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Conserved domains on  [gi|960858405|ref|WP_058336799|]
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MULTISPECIES: VOC family protein [Bacillus]

Protein Classification

VOC family protein( domain architecture ID 10163567)

vicinal oxygen chelate (VOC) family protein uses a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms; similar to type I extradiol dioxygenase, glyoxalase I and a group of antibiotic resistance proteins such as Staphylococcus aureus bleomycin resistance protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-121 1.92e-39

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: 128.22  E-value: 1.92e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   3 MKYTILYVNDVEASIQFYHHILGFPIKLRVES--YVEFDTGEVTLSINSRQDVKESLGlpvpeAVSSSQTFEIGFVVDDV 80
Cdd:cd07264    1 IAYIVLYVDDFAASLRFYRDVLGLPPRFLHEEgeYAEFDTGETKLALFSRKEMARSGG-----PDRRGSAFELGFEVDDV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 960858405  81 NETIASLKEKGVPVIKEPAKKPWGQTVSYVSDPDGHFIEIC 121
Cdd:cd07264   76 EATVEELVERGAEFVREPANKPWGQTVAYVRDPDGNLIEIC 116
 
Name Accession Description Interval E-value
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-121 1.92e-39

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: 128.22  E-value: 1.92e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   3 MKYTILYVNDVEASIQFYHHILGFPIKLRVES--YVEFDTGEVTLSINSRQDVKESLGlpvpeAVSSSQTFEIGFVVDDV 80
Cdd:cd07264    1 IAYIVLYVDDFAASLRFYRDVLGLPPRFLHEEgeYAEFDTGETKLALFSRKEMARSGG-----PDRRGSAFELGFEVDDV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 960858405  81 NETIASLKEKGVPVIKEPAKKPWGQTVSYVSDPDGHFIEIC 121
Cdd:cd07264   76 EATVEELVERGAEFVREPANKPWGQTVAYVRDPDGNLIEIC 116
Glyoxalase_2 pfam12681
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 3-125 2.42e-30

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


Pssm-ID: 403776  Cd Length: 118  Bit Score: 105.19  E-value: 2.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405    3 MKYTILYVNDVEASIQFYHHILGFPIKLRVESYVEFDTGevtLSInsRQDVKESLGLPVPEAVSSSQtFEIGFVVDDVNE 82
Cdd:pfam12681   1 FKCPLLVVKDINISRKFYEDVLDQKIKLDFGENVSFEGG---FAI--QSDFKELIGIDLSIAEQSNN-FELYFEVADVDA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 960858405   83 TIASLKE-KGVPVIKEPAKKPWGQTVSYVSDPDGHFIEICDAVS 125
Cdd:pfam12681  75 FLQKIKEiGNIEYLHELKEQPWGQRVFRFYDPDGHIIEIGESME 118
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-121 1.43e-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: 1.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   1 MKMKYTILYVNDVEASIQFYHHILGFPIKLRVEsYVEFDTGEVTLSINSRQDvkesLGLPVPEAVSSSQT----FEIGFV 76
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTD-FGDGGFGHAFLRLGDGTE----LELFEAPGAAPAPGggglHHLAFR 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 960858405  77 VDDVNETIASLKEKGVPVIKEPAKKPWGQTVSYVSDPDGHFIEIC 121
Cdd:COG0346   76 VDDLDAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELV 120
PLN02367 PLN02367
lactoylglutathione lyase
 3-122 7.15e-07

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 46.15  E-value: 7.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   3 MKYTILYVNDVEASIQFYHHILGFPIKLRVEsyveFDTGEVTLSINSRQDVKESLGLPVPEAV---SSSQTFE------- 72
Cdd:PLN02367  76 MQQTMYRIKDPKASLDFYSRVLGMSLLKRLD----FPEMKFSLYFMGYEDTASAPTDPTERTVwtfGQKATIElthnwgt 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 960858405  73 ---------------------IGFVVDDVNETIASLKEKGVPVIKEPAKKPWgQTVSYVSDPDGHFIEICD 122
Cdd:PLN02367 152 esdpdfkgyhngnseprgfghIGITVDDVYKACERFEELGVEFVKKPNDGKM-KGIAFIKDPDGYWIEIFD 221
 
Name Accession Description Interval E-value
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-121 1.92e-39

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: 128.22  E-value: 1.92e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   3 MKYTILYVNDVEASIQFYHHILGFPIKLRVES--YVEFDTGEVTLSINSRQDVKESLGlpvpeAVSSSQTFEIGFVVDDV 80
Cdd:cd07264    1 IAYIVLYVDDFAASLRFYRDVLGLPPRFLHEEgeYAEFDTGETKLALFSRKEMARSGG-----PDRRGSAFELGFEVDDV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 960858405  81 NETIASLKEKGVPVIKEPAKKPWGQTVSYVSDPDGHFIEIC 121
Cdd:cd07264   76 EATVEELVERGAEFVREPANKPWGQTVAYVRDPDGNLIEIC 116
Glyoxalase_2 pfam12681
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 3-125 2.42e-30

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


Pssm-ID: 403776  Cd Length: 118  Bit Score: 105.19  E-value: 2.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405    3 MKYTILYVNDVEASIQFYHHILGFPIKLRVESYVEFDTGevtLSInsRQDVKESLGLPVPEAVSSSQtFEIGFVVDDVNE 82
Cdd:pfam12681   1 FKCPLLVVKDINISRKFYEDVLDQKIKLDFGENVSFEGG---FAI--QSDFKELIGIDLSIAEQSNN-FELYFEVADVDA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 960858405   83 TIASLKE-KGVPVIKEPAKKPWGQTVSYVSDPDGHFIEICDAVS 125
Cdd:pfam12681  75 FLQKIKEiGNIEYLHELKEQPWGQRVFRFYDPDGHIIEIGESME 118
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-121 1.43e-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: 1.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   1 MKMKYTILYVNDVEASIQFYHHILGFPIKLRVEsYVEFDTGEVTLSINSRQDvkesLGLPVPEAVSSSQT----FEIGFV 76
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTD-FGDGGFGHAFLRLGDGTE----LELFEAPGAAPAPGggglHHLAFR 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 960858405  77 VDDVNETIASLKEKGVPVIKEPAKKPWGQTVSYVSDPDGHFIEIC 121
Cdd:COG0346   76 VDDLDAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELV 120
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-120 9.93e-23

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 85.58  E-value: 9.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405    2 KMKYTILYVNDVEASIQFYHHILGFPIKLRVE-------SYVEFDTGEVTLSINSRQDVKESLGLPVPEAVSSsqtfeIG 74
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDageegglRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAF-----IA 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 960858405   75 FVVDDVNETIASLKEKGVPVIKEPAKKPWGQTVSYVSDPDGHFIEI 120
Cdd:pfam00903  76 FSVDDVDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
5-121 1.46e-21

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 82.60  E-value: 1.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   5 YTILYVNDVEASIQFYHHILGFPIKLRVES------YVEFDTGEVTLSINSRQDvkeslGLPVPEAvsssQTFEIGFVVD 78
Cdd:COG2764    3 TPYLVVDDAEEALEFYEDVFGFEVVFRMTDpdgkimHAELRIGGSVLMLSDAPP-----DSPAAEG----NGVSLSLYVD 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 960858405  79 DVNETIASLKEKGVPVIKEPAKKPWGQTVSYVSDPDGHFIEIC 121
Cdd:COG2764   74 DVDALFARLVAAGATVVMPLQDTFWGDRFGMVRDPFGVLWMIN 116
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-121 1.03e-18

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 75.44  E-value: 1.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   1 MKMKYTILYVNDVEASIQFYHHILGFPIKLRVES---YVEFDTGEVtlsinsrqdvkESLGLPVPEAVSSSQTFEIGFVV 77
Cdd:COG3324    3 GTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPggdYAEFDTDGG-----------QVGGLMPGAEEPGGPGWLLYFAV 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 960858405  78 DDVNETIASLKEKGVPVIKEPAK-KPWGqTVSYVSDPDGHFIEIC 121
Cdd:COG3324   72 DDLDAAVARVEAAGGTVLRPPTDiPPWG-RFAVFRDPEGNRFGLW 115
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-120 1.67e-17

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: 72.33  E-value: 1.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   8 LYVNDVEASIQFYHHiLGFPIKLRVE-SYVEFDTGEVTLSINSRQDVKESLGLPVPEAVSSSQTfeIGFVV---DDVNET 83
Cdd:cd07251    4 LGVRDLERSARFYEA-LGWKPNLDPNdGVVFFQLGGTVLALYPRDALAEDAGVSVTGAGFSGVT--LAHNVrsrEEVDQL 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 960858405  84 IASLKEKGVPVIKEPAKKPWGQTVSYVSDPDGHFIEI 120
Cdd:cd07251   81 LAKAVAAGGKILKPPQEVFWGGYSGYFADPDGHIWEV 117
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 5-120 3.54e-17

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: 71.40  E-value: 3.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   5 YTILYVNDVEASIQFYHHILGFPIKLRVES--YVEFDTGE-VTLSINSRQDVKESLGLPVpeavsssqtFEIGFVVDDVN 81
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGggFAFLRLGPgLRLALLEGPEPERPGGGGL---------FHLAFEVDDVD 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 960858405  82 ETIASLKEKGV--PVIKEPAKKPWGQTVSYVSDPDGHFIEI 120
Cdd:cd06587   72 EVDERLREAGAegELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
EhpR_like cd07261
phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter ...
 6-121 1.01e-16

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: 70.12  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   6 TILYVNDVEASIQFYHHILGFPIKLRVESYVEFDTGE-VTLSINSRQDVKeslglpvPEAVSSSQTFEIGFVV---DDVN 81
Cdd:cd07261    2 VILYVDNPERSTEFYRFLLGKEPVESSPTFASFVLSGgAKLGLWSSEEVE-------PKVAVTGGGAELSFMVpsgEQVD 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 960858405  82 ETIASLKEKGVPVIKEPAKKPWGQTVSyVSDPDGHFIEIC 121
Cdd:cd07261   75 EVYAEWKAMGIPIIQEPTTMDFGYTFV-ATDPDGHRLRVC 113
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-120 1.03e-16

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 70.24  E-value: 1.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   1 MKMKYTILYVNDVEASIQFYHHiLGFPIKLRV--ESYVEFDTGE-VTLSINSRQDVKESLGLPVPEAVSSSQtFEIGFVV 77
Cdd:COG3607    2 PRIIFVNLPVADLERSRAFYEA-LGFTFNPQFsdEGAACFVLGEgIVLMLLPREKFATFTGKPIADATGFTE-VLLALNV 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 960858405  78 D---DVNETIASLKEKGVPVIKEPAKKPWGQTvSYVSDPDGHFIEI 120
Cdd:COG3607   80 EsreEVDALVAKALAAGGTVLKPPQDVGGMYS-GYFADPDGHLWEV 124
VOC_like cd09011
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 1-120 1.11e-14

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


Pssm-ID: 319953  Cd Length: 122  Bit Score: 65.18  E-value: 1.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   1 MKMKYTILYVNDVEASIQFYHHILGFPIKLRVESYVEFDTGevtLSINSRQDVKESLGLPVPEAVSSSQTFEIGFVVDDV 80
Cdd:cd09011    1 MKFVNPLLVVKDIEKSKKFYEDVLGQKILLDFGENVVFEGG---FALQEKKSWLETIIISDLSIKQQSNNFELYFEVDDF 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 960858405  81 NETIASLKE-KGVPVIKEPAKKPWGQTVSYVSDPDGHFIEI 120
Cdd:cd09011   78 DAFFEKLNPhKDIEFIHPILEHPWGQRVFRFYDPDGHIIEI 118
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
1-120 2.33e-14

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 64.59  E-value: 2.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   1 MKMKYTILYVNDVEASIQFYHHILGFPIKLRVESYVEF--DTGEVTLsinsrqDVKESLGLPVPEAVSSSqtFEIGFVVD 78
Cdd:COG2514    2 TRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLraDGGEHLL------VLEEAPGAPPRPGAAGL--DHVAFRVP 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 960858405  79 DVNE---TIASLKEKGVPVikEPAKKPWGQTVSYVSDPDGHFIEI 120
Cdd:COG2514   74 SRADldaALARLAAAGVPV--EGAVDHGVGESLYFRDPDGNLIEL 116
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 6-121 1.11e-13

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: 62.31  E-value: 1.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   6 TILYVNDVEASIQFYHHILGFPIKLRVEsyvefDTGEVTLSINSRQDVKESLGLpVPEAVSSSQTFE---------IGFV 76
Cdd:cd07263    2 VMLYVDDQDKALDFYVEKLGFEVVEDVP-----MGGMRWVTVAPPGSPGTSLLL-EPKAHPAQMPQSpeaaggtpgILLA 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 960858405  77 VDDVNETIASLKEKGVPVIKEPAKKPWGqTVSYVSDPDGHFIEIC 121
Cdd:cd07263   76 TDDIDATYERLTAAGVTFVQEPTQMGGG-RVANFRDPDGNLFALM 119
PsjN_like cd16356
Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme ...
 5-120 1.97e-12

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: 59.36  E-value: 1.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   5 YTILYVNDVEASIQFYHHILGFP--IKLRVESYVEFDTGEVTLSINSRQDVkESLGLPVPEAVSSS---QTFEIgFVVDD 79
Cdd:cd16356    1 YVNIFTADIVALSDFYSELFGLEeiFEIRSPIFRGLRTGDSCLGFNAPEAY-ELLGLPEFSDTPGIrilLTFDV-DDVEA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 960858405  80 VNETIASLKEKGVPVIKEPAKKPWGQTVSYVSDPDGHFIEI 120
Cdd:cd16356   79 VDRLVPRAAALGATLIKPPYDTYYGWYQAVLLDPEGNVFRI 119
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 6-120 5.81e-12

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: 58.15  E-value: 5.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   6 TILYVNDVEASIQFYHHILGFPIKLRVESYVEFDTGEVTLSI-NSRQDVKESLGLPVPEAVSSSQT-FEIGFVVDDVNET 83
Cdd:cd08354    4 TCLYADDLDAAEAFYEDVLGLKPMLRSGRHAFFRLGPQVLLVfDPGATSKDVRTGEVPGHGASGHGhFAFAVPTEELAAW 83

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 960858405  84 IASLKEKGVPVIKEpAKKPWGQTVSYVSDPDGHFIEI 120
Cdd:cd08354   84 EARLEAKGVPIESY-TQWPEGGKSLYFRDPAGNLVEL 119
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 3-120 1.15e-11

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


Pssm-ID: 319965 [Multi-domain]  Cd Length: 122  Bit Score: 57.41  E-value: 1.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   3 MKYTILYVNDVEASIQFYHHILGFPIkLRVESYVEfdtGEVTLSINSRQDVKESLGLPVP-----EAVSSSQTF-EIGFV 76
Cdd:cd16358    1 MLHTMLRVGDLDRSIKFYTEVLGMKL-LRKRDYPE---GKYTLAFVGYGDEDENTVLELTynwgvDKYDLGTAYgHIAIG 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 960858405  77 VDDVNETIASLKEKGVPVIKEPAKKPWGQTV-SYVSDPDGHFIEI 120
Cdd:cd16358   77 VEDVYETCERIRKKGGKVTREPGPMKGGTTViAFVEDPDGYKIEL 121
VOC_like cd08359
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-120 1.67e-11

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: 56.64  E-value: 1.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   5 YTILYVNDVEASIQFYHHILGFPIKLRVESYVEFDTGEvtlsinsRQDVKESLGLPVPEAV-SSSQTFE----IGFVVDD 79
Cdd:cd08359    4 GPVIVTEDVAATAAFYVKHFGFRVIFDSDWYVSLRRAE-------RHGFELAIMDGQHGAVpAASQTQSsgliINFEVDD 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 960858405  80 VNETIASLKEKGVPVIKEPAKKPWGQTVSYVSDPDGHFIEI 120
Cdd:cd08359   77 ADAEYERLTQAGLEFLEPPRDEPWGQRRFIVRDPNGVLIDV 117
MRD cd07235
Mitomycin C resistance protein (MRD); Mitomycin C (MC) is a naturally occurring antibiotic, ...
 8-120 5.22e-10

Mitomycin C resistance protein (MRD); Mitomycin C (MC) is a naturally occurring antibiotic, and antitumor agent used in the treatment of cancer. Its antitumor activity is exerted primarily through monofunctional and bifunctional alkylation of DNA. MRD binds to MC and functions as a component of the MC exporting system. MC is bound to MRD by a stacking interaction between a His and a Trp. MRD adopts a structural fold similar to bleomycin resistance protein, glyoxalase I, and extradiol dioxygenases; and it has binding sites at an identical location to binding sites in these evolutionarily related enzymes.


Pssm-ID: 319901  Cd Length: 123  Bit Score: 52.89  E-value: 5.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   8 LYVNDVEASIQFYHhILGFPIKLRVES--YVEF-DTGEVTLSINSRQDVKESLglPVPEAVSSSQTFEIGFVVD---DVN 81
Cdd:cd07235    6 IVVEDMAKSLEFYR-KLGFEVPEEADSapHTEAaLPGGIRLALDTEETIRSYD--PGWQAPTGGGRFAIAFLCPtpaEVD 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 960858405  82 ETIASLKEKGVPVIKEPAKKPWGQTVSYVSDPDGHFIEI 120
Cdd:cd07235   83 AKYAELTGAGYEGHLKPWNAPWGQRYAIVKDPDGNVVDL 121
VOC_like cd16355
uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily; The vicinal oxygen ...
 7-116 1.44e-09

uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily; 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: 319962  Cd Length: 121  Bit Score: 51.72  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   7 ILYVNDVEASIQFYHHILGFPIKLRVESYVEF-----DTGEVTLSINsRQDVKESLGlPVPEAVSSSQTFeIGFVVDDVN 81
Cdd:cd16355    4 VLNVSDIPASFAWFEKVLGFQKDWDWGDPPTFgsvgsGECEIFLCQG-GQGGSLRLG-PCGDALPSYGAW-MSVWVDDVD 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 960858405  82 ETIASLKEKGVPVIKEPAKKPWGQTVSYVSDPDGH 116
Cdd:cd16355   81 ALHRECRARGADIRQPPTDMPWGMREMHVRHPDGH 115
VOC_like cd07238
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-120 2.78e-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: 319903  Cd Length: 112  Bit Score: 50.94  E-value: 2.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   8 LYVNDVEASIQFYHHILGFPiklrvesyVEFDTGEV-TLSINSRQDVKESL------GLPVPEAvsssqTFEigfvVDDV 80
Cdd:cd07238    6 IATADPERAAAFYGDHLGLP--------LVMDHGWIvTFASPGNAHAQISLareggsGTVVPDL-----SIE----VDDV 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 960858405  81 NETIASLKEKGVPVIKEPAKKPWGQTVSYVSDPDGHFIEI 120
Cdd:cd07238   69 DAVHARVVAAGLRIEYGPTTEAWGVRRFFVRDPFGRLINI 108
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 7-121 1.01e-07

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: 46.84  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   7 ILYVNDVEASIQFYHHILGFpiklrvesYVEFDTGEVTLSINSRQDVKESLgLPVPEAVSSSQTFEIGFVVDDVNETIAS 86
Cdd:cd08349    3 ILPVRDIDKTLAFYVDVLGF--------EVDYERPPPGYAILSRGGVELHL-FEHPGLDPAGSGVAAYIRVEDIDALHAE 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 960858405  87 LKEKGVPV-----IKEPAKKPWGQTVSYVSDPDGHFIEIC 121
Cdd:cd08349   74 LKAAGLPLfgiprITPIEDKPWGMREFAVVDPDGNLLRFG 113
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 3-120 1.10e-07

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


Pssm-ID: 319900 [Multi-domain]  Cd Length: 142  Bit Score: 47.32  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   3 MKYTILYVNDVEASIQFYHHILGfpikLRVESYVEFDTGEVTLSINSRQDVKESLGLPVPEAVSSSQT------------ 70
Cdd:cd07233    1 FNHTMLRVKDPKKSLKFYTEVLG----MKLLRKKDFPEMKFSLYFLGYEDPKDIPKDPRTAWVFSREGtlelthnwgten 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 960858405  71 ----------------FEIGFVVDDVNETIASLKEKGVPVIKEPaKKPWGQTVSYVSDPDGHFIEI 120
Cdd:cd07233   77 dedpvyhngnsdprgfGHIGIAVDDVYAACERFEELGVKFKKKP-DDGKMKGIAFIKDPDGYWIEI 141
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 10-122 3.13e-07

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


Pssm-ID: 319912 [Multi-domain]  Cd Length: 127  Bit Score: 45.64  E-value: 3.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405  10 VNDVEASIQFYHHILGfpikLRVESYVEFDTGEVTLSINSRQDVKESLGLPVPEAVSSSQTFE--------IGFVVDDVN 81
Cdd:cd07249    8 VPDLDEALKFYEDVLG----VKVSEPEELEEQGVRVAFLELGNTQIELLEPLGEDSPIAKFLDkkggglhhIAFEVDDID 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 960858405  82 ETIASLKEKGVPVI-KEPAKKPWGQTVSYVSDPDGH--FIEICD 122
Cdd:cd07249   84 AAVEELKAQGVRLLsEGPRIGAHGKRVAFLHPKDTGgvLIELVE 127
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 10-120 3.77e-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: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 45.39  E-value: 3.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405  10 VNDVEASIQFYHHILGFPIKLRVESYVE----FDTGEV-TLSINSRQDVKEslgLPVPEAVSSSQtfEIGFVVDDVNETI 84
Cdd:cd07245    8 CPDLERARRFYTDVLGLEEVPRPPFLKFggawLYLGGGqQIHLVVEQNPSE---LPRPEHPGRDR--HPSFSVPDLDALK 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 960858405  85 ASLKEKGVPVIKEPAKKPwGQTVSYVSDPDGHFIEI 120
Cdd:cd07245   83 QRLKEAGIPYTESTSPGG-GVTQLFFRDPDGNRLEF 117
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 10-120 4.64e-07

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: 45.23  E-value: 4.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405  10 VNDVEASIQFYHHILGFPIKLRVE-----SY---VEFDTGEVTLSI--NSRQDVKEslglpvPEAvsssQTFE-IGFVVD 78
Cdd:cd08352   10 CSDYEKSKDFYVDKLGFEIIREHYrpernDIkldLALGGYQLELFIkpDAPARPSY------PEA----LGLRhLAFKVE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 960858405  79 DVNETIASLKEKGVPVikEPAKK--PWGQTVSYVSDPDGHFIEI 120
Cdd:cd08352   80 DVEATVAELKSLGIET--EPIRVddFTGKKFTFFFDPDGLPLEL 121
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 7-121 6.72e-07

Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily of VOC family contains human glyoxalase domain-containing protein 5 and similar proteins. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319916 [Multi-domain]  Cd Length: 123  Bit Score: 44.91  E-value: 6.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   7 ILYVNDVEASIQFYHHILGFpiklrveSYVEFDTGEVTLS-----INSRQDVKEslGLPVPEAVSSSqTFEIGFVVD-DV 80
Cdd:cd07253    8 VLTVKDIERTIDFYTKVLGM-------TVVTFKEGRKALRfgnqkINLHQKGKE--FEPKASAPTPG-SADLCFITEtPI 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 960858405  81 NETIASLKEKGVPVIKEPAKKpWGQT---VS-YVSDPDGHFIEIC 121
Cdd:cd07253   78 DEVLEHLEACGVTIEEGPVKR-TGALgpiLSiYFRDPDGNLIELS 121
PLN02367 PLN02367
lactoylglutathione lyase
 3-122 7.15e-07

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 46.15  E-value: 7.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   3 MKYTILYVNDVEASIQFYHHILGFPIKLRVEsyveFDTGEVTLSINSRQDVKESLGLPVPEAV---SSSQTFE------- 72
Cdd:PLN02367  76 MQQTMYRIKDPKASLDFYSRVLGMSLLKRLD----FPEMKFSLYFMGYEDTASAPTDPTERTVwtfGQKATIElthnwgt 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 960858405  73 ---------------------IGFVVDDVNETIASLKEKGVPVIKEPAKKPWgQTVSYVSDPDGHFIEICD 122
Cdd:PLN02367 152 esdpdfkgyhngnseprgfghIGITVDDVYKACERFEELGVEFVKKPNDGKM-KGIAFIKDPDGYWIEIFD 221
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 10-120 8.95e-07

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


Pssm-ID: 319951 [Multi-domain]  Cd Length: 131  Bit Score: 44.65  E-value: 8.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405  10 VNDVEASIQFYHHILGFPIKLRVESYVEFDTGEVTLSINSRQDVKESlglpvpeAVSSSQTfEIGFVVD--DVNETIASL 87
Cdd:cd08363    8 VSNLNKSIAFYKDVLDAKLLVLGEKTAYFDLNGLWLALNVQEDIPRN-------EISHSYT-HIAFSIDeeDLDAFKERL 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 960858405  88 KEKGVPVIK-EPAKKPWGQTVsYVSDPDGHFIEI 120
Cdd:cd08363   80 KDNGVNILEgRKRDILEGQSI-YFTDPDGHLFEL 112
PRK04101 PRK04101
metallothiol transferase FosB;
10-119 1.22e-06

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 44.55  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405  10 VNDVEASIQFYHHILGFPIKLRVESYVEFDTGEVTLSINSRQDVKESlglpvpeAVSSSQTfEIGFVVD--DVNETIASL 87
Cdd:PRK04101  12 VSNLEKSIEFYEKVLGAKLLVKGRKTAYFDLNGLWIALNEEKDIPRN-------EIHQSYT-HIAFSIEeeDFDHWYQRL 83

                         90       100       110
                 ....*....|....*....|....*....|..
gi 960858405  88 KEKGVPVIKEPAKKPWGQTVSYVSDPDGHFIE 119
Cdd:PRK04101  84 KENDVNILPGRERDERDKKSIYFTDPDGHKFE 115
VOC_like cd07246
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-116 8.56e-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: 319910 [Multi-domain]  Cd Length: 124  Bit Score: 41.90  E-value: 8.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   8 LYVNDVEASIQFYHHILGFPIKLRVESY------VEFDTGEVTLSINsrqDVKESLGLPVPEAV-SSSQTFEIGfvVDDV 80
Cdd:cd07246    7 LVVEDAAAAIAFYKKAFGAEELGRTTQEdgrvghAELRIGGTVVMVA---DENPERGALSPTKLgGTPVIFHLY--VEDV 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 960858405  81 NETIASLKEKGVPVIKEPAKKPWGQTVSYVSDPDGH 116
Cdd:cd07246   82 DATFARAVAAGAVVVEPVEDQFWGDRVGKVKDPFGH 117
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 8-115 1.19e-05

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: 41.48  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   8 LYVNDVEASIQFYHHILGF---PIKLRVESYVEFDTGEvtlsinsrqdvKESLGL-PVPEAVSSSQT-FEIGFVVDDVNE 82
Cdd:cd07247    6 LPTTDLERAKAFYGAVFGWtfeDEGDGGGDYALFTAGG-----------GAVGGLmRAPEEVAGAPPgWLIYFAVDDLDA 74

                         90       100       110
                 ....*....|....*....|....*....|...
gi 960858405  83 TIASLKEKGVPVIKEPAKKPWGQTVSYVSDPDG 115
Cdd:cd07247   75 ALARVEAAGGKVVVPPTDIPGGGRFAVFADPEG 107
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-120 2.11e-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: 319917 [Multi-domain]  Cd Length: 120  Bit Score: 40.91  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   8 LYVNDVEASIQFYHHILGFPIKLRVESYVEF--DTGEVTLSInSRQDVKESLGLpvpeavsssqtFEIGFVVDDVNETIA 85
Cdd:cd07254    7 LNVTDLERSIRFYSDLFGAEPAKRKADYAKFmlEDPPLNLAL-LVNDRKEPYGL-----------NHLGIQVDSKEEVAA 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 960858405  86 S---LKEKGVPVIKEPAKKpWGQTVS---YVSDPDGHFIEI 120
Cdd:cd07254   75 LkarAEAAGLPVRKEPRTT-CCYAVQdkfWLTDPDGNAWEF 114
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 3-123 2.98e-05

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 41.34  E-value: 2.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   3 MKYTILYVNDVEASIQFYHHILGFpiklRVESYVEFDTGEVTLSINSRQDVKESLGLPVPEAV----------------- 65
Cdd:PLN03042  28 MQQTMFRIKDPKASLDFYSRVLGM----SLLKRLDFPEMKFSLYFLGYEDSETAPTDPPERTVwtfgrkatielthnwgt 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 960858405  66 SSSQTFE--------------IGFVVDDVNETIASLKEKGVPVIKEPAKKPWgQTVSYVSDPDGHFIEICDA 123
Cdd:PLN03042 104 ESDPEFKgyhngnsdprgfghIGITVDDVYKACERFEKLGVEFVKKPDDGKM-KGLAFIKDPDGYWIEIFDL 174
TioX_like cd08355
Micromonospora sp. TioX and similar proteins; Micromonospora sp. TioX is encoded by a gene of ...
 5-116 4.15e-05

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: 40.10  E-value: 4.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   5 YTILYVNDVEASIQFYHHILGFPIKLRVES------YVEFDTGEVTLSINSRQDVKESlglPVPEAVSSSQTFEIGFVVD 78
Cdd:cd08355    2 VPTLRYRDAVAAIDWLVEAFGFEERMVVPGdegtihHAELTFGGGGVMVGSVRDEARP---DRPADAGGHGTQSVYVAVA 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 960858405  79 DVNETIASLKEKGVPVIKEPAKKPWGQTVSYVSDPDGH 116
Cdd:cd08355   79 DPDAHYERARAAGAEIVMEPTDTDYGSRDYSARDPEGH 116
BphC2-C3-RGP6_C_like cd08348
The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus ...
 2-122 1.30e-04

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


Pssm-ID: 319936  Cd Length: 137  Bit Score: 39.04  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   2 KMKYTILYVNDV--EASIQFYHHILGFPIKLRVE--SYVEFDTGEVTLSINSRqdvkESLGLPVPEAVSSSQTFEIGFV- 76
Cdd:cd08348    1 KLAHFVLRTNPEkfEAMVQWYLDILGARIVARNAkgCFLSFDEEHHRIAIFGA----PGGAQPPDKRPTRVGLAHIAFTy 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 960858405  77 --VDDVNETIASLKEKGVpVIKEPAKKpwGQTVS-YVSDPDGHFIEI-CD 122
Cdd:cd08348   77 asLDDLARNYAQLKERGI-KPVWPVNH--GVTTSiYYRDPDGNMLEMqVD 123
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 8-120 1.34e-04

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: 38.80  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   8 LYVNDVEASIQFYHHILGFpiKLRVE----SYVEFdtGEVTLSINsrqdvkeslglpVPEAVSSSQTF-EIGFVVD--DV 80
Cdd:cd07244    7 LAVSDLERSLAFYVDLLGF--KPHVRwdkgAYLTA--GDLWLCLS------------LDPAAEPSPDYtHIAFTVSeeDF 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 960858405  81 NETIASLKEKGVPVikepakkpWGQTVS-----YVSDPDGHFIEI 120
Cdd:cd07244   71 EELSERLRAAGVKI--------WQENSSegdslYFLDPDGHKLEL 107
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 8-119 2.02e-04

C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family contains the C-terminal, catalytic domain of type I, class II extradiol dioxygenases. Dioxygenases catalyze the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms, resulting in the cleavage of aromatic rings. Two major groups of dioxygenases have been identified according to the cleavage site; extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon, whereas intradiol enzymes cleave the aromatic ring between two hydroxyl groups. Extradiol dioxygenases are classified into type I and type II enzymes. Type I extradiol dioxygenases include class I and class II enzymes. These two classes of enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. The extradiol dioxygenases represented in this family are type I, class II enzymes, and are composed of the N- and C-terminal domains of similar structure fold, resulting from an ancient gene duplication. The active site is located in a funnel-shaped space of the C-terminal domain. A catalytically essential metal, Fe(II) or Mn(II), presents in all the enzymes in this family.


Pssm-ID: 319931  Cd Length: 132  Bit Score: 38.45  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   8 LYVNDVEASIQFYHHILGFpiklRV--ESYVEFDTGEVTLSINSRQDVKES--LGLPVPEAVSSSqtfeigFVVDDVNET 83
Cdd:cd08343    5 LCSPDVEASRDFYTDVLGF----RVsdRIVDPGVDGGAFLHCDRGTDHHTValAGGPHPGLHHVA------FEVHDLDDV 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 960858405  84 IAS---LKEKGVPVIKEPAKKPWGQTVS-YVSDPDGHFIE 119
Cdd:cd08343   75 GRGhdrLREKGYKIEWGPGRHGLGSQVFdYWFDPSGNRVE 114
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 8-120 2.83e-04

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: 37.68  E-value: 2.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   8 LYVNDVEASIQFYHHILGFpiklrveSYVEFDTGEVTLSINSRQD---VKESLGLPVPEaVSSSQTFEIGFVVDDVNETI 84
Cdd:cd07255    8 LKVADLERQSAFYQNVIGL-------SVLKQNASRAYLGVDGKQVllvLEAIPDAVLAP-RSTTGLYHFAILLPDRKALG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 960858405  85 ASLKEkgvpVIKE-PAKKPWGQTVS---YVSDPDGHFIEI 120
Cdd:cd07255   80 RALAH----LAEHgPLIGAADHGVSeaiYLSDPEGNGIEI 115
PRK10291 PRK10291
glyoxalase I; Provisional
 7-123 4.13e-04

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 37.70  E-value: 4.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   7 ILYVNDVEASIQFYHHILGFPIkLRVESYVEF--DTGEVTLSINSRQDVKE-SLGLPVPEAVSSSQTFEIGFVVDDVNET 83
Cdd:PRK10291   1 MLRVGDLQRSIDFYTNVLGMKL-LRTSENPEYkySLAFVGYGPETEEAVIElTYNWGVDKYELGTAYGHIALSVDNAAEA 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 960858405  84 IASLKEKGVPVIKEPAKKPWGQTV-SYVSDPDGHFIEICDA 123
Cdd:PRK10291  80 CEKIRQNGGNVTREAGPVKGGTTViAFVEDPDGYKIELIEE 120
PLN02300 PLN02300
lactoylglutathione lyase
 74-120 5.47e-04

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 38.22  E-value: 5.47e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 960858405  74 GFVVDDVNETIASLKEKGVPVIKEPAKKPWGQTV-SYVSDPDGHFIEI 120
Cdd:PLN02300  98 GIAVEDVAKTVELVKAKGGKVTREPGPVKGGKSViAFVKDPDGYKFEL 145
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 7-121 8.75e-04

C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319964  Cd Length: 114  Bit Score: 36.38  E-value: 8.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   7 ILYVNDVEASIQFYHHILGFPIklrvesyVEFDTGEVTLSINSRQDVKESLGLPVPE-----------AVSSSQTFEIGF 75
Cdd:cd16357    3 SLAVSDLEKSIDYWSDLLGMKV-------FEKSEKSALLGYGEDQAKLELVDIPEPVdhgtafgriafSCPADELPPIEE 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 960858405  76 VVDDVNETIaslkekGVPVIK--EPAKKpwgqTVSYV--SDPDGHfiEIC 121
Cdd:cd16357   76 KVKAAGQTI------LTPLVSldTPGKA----TVQVVilADPDGH--EIC 113
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
10-98 1.09e-03

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 36.10  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   10 VNDVEASIQFYHHILGFpiklRVESYVEFDTGEVTLSI--NSRQDVKESLGLPVPE----AVSSSQTFEIGFVVDDVNET 83
Cdd:pfam13669   7 VPDLDRALALWGALLGL----GPEGDYRSEPQNVDLAFalLGDGPVEVELIQPLDGdsplARHGPGLHHLAYWVDDLDAA 82

                          90
                  ....*....|....*
gi 960858405   84 IASLKEKGVPVIKEP 98
Cdd:pfam13669  83 VARLLDQGYRVAPKG 97
VOC_BsYyaH cd07241
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal ...
 2-120 1.74e-03

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: 35.85  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   2 KMKYTILYVNDVEASIQFYHHILGFPI-------KLRVESY-VEFDTGeVTLSINSRQDVkeslglpVPEAVSSSQT--F 71
Cdd:cd07241    1 KIEHVALWTNDLERMKDFYVKYFGAESndiyhnkKKGFRSYfLTFDSG-ARLELMSRPDV-------TDPDKEVERTglA 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 960858405  72 EIGFVV---DDVNETIASLKEKGVPVIKEPAKKPWGQTVSYVSDPDGHFIEI 120
Cdd:cd07241   73 HIAFSVgskEAVDELTERLRADGYAVVGGPRTTGDGYYESVILDPEGNRIEI 124
TflA cd16362
Toxoflavin Lyase; Toxoflavin lyase (TflA) is metalloenzyme degrading toxoflavin at the ...
 8-120 2.13e-03

Toxoflavin Lyase; Toxoflavin lyase (TflA) is metalloenzyme degrading toxoflavin at the presence of oxygen, Mn(II), and dithiothreitol. TflA is structurally homologous to proteins of the vicinal oxygen chelate superfamily. The structure of TflA contains fold that displays a rare rearrangement of the structural modules indicative of domain permutation. Moreover, unlike the 2-His-1-carboxylate facial triad commonly utilized by vicinal oxygen chelate dioxygenases and other dioxygen-activating non-heme Fe(II) enzymes, the metal center in TflA consists of a 1-His-2-carboxylate facial triad. Toxoflavin is an azapteridine that is toxic to various plants, fungi, animals, and bacteria.


Pssm-ID: 319969  Cd Length: 110  Bit Score: 35.27  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   8 LYVNDVEASIQFYHHILGFPIklRVESYVEFDTGEVTLSINSRQDvkeslglPVPEAVSSSQTFEIGFVVDDVNETIASL 87
Cdd:cd16362    5 LYAPNLERSLAFYTNFLGAQH--VHESNDAFTVLLNVSSIQLVAA-------AEGTASSPFYHIAINISANHFQEGKAAL 75

                         90       100       110
                 ....*....|....*....|....*....|...
gi 960858405  88 KEKGVPVIKEPakKPWGQTVSYVSDPDGHFIEI 120
Cdd:cd16362   76 SGGGELLTEND--EDQNASSCYVEDPSGNLIEL 106
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 8-119 3.59e-03

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: 34.84  E-value: 3.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   8 LYVNDVEASIQFYHHILGF---------PIKLRVESYveFDTGEVTLSINSrqdvkeslGLPVPEAVSSSQTFEIGfvVD 78
Cdd:cd08345    4 LIVRDLEKSTAFLQDIFGArevyssgdkTFSLSKEKF--FLLGGLWIALME--------GESLQERSYTHIAFQIQ--SE 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 960858405  79 DVNETIASLKEKGVPvIKEPAKKPWGQTVS-YVSDPDGHFIE 119
Cdd:cd08345   72 DFDRYAERLGALGVE-MRPPRPRVEGEGRSiYFYDPDNHLFE 112
BLMT_like cd08350
BLMT, a bleomycin resistance protein encoded on the transposon Tn5, and similar proteins; BLMT ...
 12-122 4.23e-03

BLMT, a bleomycin resistance protein encoded on the transposon Tn5, and similar proteins; BLMT is a bleomycin (Bm) resistance protein, encoded by the ble gene on the transposon Tn5. This protein confers a survival advantage to Escherichia coli host cells. 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. BLMT has strong binding affinity to Bm and it protects against this lethal compound through drug sequestering. BLMT has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMT is a dimer with two Bm-binding pockets formed at the dimer interface.


Pssm-ID: 319938  Cd Length: 118  Bit Score: 34.56  E-value: 4.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405  12 DVEASIQFYHHiLGFPIKLRVESYVEFDTGEVTLSINSRQDVkeslglpVPEAVSSSQTFEigfvVDDVNETIASLKEKG 91
Cdd:cd08350   12 DFDATAAFYAR-LGFQTVYRDDGWMILRRGDLTLEFFPHPDL-------DPAASWFSCCLR----VDDLDALYAQWSAAG 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 960858405  92 VPV-------IKEPAKKPWGQTVSYVSDPDGHFIEICD 122
Cdd:cd08350   80 IPEdtrgiprLHPPQTQPWGIRMFALIDPDGSLLRLIQ 117
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 4-121 4.29e-03

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: 34.53  E-value: 4.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   4 KYTILYVNDVEASIQFYHHILGFPIKLRVESYVEF-DTGEVTLSINSRQDVKESLGLpvpeavsssqtfeIGFVVD---D 79
Cdd:cd08362    5 RYVALGVPDLAAEREFYTEVWGLEEVAEDDDVVYLrAEGSEHHVLRLRQSDENRLDL-------------IAFAAAtraD 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 960858405  80 VNETIASLKEKGVPVIKEPAK--KPWGQTVSYVSDPDGHFIEIC 121
Cdd:cd08362   72 VDALAARLAAAGVRILSEPGPldDPGGGYGFRFFDPDGRTIEVS 115
VOC_BsCatE_like_C cd16359
C-terminal of Bacillus subtilis CatE like protein, a vicinal oxygen chelate subfamily; ...
 8-107 6.19e-03

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


Pssm-ID: 319966  Cd Length: 110  Bit Score: 33.88  E-value: 6.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960858405   8 LYVNDVEASIQFYHHILGFPIKLRVESYVEFDTGEVT--LSINSRQDVKesLGLPvPEAVSSSQTFEIgfVVDDVN---E 82
Cdd:cd16359    5 LRVSDLKAASHFYHQVLGFDIKSRRPGALFLSAGGYHhhIGLNTWAGRG--LPLP-PEDATGLAYFTI--VLPDQEalaA 79

                         90       100
                 ....*....|....*....|....*....
gi 960858405  83 TIASLKEKGVPVIKEP----AKKPWGQTV 107
Cdd:cd16359   80 ILERLDLAGYDVEALDdgleLTDPWGITV 108
 
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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