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Conserved domains on  [gi|489419402|ref|WP_003325164|]
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VOC family protein [Bacillus atrophaeus]

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 ...
 5-125 1.62e-38

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: 125.91  E-value: 1.62e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   5 MRYVILYVSDGERSLHFYKDILGLTVRAQHDT--YVEFDTGSAILAFNTRKNVREITPLEIPEEAgysqtFELGFVTEDV 82
Cdd:cd07264    1 IAYIVLYVDDFAASLRFYRDVLGLPPRFLHEEgeYAEFDTGETKLALFSRKEMARSGGPDRRGSA-----FELGFEVDDV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489419402  83 GAVIEKLRGEGVSILSEPKVKPWGQTVAYVADPDGHYIEICSP 125
Cdd:cd07264   76 EATVEELVERGAEFVREPANKPWGQTVAYVRDPDGNLIEICEP 118
 
Name Accession Description Interval E-value
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-125 1.62e-38

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: 125.91  E-value: 1.62e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   5 MRYVILYVSDGERSLHFYKDILGLTVRAQHDT--YVEFDTGSAILAFNTRKNVREITPLEIPEEAgysqtFELGFVTEDV 82
Cdd:cd07264    1 IAYIVLYVDDFAASLRFYRDVLGLPPRFLHEEgeYAEFDTGETKLALFSRKEMARSGGPDRRGSA-----FELGFEVDDV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489419402  83 GAVIEKLRGEGVSILSEPKVKPWGQTVAYVADPDGHYIEICSP 125
Cdd:cd07264   76 EATVEELVERGAEFVREPANKPWGQTVAYVRDPDGNLIEICEP 118
Glyoxalase_2 pfam12681
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 5-127 2.76e-35

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


Pssm-ID: 403776  Cd Length: 118  Bit Score: 117.51  E-value: 2.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402    5 MRYVILYVSDGERSLHFYKDILGLTVRAQHDTYVEFDTGSAIlafntRKNVREITPLEIPEEAGySQTFELGFVTEDVGA 84
Cdd:pfam12681   1 FKCPLLVVKDINISRKFYEDVLDQKIKLDFGENVSFEGGFAI-----QSDFKELIGIDLSIAEQ-SNNFELYFEVADVDA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 489419402   85 VIEKLRG-EGVSILSEPKVKPWGQTVAYVADPDGHYIEICSPVE 127
Cdd:pfam12681  75 FLQKIKEiGNIEYLHELKEQPWGQRVFRFYDPDGHIIEIGESME 118
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 8-127 6.54e-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: 86.20  E-value: 6.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   8 VILYVSDGERSLHFYKDILGLTVRAQHDtYVEFDTGSAILAFNtrkNVREITPLEIPEEAGYSQT---FELGFVTEDVGA 84
Cdd:COG0346    6 VTLRVSDLEASLAFYTDVLGLELVKRTD-FGDGGFGHAFLRLG---DGTELELFEAPGAAPAPGGgglHHLAFRVDDLDA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489419402  85 VIEKLRGEGVSILSEPKVKPWGQTVAYVADPDGHYIEICSPVE 127
Cdd:COG0346   82 AYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVEPPP 124
PRK04101 PRK04101
metallothiol transferase FosB;
12-121 1.03e-07

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 47.25  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402  12 VSDGERSLHFYKDILG--LTVRAQHDTYveFDTGSAILAFNTRKNvreitpleIP-EEAGYSQTfELGFVT--EDVGAVI 86
Cdd:PRK04101  12 VSNLEKSIEFYEKVLGakLLVKGRKTAY--FDLNGLWIALNEEKD--------IPrNEIHQSYT-HIAFSIeeEDFDHWY 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489419402  87 EKLRGEGVSILSEPKVKPWGQTVAYVADPDGHYIE 121
Cdd:PRK04101  81 QRLKENDVNILPGRERDERDKKSIYFTDPDGHKFE 115
 
Name Accession Description Interval E-value
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-125 1.62e-38

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: 125.91  E-value: 1.62e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   5 MRYVILYVSDGERSLHFYKDILGLTVRAQHDT--YVEFDTGSAILAFNTRKNVREITPLEIPEEAgysqtFELGFVTEDV 82
Cdd:cd07264    1 IAYIVLYVDDFAASLRFYRDVLGLPPRFLHEEgeYAEFDTGETKLALFSRKEMARSGGPDRRGSA-----FELGFEVDDV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489419402  83 GAVIEKLRGEGVSILSEPKVKPWGQTVAYVADPDGHYIEICSP 125
Cdd:cd07264   76 EATVEELVERGAEFVREPANKPWGQTVAYVRDPDGNLIEICEP 118
Glyoxalase_2 pfam12681
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 5-127 2.76e-35

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


Pssm-ID: 403776  Cd Length: 118  Bit Score: 117.51  E-value: 2.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402    5 MRYVILYVSDGERSLHFYKDILGLTVRAQHDTYVEFDTGSAIlafntRKNVREITPLEIPEEAGySQTFELGFVTEDVGA 84
Cdd:pfam12681   1 FKCPLLVVKDINISRKFYEDVLDQKIKLDFGENVSFEGGFAI-----QSDFKELIGIDLSIAEQ-SNNFELYFEVADVDA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 489419402   85 VIEKLRG-EGVSILSEPKVKPWGQTVAYVADPDGHYIEICSPVE 127
Cdd:pfam12681  75 FLQKIKEiGNIEYLHELKEQPWGQRVFRFYDPDGHIIEIGESME 118
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 8-127 6.54e-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: 86.20  E-value: 6.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   8 VILYVSDGERSLHFYKDILGLTVRAQHDtYVEFDTGSAILAFNtrkNVREITPLEIPEEAGYSQT---FELGFVTEDVGA 84
Cdd:COG0346    6 VTLRVSDLEASLAFYTDVLGLELVKRTD-FGDGGFGHAFLRLG---DGTELELFEAPGAAPAPGGgglHHLAFRVDDLDA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489419402  85 VIEKLRGEGVSILSEPKVKPWGQTVAYVADPDGHYIEICSPVE 127
Cdd:COG0346   82 AYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVEPPP 124
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
7-125 1.27e-21

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 82.98  E-value: 1.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   7 YVILYVSDGERSLHFYKDILGLTVRAQHDT------YVEFDTGSAILAFNTrknvreiTPLEIPEEAGysQTFELGFVTE 80
Cdd:COG2764    3 TPYLVVDDAEEALEFYEDVFGFEVVFRMTDpdgkimHAELRIGGSVLMLSD-------APPDSPAAEG--NGVSLSLYVD 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489419402  81 DVGAVIEKLRGEGVSILSEPKVKPWGQTVAYVADPDGHYIEICSP 125
Cdd:COG2764   74 DVDALFARLVAAGATVVMPLQDTFWGDRFGMVRDPFGVLWMINTP 118
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-127 5.79e-20

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 78.52  E-value: 5.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   1 MNLSMRYVILYVSDGERSLHFYKDILGLTVRAQHD---TYVEFDTGSAILAfntrknvrEITPleiPEEAGYSQTFELGF 77
Cdd:COG3324    1 MPGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGpggDYAEFDTDGGQVG--------GLMP---GAEEPGGPGWLLYF 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489419402  78 VTEDVGAVIEKLRGEGVSILSEPK-VKPWGqTVAYVADPDGHYIEICSPVE 127
Cdd:COG3324   70 AVDDLDAAVARVEAAGGTVLRPPTdIPPWG-RFAVFRDPEGNRFGLWQPAA 119
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-122 3.38e-19

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 76.72  E-value: 3.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402    7 YVILYVSDGERSLHFYKDILGLTVRAQHDTYVEFDTGSAilAFNTRKNVREITPLEIPEEAGYSQTFE----LGFVTEDV 82
Cdd:pfam00903   4 HVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSA--FFLAGGRVLELLLNETPPPAAAGFGGHhiafIAFSVDDV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 489419402   83 GAVIEKLRGEGVSILSEPKVKPWGQTVAYVADPDGHYIEI 122
Cdd:pfam00903  82 DAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 7-122 3.67e-18

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 74.10  E-value: 3.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   7 YVILYVSDGERSLHFYKDiLGLTVRAQ--HDTYVEFDTGSAI-LAFNTRKNVREITPLEIPEEAGYSQ-TFELGFVT-ED 81
Cdd:COG3607    6 FVNLPVADLERSRAFYEA-LGFTFNPQfsDEGAACFVLGEGIvLMLLPREKFATFTGKPIADATGFTEvLLALNVESrEE 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489419402  82 VGAVIEKLRGEGVSILSEPKVKPWGQTvAYVADPDGHYIEI 122
Cdd:COG3607   85 VDALVAKALAAGGTVLKPPQDVGGMYS-GYFADPDGHLWEV 124
VOC_like cd09011
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-122 2.21e-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: 319953  Cd Length: 122  Bit Score: 72.12  E-value: 2.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   5 MRY--VILYVSDGERSLHFYKDILGLTVRAQHDTYVEFDTGSAILAFNTRKNVREITPLEIPEEagySQTFELGFVTEDV 82
Cdd:cd09011    1 MKFvnPLLVVKDIEKSKKFYEDVLGQKILLDFGENVVFEGGFALQEKKSWLETIIISDLSIKQQ---SNNFELYFEVDDF 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489419402  83 GAVIEKL-RGEGVSILSEPKVKPWGQTVAYVADPDGHYIEI 122
Cdd:cd09011   78 DAFFEKLnPHKDIEFIHPILEHPWGQRVFRFYDPDGHIIEI 118
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 7-122 3.78e-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: 3.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   7 YVILYVSDGERSLHFYKDILGLTV--RAQHDTYVEFDTGSAIlafntrknVREITPLEIPEEAGYSQTFELGFVTEDVGA 84
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVvsRNEGGGFAFLRLGPGL--------RLALLEGPEPERPGGGGLFHLAFEVDDVDE 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489419402  85 VIEKLR--GEGVSILSEPKVKPWGQTVAYVADPDGHYIEI 122
Cdd:cd06587   73 VDERLReaGAEGELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-122 1.60e-15

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: 67.32  E-value: 1.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   8 VILYVSDGERSLHFYKDiLGLTV-RAQHDTYVEFDTGSAILAFNTRKNVREITPLEIpEEAGYSQtFELGFVT---EDVG 83
Cdd:cd07251    2 ITLGVRDLERSARFYEA-LGWKPnLDPNDGVVFFQLGGTVLALYPRDALAEDAGVSV-TGAGFSG-VTLAHNVrsrEEVD 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489419402  84 AVIEKLRGEGVSILSEPKVKPWGQTVAYVADPDGHYIEI 122
Cdd:cd07251   79 QLLAKAVAAGGKILKPPQEVFWGGYSGYFADPDGHIWEV 117
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
3-127 4.19e-15

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 66.91  E-value: 4.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   3 LSMRYVILYVSDGERSLHFYKDILGLTVRAQHDTYVEF--DTGSAILAFNTRKNVReitplEIPEEAGYsqtFELGFVT- 79
Cdd:COG2514    2 TRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLraDGGEHLLVLEEAPGAP-----PRPGAAGL---DHVAFRVp 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489419402  80 --EDVGAVIEKLRGEGVSIlsEPKVKPWGQTVAYVADPDGHYIEICSPVE 127
Cdd:COG2514   74 srADLDAALARLAAAGVPV--EGAVDHGVGESLYFRDPDGNLIELYTDRP 121
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 9-125 8.50e-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: 319942  Cd Length: 122  Bit Score: 62.77  E-value: 8.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   9 ILYVSDGERSLHFYKDILGLTVRAQHDTYVEFDTG-SAILAFNTRKNVREITPLEIPEEAGYSQT-FELGFVTEDVGAVI 86
Cdd:cd08354    5 CLYADDLDAAEAFYEDVLGLKPMLRSGRHAFFRLGpQVLLVFDPGATSKDVRTGEVPGHGASGHGhFAFAVPTEELAAWE 84

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489419402  87 EKLRGEGVSILSEPKVKPWGQTVaYVADPDGHYIEICSP 125
Cdd:cd08354   85 ARLEAKGVPIESYTQWPEGGKSL-YFRDPAGNLVELASA 122
EhpR_like cd07261
phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter ...
 8-123 1.49e-12

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: 59.34  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   8 VILYVSDGERSLHFYKDILGLTVRAQHDTYVEFD-TGSAILAFNTRKnvrEITPLEIPEEAGysqtFELGFVT---EDVG 83
Cdd:cd07261    2 VILYVDNPERSTEFYRFLLGKEPVESSPTFASFVlSGGAKLGLWSSE---EVEPKVAVTGGG----AELSFMVpsgEQVD 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489419402  84 AVIEKLRGEGVSILSEPKVKPWGQTvaYVA-DPDGHYIEIC 123
Cdd:cd07261   75 EVYAEWKAMGIPIIQEPTTMDFGYT--FVAtDPDGHRLRVC 113
MRD cd07235
Mitomycin C resistance protein (MRD); Mitomycin C (MC) is a naturally occurring antibiotic, ...
 10-122 7.89e-11

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: 55.20  E-value: 7.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402  10 LYVSDGERSLHFYKdILGLTVRAQHDT--YVEFDTGSAI-LAFNTRKNVREITPLEIPEEAGYSQTFELGFVTE-DVGAV 85
Cdd:cd07235    6 IVVEDMAKSLEFYR-KLGFEVPEEADSapHTEAALPGGIrLALDTEETIRSYDPGWQAPTGGGRFAIAFLCPTPaEVDAK 84

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489419402  86 IEKLRGEGVSILSEPKVKPWGQTVAYVADPDGHYIEI 122
Cdd:cd07235   85 YAELTGAGYEGHLKPWNAPWGQRYAIVKDPDGNVVDL 121
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-123 1.22e-10

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: 54.61  E-value: 1.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   8 VILYVSDGERSLHFYKDILGLTVRAQHDT----YVEF----DTGSAILafntrknvreITPLEIPEEAGYSQTFELG--- 76
Cdd:cd07263    2 VMLYVDDQDKALDFYVEKLGFEVVEDVPMggmrWVTVappgSPGTSLL----------LEPKAHPAQMPQSPEAAGGtpg 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489419402  77 --FVTEDVGAVIEKLRGEGVSILSEPkVKPWGQTVAYVADPDGHYIEIC 123
Cdd:cd07263   72 ilLATDDIDATYERLTAAGVTFVQEP-TQMGGGRVANFRDPDGNLFALM 119
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 5-122 2.65e-10

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: 53.94  E-value: 2.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   5 MRYVILYVSDGERSLHFYKDILGLTVRAQHDtYVEfdtGSAILAFNTRKNVREITPLEIPEEAG---YSQTFELGFV--- 78
Cdd:cd16358    1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKRD-YPE---GKYTLAFVGYGDEDENTVLELTYNWGvdkYDLGTAYGHIaig 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489419402  79 TEDVGAVIEKLRGEGVSILSEPKVKPWGQTV-AYVADPDGHYIEI 122
Cdd:cd16358   77 VEDVYETCERIRKKGGKVTREPGPMKGGTTViAFVEDPDGYKIEL 121
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 4-125 1.29e-09

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: 51.84  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   4 SMRYVILYVSDGERSLHFYKDILGLTVraqhdtyVEFDTGSAILAFNTRK-NVREI-TPLEIPEEAGYSQTFELGFVTE- 80
Cdd:cd07253    3 RLDHLVLTVKDIERTIDFYTKVLGMTV-------VTFKEGRKALRFGNQKiNLHQKgKEFEPKASAPTPGSADLCFITEt 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489419402  81 DVGAVIEKLRGEGVSIlSEPKVKPWGQ----TVAYVADPDGHYIEICSP 125
Cdd:cd07253   76 PIDEVLEHLEACGVTI-EEGPVKRTGAlgpiLSIYFRDPDGNLIELSNY 123
VOC_like cd08359
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 21-122 2.17e-09

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


Pssm-ID: 319947 [Multi-domain]  Cd Length: 119  Bit Score: 51.25  E-value: 2.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402  21 FYKDILGLTVRAQHDTYVefdtgsaILAFNTRKNVrEITPLEIPEEAG--YSQTFE----LGFVTEDVGAVIEKLRGEGV 94
Cdd:cd08359   18 FYVKHFGFRVIFDSDWYV-------SLRRAERHGF-ELAIMDGQHGAVpaASQTQSsgliINFEVDDADAEYERLTQAGL 89

                         90       100
                 ....*....|....*....|....*...
gi 489419402  95 SILSEPKVKPWGQTVAYVADPDGHYIEI 122
Cdd:cd08359   90 EFLEPPRDEPWGQRRFIVRDPNGVLIDV 117
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 9-123 3.83e-09

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: 50.69  E-value: 3.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   9 ILYVSDGERSLHFYKDILGLTVRAQH--DTYvefdtgsAILAFNTrknvREITPLEIPEEAGYSQTFELGFVTEDVGAVI 86
Cdd:cd08349    3 ILPVRDIDKTLAFYVDVLGFEVDYERppPGY-------AILSRGG----VELHLFEHPGLDPAGSGVAAYIRVEDIDALH 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489419402  87 EKLRGEGVSILSEPKV-----KPWGQTVAYVADPDGHYIEIC 123
Cdd:cd08349   72 AELKAAGLPLFGIPRItpiedKPWGMREFAVVDPDGNLLRFG 113
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 10-120 3.01e-08

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: 48.41  E-value: 3.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402  10 LYVSDGERSLHFYKDILGLTVRAQHD---TYVEFDTGSAILAfntrkNVREITPLEIPEEAGYSqtfeLGFVTEDVGAVI 86
Cdd:cd07247    6 LPTTDLERAKAFYGAVFGWTFEDEGDgggDYALFTAGGGAVG-----GLMRAPEEVAGAPPGWL----IYFAVDDLDAAL 76

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489419402  87 EKLRGEGVSILSEPKVKPWGQTVAYVADPDGHYI 120
Cdd:cd07247   77 ARVEAAGGKVVVPPTDIPGGGRFAVFADPEGNRF 110
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 12-122 4.17e-08

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: 48.12  E-value: 4.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402  12 VSDGERSLHFYKDILG--LTVRAQHDTYveFDTGSAILAFNTRKNV--REItpleipeeagySQTF-ELGFVT--EDVGA 84
Cdd:cd08363    8 VSNLNKSIAFYKDVLDakLLVLGEKTAY--FDLNGLWLALNVQEDIprNEI-----------SHSYtHIAFSIdeEDLDA 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489419402  85 VIEKLRGEGVSIL-SEPKVKPWGQTVaYVADPDGHYIEI 122
Cdd:cd08363   75 FKERLKDNGVNILeGRKRDILEGQSI-YFTDPDGHLFEL 112
PsjN_like cd16356
Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme ...
 7-122 7.26e-08

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: 47.42  E-value: 7.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   7 YVILYVSDGERSLHFYKDILGL--TVRAQHDTYVEFDTGSAILAFNTRK--NVREITPLEIPEEAGYSQTFELgFVTEDV 82
Cdd:cd16356    1 YVNIFTADIVALSDFYSELFGLeeIFEIRSPIFRGLRTGDSCLGFNAPEayELLGLPEFSDTPGIRILLTFDV-DDVEAV 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489419402  83 GAVIEKLRGEGVSILSEPKVKPWGQTVAYVADPDGHYIEI 122
Cdd:cd16356   80 DRLVPRAAALGATLIKPPYDTYYGWYQAVLLDPEGNVFRI 119
PRK04101 PRK04101
metallothiol transferase FosB;
12-121 1.03e-07

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 47.25  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402  12 VSDGERSLHFYKDILG--LTVRAQHDTYveFDTGSAILAFNTRKNvreitpleIP-EEAGYSQTfELGFVT--EDVGAVI 86
Cdd:PRK04101  12 VSNLEKSIEFYEKVLGakLLVKGRKTAY--FDLNGLWIALNEEKD--------IPrNEIHQSYT-HIAFSIeeEDFDHWY 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489419402  87 EKLRGEGVSILSEPKVKPWGQTVAYVADPDGHYIE 121
Cdd:PRK04101  81 QRLKENDVNILPGRERDERDKKSIYFTDPDGHKFE 115
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 8-122 4.65e-07

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: 45.35  E-value: 4.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   8 VILYVSDGERSLHFYKDILGLTVRAQHDTYVEFDTGSAILAfntrknvreitpLEIPEEAGYSQT---FELGFVTEDVGA 84
Cdd:cd07244    5 ITLAVSDLERSLAFYVDLLGFKPHVRWDKGAYLTAGDLWLC------------LSLDPAAEPSPDythIAFTVSEEDFEE 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489419402  85 VIEKLRGEGVSIL----SEpkvkpwGQTVaYVADPDGHYIEI 122
Cdd:cd07244   73 LSERLRAAGVKIWqensSE------GDSL-YFLDPDGHKLEL 107
VOC_like cd07238
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 10-124 1.34e-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: 319903  Cd Length: 112  Bit Score: 44.00  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402  10 LYVSDGERSLHFYKDILGLTVRAQHDTYVEFdtgsailAFNTRKNVREITpleIPEEAGYSQTFELGFVTEDVGAVIEKL 89
Cdd:cd07238    6 IATADPERAAAFYGDHLGLPLVMDHGWIVTF-------ASPGNAHAQISL---AREGGSGTVVPDLSIEVDDVDAVHARV 75

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489419402  90 RGEGVSILSEPKVKPWGQTVAYVADPDGHYIEICS 124
Cdd:cd07238   76 VAAGLRIEYGPTTEAWGVRRFFVRDPFGRLINILT 110
TioX_like cd08355
Micromonospora sp. TioX and similar proteins; Micromonospora sp. TioX is encoded by a gene of ...
 7-118 2.16e-06

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: 43.56  E-value: 2.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   7 YVILYVSDGERSLHFYKDILGLTVRAQH------DTYVEFDTGSAILAF-NTRKNVREitplEIPEEAGYSQTFELGFVT 79
Cdd:cd08355    2 VPTLRYRDAVAAIDWLVEAFGFEERMVVpgdegtIHHAELTFGGGGVMVgSVRDEARP----DRPADAGGHGTQSVYVAV 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489419402  80 EDVGAVIEKLRGEGVSILSEPKVKPWGQTVAYVADPDGH 118
Cdd:cd08355   78 ADPDAHYERARAAGAEIVMEPTDTDYGSRDYSARDPEGH 116
VOC_like cd16355
uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily; The vicinal oxygen ...
 9-118 6.52e-06

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: 42.09  E-value: 6.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   9 ILYVSDGERSLHFYKDILGLTVRAQHDTYVEFDTGSA----ILAFNTRKNVREIT---PLEIPEEAGYsqtfeLGFVTED 81
Cdd:cd16355    4 VLNVSDIPASFAWFEKVLGFQKDWDWGDPPTFGSVGSgeceIFLCQGGQGGSLRLgpcGDALPSYGAW-----MSVWVDD 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489419402  82 VGAVIEKLRGEGVSILSEPKVKPWGQTVAYVADPDGH 118
Cdd:cd16355   79 VDALHRECRARGADIRQPPTDMPWGMREMHVRHPDGH 115
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 7-123 7.88e-06

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: 41.77  E-value: 7.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   7 YVILYVSDGERSLHFYKDILGLTVRAQhdtyvefDTGSAILAFntRKNVREITPLEIPEEAGYSQTF-ELGF-VTEDVGA 84
Cdd:cd16357    1 KVSLAVSDLEKSIDYWSDLLGMKVFEK-------SEKSALLGY--GEDQAKLELVDIPEPVDHGTAFgRIAFsCPADELP 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489419402  85 VIE-KLRGEGVSILSEPkVK---PWGQTVAYV--ADPDGHyiEIC 123
Cdd:cd16357   72 PIEeKVKAAGQTILTPL-VSldtPGKATVQVVilADPDGH--EIC 113
PLN02300 PLN02300
lactoylglutathione lyase
 5-122 2.72e-05

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 41.69  E-value: 2.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   5 MRYVILYVSDGERSLHFYKDILGLTVRAQHDTYVEFDTgSAILAFNTRKN--VREIT------PLEIPEEAGYsqtfeLG 76
Cdd:PLN02300  25 MLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYT-NAFLGYGPEDSnfVVELTynygvdKYDIGTGFGH-----FG 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489419402  77 FVTEDVGAVIEKLRGEGVSILSEP-KVKPWGQTVAYVADPDGHYIEI 122
Cdd:PLN02300  99 IAVEDVAKTVELVKAKGGKVTREPgPVKGGKSVIAFVKDPDGYKFEL 145
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 12-122 3.44e-05

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


Pssm-ID: 319940 [Multi-domain]  Cd Length: 123  Bit Score: 40.22  E-value: 3.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402  12 VSDGERSLHFYKDILGLTVRAQH------DTYVEFDTGSAILAFNTRKNVREItpLEIPEEAGYSQtfeLGFVTEDVGAV 85
Cdd:cd08352   10 CSDYEKSKDFYVDKLGFEIIREHyrpernDIKLDLALGGYQLELFIKPDAPAR--PSYPEALGLRH---LAFKVEDVEAT 84

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489419402  86 IEKLRGEGVSIlsEP-KVKPW-GQTVAYVADPDGHYIEI 122
Cdd:cd08352   85 VAELKSLGIET--EPiRVDDFtGKKFTFFFDPDGLPLEL 121
VOC_like cd07246
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 10-125 5.65e-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: 319910 [Multi-domain]  Cd Length: 124  Bit Score: 39.59  E-value: 5.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402  10 LYVSDGERSLHFYKDILGLTVRAQHDTY------VEFDTGSAILAFNTRknVREITPLEIPEEAGYSQTFELGfvTEDVG 83
Cdd:cd07246    7 LVVEDAAAAIAFYKKAFGAEELGRTTQEdgrvghAELRIGGTVVMVADE--NPERGALSPTKLGGTPVIFHLY--VEDVD 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489419402  84 AVIEKLRGEGVSILSEPKVKPWGQTVAYVADPDGHYIEICSP 125
Cdd:cd07246   83 ATFARAVAAGAVVVEPVEDQFWGDRVGKVKDPFGHVWWLATP 124
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-122 6.90e-05

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


Pssm-ID: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 39.61  E-value: 6.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   8 VILYVSDGERSLHFYKDILGLTV--RAQHDTY--VEFDTGSAI---LAFntRKNVREITPLEIPeeagySQTFELGFVTE 80
Cdd:cd07245    4 VALACPDLERARRFYTDVLGLEEvpRPPFLKFggAWLYLGGGQqihLVV--EQNPSELPRPEHP-----GRDRHPSFSVP 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489419402  81 DVGAVIEKLRGEGVSIlSEPKVKPWGQTVAYVADPDGHYIEI 122
Cdd:cd07245   77 DLDALKQRLKEAGIPY-TESTSPGGGVTQLFFRDPDGNRLEF 117
Glyoxalase_6 pfam18029
Glyoxalase-like domain; This entry comprises a diverse set of domains related to the ...
 21-123 1.02e-04

Glyoxalase-like domain; This entry comprises a diverse set of domains related to the Glyoxalase domain. The exact specificity of these proteins is uncertain.


Pssm-ID: 436220  Cd Length: 110  Bit Score: 38.90  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   21 FYKDILGLTVRAQHDTYVEFDTGSAILAFNTRknvreITPLEIPEEAGYSQTFELGFVTEDVGAVIEKLRGEGVSILSEP 100
Cdd:pfam18029  15 FWSAALGWEVVPDDTALPDPDGGGPIGGGGPR-----LLFQRVPEPKPGKNRVHLDLAVDDLEAAVARLVALGATVLDDG 89

                          90       100
                  ....*....|....*....|...
gi 489419402  101 KvkPWGQTVAYVADPDGHyiEIC 123
Cdd:pfam18029  90 D--DPDGGRWVLADPEGN--EFC 108
VOC_like cd08357
uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and ...
 12-122 3.82e-04

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


Pssm-ID: 319945 [Multi-domain]  Cd Length: 124  Bit Score: 37.36  E-value: 3.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402  12 VSDGERSLHFYKDILGLTVRAQHDTYVEFDT-GSAILAFNTRKNVREITPLeIPEEAGYSQTFELGFVTEDVGAVIEKLR 90
Cdd:cd08357    7 VRDLEAARDFYGDVLGCPEGRSSETWIDFNFfGHQVVAHLVPNYASTSTNA-VDGHSVPVPHFGLALTVDDFDALAERLK 85

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489419402  91 GEGVSILSEPKV----KPWGQTVAYVADPDGHYIEI 122
Cdd:cd08357   86 AAGVKFYIEPYVrfegEPGEQWTMFLLDPSGNALEF 121
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 4-124 7.41e-04

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: 36.93  E-value: 7.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   4 SMRYVILYVSDGERSLHFYKDILGLTVRAQHDTYVEFDTG---SAILAFNTRKNVREI--------TPLEIPEEAGYSQ- 71
Cdd:cd16361    1 GVNHVGITVPDLDAAVEFYTDVLGAEVVYRSTPLAEGDRGggeMRAAGFVPGFARARIamlrlgpgPGIELFEYKGPEQr 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489419402  72 ----------TFELGFVTEDVGAVIEKLRGEGVSILSEPKVKPWGQ-----TVAYVADPDGHYIEICS 124
Cdd:cd16361   81 apvprnsdvgIFHFALQVDDVEAAAERLAAAGGKVLMGPREIPDGGpgkgnRMVYLRDPWGTLIELVS 148
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 7-121 8.00e-04

Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. The three types of fosfomycin resistance proteins, employ different mechanisms to render fosfomycin [(1R,2S)-epoxypropylphosphonic acid] inactive. FosB catalyzes the addition of L-cysteine to the epoxide ring of fosfomycin. FosX catalyzes the addition of a water molecule to the C1 position of the antibiotic with inversion of configuration at C1. FosA catalyzes the addition of glutathione to the antibiotic fosfomycin, making it inactive. Catalytic activities of both FosX and FosA are Mn(II)-dependent, but FosB is activated by Mg(II). Fosfomycin resistant proteins are evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319933  Cd Length: 118  Bit Score: 36.77  E-value: 8.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   7 YVILYVSDGERSLHFYKDILG--LTVRAQHDTYVE-----FDTGSAILAFNTRknvreitplEIPEEAGYsQTFELGFVT 79
Cdd:cd08345    1 HITLIVRDLEKSTAFLQDIFGarEVYSSGDKTFSLskekfFLLGGLWIALMEG---------ESLQERSY-THIAFQIQS 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489419402  80 EDVGAVIEKLRGEGVSILSE-PKVKPWGQTVaYVADPDGHYIE 121
Cdd:cd08345   71 EDFDRYAERLGALGVEMRPPrPRVEGEGRSI-YFYDPDNHLFE 112
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 7-121 8.92e-04

N-terminal domain of type I, class II extradiol dioxygenases; This family contains the N-terminal non-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: 319967  Cd Length: 111  Bit Score: 36.14  E-value: 8.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   7 YVILYVSDGERSLHFYKDILGLTVRAQhdtyvefDTGSAIL-AFNTRKNVREITpleipeEAGYSQTFELGFVT---EDV 82
Cdd:cd16360    1 YAELGVPDLEKALEFYTDVLGLQVAKR-------DGNSVYLrGYEDEHHSLVLY------EAPEAGLKHFAFEVaseEDL 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489419402  83 GAVIEKLRGEGVSILSEPKVKPWGQTVAY-VADPDGHYIE 121
Cdd:cd16360   68 ERAAASLTALGCDVTWGPDGEVPGGGKGFrFQDPSGHLLE 107
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 4-127 1.10e-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: 36.07  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   4 SMRYVILYVSDGERSLHFYKDILGLTVRAQHDTYVEF-DTGSAILAFNTRKNVREITPLeipeeagysqtFELGFVT-ED 81
Cdd:cd08362    3 HLRYVALGVPDLAAEREFYTEVWGLEEVAEDDDVVYLrAEGSEHHVLRLRQSDENRLDL-----------IAFAAATrAD 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 489419402  82 VGAVIEKLRGEGVSILSEPKV--KPWGQTVAYVADPDGHYIEICSPVE 127
Cdd:cd08362   72 VDALAARLAAAGVRILSEPGPldDPGGGYGFRFFDPDGRTIEVSADVA 119
PRK11478 PRK11478
VOC family protein;
7-122 1.20e-03

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 36.41  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   7 YVILYVSDGERSLHFYKDILGLTVraQHDTY-VEFDTGSAILAFNTRKNVREIT---PLEIPEEAGYSQTFELGFVTEDV 82
Cdd:PRK11478   9 HIAIIATDYAVSKAFYCDILGFTL--QSEVYrEARDSWKGDLALNGQYVIELFSfpfPPERPSRPEACGLRHLAFSVDDI 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489419402  83 GAVIEKLRGEGVSilSEP-KVKPW-GQTVAYVADPDGHYIEI 122
Cdd:PRK11478  87 DAAVAHLESHNVK--CEAiRVDPYtQKRFTFFNDPDGLPLEL 126
VOC_BsYyaH cd07241
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal ...
 4-122 1.43e-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: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   4 SMRYVILYVSDGERSLHFYKDILGLTVRAQHDT--------YVEFDTGsAILAFNTRKNVrEITPLEIpEEAGYSQ-TFE 74
Cdd:cd07241    1 KIEHVALWTNDLERMKDFYVKYFGAESNDIYHNkkkgfrsyFLTFDSG-ARLELMSRPDV-TDPDKEV-ERTGLAHiAFS 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 489419402  75 LGfVTEDVGAVIEKLRGEGVSILSEPKVKPWGQTVAYVADPDGHYIEI 122
Cdd:cd07241   78 VG-SKEAVDELTERLRADGYAVVGGPRTTGDGYYESVILDPEGNRIEI 124
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 6-46 1.50e-03

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


Pssm-ID: 319918  Cd Length: 124  Bit Score: 35.75  E-value: 1.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 489419402   6 RYVILYVSDGERSLHFYKDILGLTVRAQHDTYVEFDTGSAI 46
Cdd:cd07255    4 GRVTLKVADLERQSAFYQNVIGLSVLKQNASRAYLGVDGKQ 44
PRK10291 PRK10291
glyoxalase I; Provisional
 9-122 2.39e-03

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 35.38  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   9 ILYVSDGERSLHFYKDILGLTV-RAQHDTYVEFDtgsaiLAFNTRKNVREITPLEIPEEAGYsQTFELG-------FVTE 80
Cdd:PRK10291   1 MLRVGDLQRSIDFYTNVLGMKLlRTSENPEYKYS-----LAFVGYGPETEEAVIELTYNWGV-DKYELGtayghiaLSVD 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489419402  81 DVGAVIEKLRGEGVSILSEPKVKPWGQTV-AYVADPDGHYIEI 122
Cdd:PRK10291  75 NAAEACEKIRQNGGNVTREAGPVKGGTTViAFVEDPDGYKIEL 117
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 8-121 3.39e-03

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: 34.98  E-value: 3.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419402   8 VILYVSDGERSLHFYKDILGLTVraqhdTYVEFDTGSAILAFNTRKNVRE-----ITPLEIPeeaGYSQT-FELGFVtED 81
Cdd:cd08343    3 VVLCSPDVEASRDFYTDVLGFRV-----SDRIVDPGVDGGAFLHCDRGTDhhtvaLAGGPHP---GLHHVaFEVHDL-DD 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489419402  82 VGAVIEKLRGEGVSILSEPKVKPWGQTV-AYVADPDGHYIE 121
Cdd:cd08343   74 VGRGHDRLREKGYKIEWGPGRHGLGSQVfDYWFDPSGNRVE 114
 
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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