGEYAEfdTGETKLALFSRKEMARSGGPDRRGS-----AFELGFEVDDVEATVE 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 653730313 101 RAVAAGAEVVMPVELMFWGDRYGQLRDPFGVL 132
Cdd:cd07264   81 ELVERGAEFVREPANKPWGQTVAYVRDPDGNL 112
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 23-133 2.87e-05

vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases.


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 40.59  E-value: 2.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313  23 LTVDGAVKAAEFYKKAFGAEeayLVPVDESGRTMHVHLYiNGSSLMLSDAYPDYGHPFKGHEGFAIQL-IIDDIDFWWDR 101
Cdd:cd06587    4 LRVPDLDASVAFYEEVLGFE---VVSRNEGGGFAFLRLG-PGLRLALLEGPEPERPGGGGLFHLAFEVdDVDEVDERLRE 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 653730313 102 AVAAGaEVVMPVELMFWGDRYGQLRDPFGVLW 133
Cdd:cd06587   80 AGAEG-ELVAPPVDDPWGGRSFYFRDPDGNLI 110
VOC_CChe_VCA0619_like cd08356
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; uncharacterized subfamily of ...
 84-133 2.89e-05

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; uncharacterized subfamily of vicinal oxygen chelate (VOC) family contains Vibrio cholerae VCA0619 and similar proteins. The 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: 319944  Cd Length: 113  Bit Score: 40.75  E-value: 2.89e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 653730313  84 EGFAIQLIIDDIDFWWDRAVAAGAE-----VVMPVELMFWGDRYGQLRDPFGVLW 133
Cdd:cd08356   55 ENFMMHLLVEDVDAWHQHVKTLGLAerygvKVTDPTDQPWGMRDFVLTDPSGVLW 109
PsjN_like cd16356
Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme ...
 32-130 3.79e-05

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: 40.48  E-value: 3.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313  32 AEFYKKAFGAEEaylvpVDESGRTMHVHLYINGSSLMLS--DAYPDYGHP-FKGHEGFAIQLIID-----DIDFWWDRAV 103
Cdd:cd16356   13 SDFYSELFGLEE-----IFEIRSPIFRGLRTGDSCLGFNapEAYELLGLPeFSDTPGIRILLTFDvddveAVDRLVPRAA 87

                         90       100
                 ....*....|....*....|....*..
gi 653730313 104 AAGAEVVMPVELMFWGDRYGQLRDPFG 130
Cdd:cd16356   88 ALGATLIKPPYDTYYGWYQAVLLDPEG 114
3-dmu-9_3-mt pfam06983
3-demethylubiquinone-9 3-methyltransferase; This family represents a conserved region ...
 21-133 5.74e-05

3-demethylubiquinone-9 3-methyltransferase; This family represents a conserved region approximately 100 residues long within a number of bacterial and archaeal 3-demethylubiquinone-9 3-methyltransferases (EC:2.1.1.64). Note that some family members contain more than one copy of this region, and that many members are hypothetical proteins.


Pssm-ID: 399756  Cd Length: 116  Bit Score: 39.98  E-value: 5.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313   21 PYLTVDG-AVKAAEFYKKAF-----GAEEAYlvPVDE---SGRTMHVHLYINGSSLMLSDAypdyGHPFKGHEGFAIQLI 91
Cdd:pfam06983   5 PCLWFDGqAEEAAEFYVSLFpnseiGSVNRY--PEDGpgkPGSVLTVEFTLNGQPFIALNG----GPNFKFNEAVSFQVT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 653730313   92 IDD---IDFWWDRAVAAGAEvvmpvelmfwGDRYGQLRDPFGVLW 133
Cdd:pfam06983  79 CKDqeeVDRYWNALSENGGP----------ESQCGWLKDKFGVSW 113
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 23-130 8.81e-05

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: 40.01  E-value: 8.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313  23 LTVDGAVKAAEFYKKAFGAEEAY-LVPVDESGRTMHVHLY---------INGSSLMLSD---------AYPDYGHPFK-- 81
Cdd:cd16361    7 ITVPDLDAAVEFYTDVLGAEVVYrSTPLAEGDRGGGEMRAagfvpgfarARIAMLRLGPgpgielfeyKGPEQRAPVPrn 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 653730313  82 ---GHEGFAIQliIDDIDFWWDRAVAAGAEVVMPVELMFW-----GDRYGQLRDPFG 130
Cdd:cd16361   87 sdvGIFHFALQ--VDDVEAAAERLAAAGGKVLMGPREIPDggpgkGNRMVYLRDPWG 141
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 23-135 1.30e-04

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: 38.78  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313  23 LTVDGAVKAAEFYKKAFGAEeayLVPVDESGRTMHVhLYING---SSLMLSDAYPDYGHPfkgheGFAIQLIIDDIDFWW 99
Cdd:cd07247    6 LPTTDLERAKAFYGAVFGWT---FEDEGDGGGDYAL-FTAGGgavGGLMRAPEEVAGAPP-----GWLIYFAVDDLDAAL 76

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 653730313 100 DRAVAAGAEVVMPVELMFWGDRYGQLRDPFGVLWGL 135
Cdd:cd07247   77 ARVEAAGGKVVVPPTDIPGGGRFAVFADPEGNRFGL 112
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 23-135 3.39e-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: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 38.05  E-value: 3.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313  23 LTVDGAVKAAEFYKKAFGAEEAYLVPVDEsgrtmhvHLYI-------NGSSLMLSDAYPDYGHPF----KGHEGfAIQLI 91
Cdd:cd07263    4 LYVDDQDKALDFYVEKLGFEVVEDVPMGG-------MRWVtvappgsPGTSLLLEPKAHPAQMPQspeaAGGTP-GILLA 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 653730313  92 IDDIDFWWDRAVAAGAEVVMPVELMFWGdRYGQLRDPFGVLWGL 135
Cdd:cd07263   76 TDDIDATYERLTAAGVTFVQEPTQMGGG-RVANFRDPDGNLFAL 118
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 21-130 1.21e-03

Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance protein, confers Bm resistance by directly binding to Bm. Bm is a glycopeptide antibiotic produced naturally by actinomycetes. It is a potent anti-cancer drug, which acts as a strong DNA-cutting agent, thereby causing cell death. BLMA is produced by actinomycetes to protect themselves against their own lethal compound. BLMA has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMAs are dimers and each dimer binds to two Bm molecules at the Bm-binding pockets formed at the dimer interface; two Bm molecules are bound per dimer. BLMA 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. As for the larger superfamily, this family contains members with or without domain swapping.


Pssm-ID: 319937 [Multi-domain]  Cd Length: 114  Bit Score: 36.43  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653730313  21 PYLTVDGAVKAAEFYKKAFGAEEAYLVPVDESGRtmhvhLYINGSSLMLSdAYPDYGhPFKGheGFAIQLIIDDIDFWWD 100
Cdd:cd08349    2 PILPVRDIDKTLAFYVDVLGFEVDYERPPPGYAI-----LSRGGVELHLF-EHPGLD-PAGS--GVAAYIRVEDIDALHA 72

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 653730313 101 RAVAAG-----AEVVMPVELMFWGDRYGQLRDPFG 130
Cdd:cd08349   73 ELKAAGlplfgIPRITPIEDKPWGMREFAVVDPDG 107
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 93-133 7.80e-03

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 34.42  E-value: 7.80e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 653730313  93 DDIDFWWDRAVAAGAEVVMPVELMFWGdRYGQLRDPFGVLW 133
Cdd:COG3607   83 EEVDALVAKALAAGGTVLKPPQDVGGM-YSGYFADPDGHLW 122
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 93-133 8.20e-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: 319914 [Multi-domain]  Cd Length: 120  Bit Score: 34.19  E-value: 8.20e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 653730313  93 DDIDFWWDRAVAAGAEVVMPVELMFWGDRYGQLRDPFGVLW 133
Cdd:cd07251   75 EEVDQLLAKAVAAGGKILKPPQEVFWGGYSGYFADPDGHIW 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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