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Conserved domains on  [gi|2124874145|ref|WP_227099012|]
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MULTISPECIES: VOC family protein [Bacillus]

Protein Classification

VOC family protein( domain architecture ID 50733)

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

CATH:  3.10.180.10
Gene Ontology:  GO:0046872|GO:0003824
PubMed:  21820381|11076500

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VOC super family cl14632
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 1-122 6.79e-41

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


The actual alignment was detected with superfamily member pfam12681:

Pssm-ID: 472697  Cd Length: 118  Bit Score: 131.76  E-value: 6.79e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   1 MKYLILYVSDSKRAIHFYRDILGLPIRAEHGTYVEFETGSTIlalntRESARDITALDIPETSASNTFEIGFVTENVETV 80
Cdd:pfam12681   1 FKCPLLVVKDINISRKFYEDVLDQKIKLDFGENVSFEGGFAI-----QSDFKELIGIDLSIAEQSNNFELYFEVADVDAF 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2124874145  81 IKRMREQG-VSIIGEPKVKPWGQTVAYIADPDGHYIEICSPME 122
Cdd:pfam12681  76 LQKIKEIGnIEYLHELKEQPWGQRVFRFYDPDGHIIEIGESME 118
 
Name Accession Description Interval E-value
Glyoxalase_2 pfam12681
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 1-122 6.79e-41

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


Pssm-ID: 403776  Cd Length: 118  Bit Score: 131.76  E-value: 6.79e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   1 MKYLILYVSDSKRAIHFYRDILGLPIRAEHGTYVEFETGSTIlalntRESARDITALDIPETSASNTFEIGFVTENVETV 80
Cdd:pfam12681   1 FKCPLLVVKDINISRKFYEDVLDQKIKLDFGENVSFEGGFAI-----QSDFKELIGIDLSIAEQSNNFELYFEVADVDAF 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2124874145  81 IKRMREQG-VSIIGEPKVKPWGQTVAYIADPDGHYIEICSPME 122
Cdd:pfam12681  76 LQKIKEIGnIEYLHELKEQPWGQRVFRFYDPDGHIIEIGESME 118
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 1-120 1.73e-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: 1.73e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   1 MKYLILYVSDSKRAIHFYRDILGLPIRAEH--GTYVEFETGSTILALNTRESARDITALDiPETSAsntFEIGFVTENVE 78
Cdd:cd07264     1 IAYIVLYVDDFAASLRFYRDVLGLPPRFLHeeGEYAEFDTGETKLALFSRKEMARSGGPD-RRGSA---FELGFEVDDVE 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2124874145  79 TVIKRMREQGVSIIGEPKVKPWGQTVAYIADPDGHYIEICSP 120
Cdd:cd07264    77 ATVEELVERGAEFVREPANKPWGQTVAYVRDPDGNLIEICEP 118
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-122 1.41e-24

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: 90.44  E-value: 1.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   6 LYVSDSKRAIHFYRDILGLPIRAEH------GTYVEFETGS-TILALNTRESARditaldiPETSASNTFEIGFVTENVE 78
Cdd:COG0346     8 LRVSDLEASLAFYTDVLGLELVKRTdfgdggFGHAFLRLGDgTELELFEAPGAA-------PAPGGGGLHHLAFRVDDLD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2124874145  79 TVIKRMREQGVSIIGEPKVKPWGQTVAYIADPDGHYIEICSPME 122
Cdd:COG0346    81 AAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVEPPP 124
PRK04101 PRK04101
metallothiol transferase FosB;
8-116 4.32e-07

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 45.71  E-value: 4.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   8 VSDSKRAIHFYRDILG--LPIRAEHGTYveFETGSTILALNTREsarditalDIP--ETSASNT---FEIGfvTENVETV 80
Cdd:PRK04101   12 VSNLEKSIEFYEKVLGakLLVKGRKTAY--FDLNGLWIALNEEK--------DIPrnEIHQSYThiaFSIE--EEDFDHW 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2124874145  81 IKRMREQGVSII-GEPKVKPWGQTVaYIADPDGHYIE 116
Cdd:PRK04101   80 YQRLKENDVNILpGRERDERDKKSI-YFTDPDGHKFE 115
 
Name Accession Description Interval E-value
Glyoxalase_2 pfam12681
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 1-122 6.79e-41

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


Pssm-ID: 403776  Cd Length: 118  Bit Score: 131.76  E-value: 6.79e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   1 MKYLILYVSDSKRAIHFYRDILGLPIRAEHGTYVEFETGSTIlalntRESARDITALDIPETSASNTFEIGFVTENVETV 80
Cdd:pfam12681   1 FKCPLLVVKDINISRKFYEDVLDQKIKLDFGENVSFEGGFAI-----QSDFKELIGIDLSIAEQSNNFELYFEVADVDAF 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2124874145  81 IKRMREQG-VSIIGEPKVKPWGQTVAYIADPDGHYIEICSPME 122
Cdd:pfam12681  76 LQKIKEIGnIEYLHELKEQPWGQRVFRFYDPDGHIIEIGESME 118
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 1-120 1.73e-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: 1.73e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   1 MKYLILYVSDSKRAIHFYRDILGLPIRAEH--GTYVEFETGSTILALNTRESARDITALDiPETSAsntFEIGFVTENVE 78
Cdd:cd07264     1 IAYIVLYVDDFAASLRFYRDVLGLPPRFLHeeGEYAEFDTGETKLALFSRKEMARSGGPD-RRGSA---FELGFEVDDVE 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2124874145  79 TVIKRMREQGVSIIGEPKVKPWGQTVAYIADPDGHYIEICSP 120
Cdd:cd07264    77 ATVEELVERGAEFVREPANKPWGQTVAYVRDPDGNLIEICEP 118
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-122 1.41e-24

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: 90.44  E-value: 1.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   6 LYVSDSKRAIHFYRDILGLPIRAEH------GTYVEFETGS-TILALNTRESARditaldiPETSASNTFEIGFVTENVE 78
Cdd:COG0346     8 LRVSDLEASLAFYTDVLGLELVKRTdfgdggFGHAFLRLGDgTELELFEAPGAA-------PAPGGGGLHHLAFRVDDLD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2124874145  79 TVIKRMREQGVSIIGEPKVKPWGQTVAYIADPDGHYIEICSPME 122
Cdd:COG0346    81 AAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVEPPP 124
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 3-120 1.88e-20

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 79.68  E-value: 1.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   3 YLILYVSDSKRAIHFYRDILGLPIRAEHG---TYVEFETGS-TILALNTResarditaldiPETSASNTFEIGFVTENVE 78
Cdd:COG3324     7 WVELPVDDLERAKAFYEEVFGWTFEDDAGpggDYAEFDTDGgQVGGLMPG-----------AEEPGGPGWLLYFAVDDLD 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2124874145  79 TVIKRMREQGVSIIGEPK-VKPWGqTVAYIADPDGHYIEICSP 120
Cdd:COG3324    76 AAVARVEAAGGTVLRPPTdIPPWG-RFAVFRDPEGNRFGLWQP 117
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
5-120 1.08e-19

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 77.59  E-value: 1.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   5 ILYVSDSKRAIHFYRDILGLPIRAEHGT------YVEFETGSTILALNTRESarditalDIPETSAsNTFEIGFVTENVE 78
Cdd:COG2764     5 YLVVDDAEEALEFYEDVFGFEVVFRMTDpdgkimHAELRIGGSVLMLSDAPP-------DSPAAEG-NGVSLSLYVDDVD 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2124874145  79 TVIKRMREQGVSIIGEPKVKPWGQTVAYIADPDGHYIEICSP 120
Cdd:COG2764    77 ALFARLVAAGATVVMPLQDTFWGDRFGMVRDPFGVLWMINTP 118
VOC_like cd09011
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 1-121 7.34e-19

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: 75.59  E-value: 7.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   1 MKYL--ILYVSDSKRAIHFYRDILGLPIRAEHGTYVEFETGSTI----LALNTRESArditalDIPETSASNTFEIGFVT 74
Cdd:cd09011     1 MKFVnpLLVVKDIEKSKKFYEDVLGQKILLDFGENVVFEGGFALqekkSWLETIIIS------DLSIKQQSNNFELYFEV 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2124874145  75 ENVETVIKRM-REQGVSIIGEPKVKPWGQTVAYIADPDGHYIEICSPM 121
Cdd:cd09011    75 DDFDAFFEKLnPHKDIEFIHPILEHPWGQRVFRFYDPDGHIIEIGESM 122
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
3-117 2.31e-18

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 74.41  E-value: 2.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   3 YLILYVSDSKRAIHFYRDILGLPIRAEH-------GTYVEFETGSTILALNTRESARDitalDIPETSASNTFEIGFVTE 75
Cdd:pfam00903   4 HVALRVGDLEKSLDFYTDVLGFKLVEETdageeggLRSAFFLAGGRVLELLLNETPPP----AAAGFGGHHIAFIAFSVD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2124874145  76 NVETVIKRMREQGVSIIGEPKVKPWGQTVAYIADPDGHYIEI 117
Cdd:pfam00903  80 DVDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 3-117 1.14e-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: 72.56  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   3 YLILYVSDSKRAIHFYRDILGLPI--RAEHGTYVEFETGS-TILALNTRESARDITALDIpetsasntFEIGFVTENVET 79
Cdd:cd06587     1 HVALRVPDLDASVAFYEEVLGFEVvsRNEGGGFAFLRLGPgLRLALLEGPEPERPGGGGL--------FHLAFEVDDVDE 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2124874145  80 VIKRMREQGV--SIIGEPKVKPWGQTVAYIADPDGHYIEI 117
Cdd:cd06587    73 VDERLREAGAegELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 3-117 2.11e-17

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 72.17  E-value: 2.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   3 YLILYVSDSKRAIHFYRDiLGLPI--RAEHGTYVEFETGSTI-LALNTRESARDITALDIPETSASNTFEIGFVTEN--- 76
Cdd:COG3607     6 FVNLPVADLERSRAFYEA-LGFTFnpQFSDEGAACFVLGEGIvLMLLPREKFATFTGKPIADATGFTEVLLALNVESree 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2124874145  77 VETVIKRMREQGVSIIGEPKVKPWGQTvAYIADPDGHYIEI 117
Cdd:COG3607    85 VDALVAKALAAGGTVLKPPQDVGGMYS-GYFADPDGHLWEV 124
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
1-122 1.37e-16

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 70.37  E-value: 1.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   1 MKYLILYVSDSKRAIHFYRDILGLPIRAEHGTYVEFET--GSTILALNTRESARditaldiPETSASNTFEIGFVTEN-- 76
Cdd:COG2514     4 LGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRAdgGEHLLVLEEAPGAP-------PRPGAAGLDHVAFRVPSra 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2124874145  77 -VETVIKRMREQGVSIIGEpkVKPWGQTVAYIADPDGHYIEICSPME 122
Cdd:COG2514    77 dLDAALARLAAAGVPVEGA--VDHGVGESLYFRDPDGNLIELYTDRP 121
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 6-117 7.62e-16

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: 68.09  E-value: 7.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   6 LYVSDSKRAIHFYRDiLGLPI-RAEHGTYVEFETGSTILALNTRES-ARDITALDipETSASNTFEIGFVT---ENVETV 80
Cdd:cd07251     4 LGVRDLERSARFYEA-LGWKPnLDPNDGVVFFQLGGTVLALYPRDAlAEDAGVSV--TGAGFSGVTLAHNVrsrEEVDQL 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2124874145  81 IKRMREQGVSIIGEPKVKPWGQTVAYIADPDGHYIEI 117
Cdd:cd07251    81 LAKAVAAGGKILKPPQEVFWGGYSGYFADPDGHIWEV 117
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-120 5.06e-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: 63.15  E-value: 5.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   5 ILYVSDSKRAIHFYRDILGLPIRAEHGTYVEFETG-STILALNTRESARDITALDIP--ETSASNTFEIGFVTENVETVI 81
Cdd:cd08354     5 CLYADDLDAAEAFYEDVLGLKPMLRSGRHAFFRLGpQVLLVFDPGATSKDVRTGEVPghGASGHGHFAFAVPTEELAAWE 84

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2124874145  82 KRMREQGVSIIGEPKVKPWGQTVaYIADPDGHYIEICSP 120
Cdd:cd08354    85 ARLEAKGVPIESYTQWPEGGKSL-YFRDPAGNLVELASA 122
EhpR_like cd07261
phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter ...
 5-118 2.58e-13

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: 61.26  E-value: 2.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   5 ILYVSDSKRAIHFYRDILGLPIRAEHGTYVEFE-TGSTILALNTREsarditALDIPETSASNTFEIGFVTENVETVIKR 83
Cdd:cd07261     3 ILYVDNPERSTEFYRFLLGKEPVESSPTFASFVlSGGAKLGLWSSE------EVEPKVAVTGGGAELSFMVPSGEQVDEV 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2124874145  84 MRE---QGVSIIGEPKVKPWGQTVAyIADPDGHYIEIC 118
Cdd:cd07261    77 YAEwkaMGIPIIQEPTTMDFGYTFV-ATDPDGHRLRVC 113
PsjN_like cd16356
Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme ...
 3-117 5.80e-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: 57.82  E-value: 5.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   3 YLILYVSDSKRAIHFYRDILGLP----IRAEHgtYVEFETGSTILALNTREsARDITALDIPETSASNTFEIGFVTENVE 78
Cdd:cd16356     1 YVNIFTADIVALSDFYSELFGLEeifeIRSPI--FRGLRTGDSCLGFNAPE-AYELLGLPEFSDTPGIRILLTFDVDDVE 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2124874145  79 TV---IKRMREQGVSIIGEPKVKPWGQTVAYIADPDGHYIEI 117
Cdd:cd16356    78 AVdrlVPRAAALGATLIKPPYDTYYGWYQAVLLDPEGNVFRI 119
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 6-118 7.84e-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: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 57.69  E-value: 7.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   6 LYVSDSKRAIHFYRDILGLPIRAEH--GTYVEFETGS-----TILALNtrESARDITALDIPEtSASNTFEIGFVTENVE 78
Cdd:cd07263     4 LYVDDQDKALDFYVEKLGFEVVEDVpmGGMRWVTVAPpgspgTSLLLE--PKAHPAQMPQSPE-AAGGTPGILLATDDID 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2124874145  79 TVIKRMREQGVSIIGEPkVKPWGQTVAYIADPDGHYIEIC 118
Cdd:cd07263    81 ATYERLTAAGVTFVQEP-TQMGGGRVANFRDPDGNLFALM 119
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 8-117 3.09e-10

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: 53.51  E-value: 3.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   8 VSDSKRAIHFYRDILGLPIRAEHGTYVEFETGSTILALNTREsarditalDIPETSASNTF-EIGFVT--ENVETVIKRM 84
Cdd:cd08363     8 VSNLNKSIAFYKDVLDAKLLVLGEKTAYFDLNGLWLALNVQE--------DIPRNEISHSYtHIAFSIdeEDLDAFKERL 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2124874145  85 REQGVSII-GEPKVKPWGQTVaYIADPDGHYIEI 117
Cdd:cd08363    80 KDNGVNILeGRKRDILEGQSI-YFTDPDGHLFEL 112
VOC_like cd07238
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 6-119 5.07e-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: 319903  Cd Length: 112  Bit Score: 52.86  E-value: 5.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   6 LYVSDSKRAIHFYRDILGLPIRAEHGTYVEFetgstilALNTRESAR------DITALDIPETSASntfeigfvTENVET 79
Cdd:cd07238     6 IATADPERAAAFYGDHLGLPLVMDHGWIVTF-------ASPGNAHAQislareGGSGTVVPDLSIE--------VDDVDA 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2124874145  80 VIKRMREQGVSIIGEPKVKPWGQTVAYIADPDGHYIEICS 119
Cdd:cd07238    71 VHARVVAAGLRIEYGPTTEAWGVRRFFVRDPFGRLINILT 110
MRD cd07235
Mitomycin C resistance protein (MRD); Mitomycin C (MC) is a naturally occurring antibiotic, ...
 6-117 5.75e-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: 5.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   6 LYVSDSKRAIHFYRdILGLPIRAEHGT--YVEFE-TGSTILALNTRESARDITALDIPETSAsNTFEIGFVTE---NVET 79
Cdd:cd07235     6 IVVEDMAKSLEFYR-KLGFEVPEEADSapHTEAAlPGGIRLALDTEETIRSYDPGWQAPTGG-GRFAIAFLCPtpaEVDA 83

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2124874145  80 VIKRMREQGVSIIGEPKVKPWGQTVAYIADPDGHYIEI 117
Cdd:cd07235    84 KYAELTGAGYEGHLKPWNAPWGQRYAIVKDPDGNVVDL 121
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 5-118 3.72e-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: 50.30  E-value: 3.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   5 ILYVSDSKRAIHFYRDILGLPIRAEHG--TYVefetgstILALNTRESARDITALDIPETSASNTFeigFVTENVETVIK 82
Cdd:cd08349     3 ILPVRDIDKTLAFYVDVLGFEVDYERPppGYA-------ILSRGGVELHLFEHPGLDPAGSGVAAY---IRVEDIDALHA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2124874145  83 RMREQGVSIIGEPKV-----KPWGQTVAYIADPDGHYIEIC 118
Cdd:cd08349    73 ELKAAGLPLFGIPRItpiedKPWGMREFAVVDPDGNLLRFG 113
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 6-115 3.95e-09

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: 50.34  E-value: 3.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   6 LYVSDSKRAIHFYRDILGLPIRAEH---GTYVEFETGSTILAlntresarDITALDIPETSASNTFEIGFVTENVETVIK 82
Cdd:cd07247     6 LPTTDLERAKAFYGAVFGWTFEDEGdggGDYALFTAGGGAVG--------GLMRAPEEVAGAPPGWLIYFAVDDLDAALA 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2124874145  83 RMREQGVSIIGEPKVKPWGQTVAYIADPDGHYI 115
Cdd:cd07247    78 RVEAAGGKVVVPPTDIPGGGRFAVFADPEGNRF 110
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 1-120 6.11e-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: 49.92  E-value: 6.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   1 MKYLILYVSDSKRAIHFYRDILGLpiraehgTYVEFETGSTilALNTRESARDITALDIP-----ETSASNTFEIGFVTE 75
Cdd:cd07253     4 LDHLVLTVKDIERTIDFYTKVLGM-------TVVTFKEGRK--ALRFGNQKINLHQKGKEfepkaSAPTPGSADLCFITE 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2124874145  76 -NVETVIKRMREQGVSIIgEPKVKPWGQ----TVAYIADPDGHYIEICSP 120
Cdd:cd07253    75 tPIDEVLEHLEACGVTIE-EGPVKRTGAlgpiLSIYFRDPDGNLIELSNY 123
VOC_like cd07246
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 6-120 1.02e-08

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


Pssm-ID: 319910 [Multi-domain]  Cd Length: 124  Bit Score: 49.60  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   6 LYVSDSKRAIHFYRDILG------LPIRAEHGTYVEFETGSTILALNTRESARDITAldiPETSASNTFEIGFVTENVET 79
Cdd:cd07246     7 LVVEDAAAAIAFYKKAFGaeelgrTTQEDGRVGHAELRIGGTVVMVADENPERGALS---PTKLGGTPVIFHLYVEDVDA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2124874145  80 VIKRMREQGVSIIGEPKVKPWGQTVAYIADPDGHYIEICSP 120
Cdd:cd07246    84 TFARAVAAGAVVVEPVEDQFWGDRVGKVKDPFGHVWWLATP 124
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 6-117 3.14e-08

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: 48.05  E-value: 3.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   6 LYVSDSKRAIHFYRDILGLPIRA--EHGTYVEFetGSTILALN---TRESARDIT--ALDIPEtsasntfeigfvtENVE 78
Cdd:cd07244     7 LAVSDLERSLAFYVDLLGFKPHVrwDKGAYLTA--GDLWLCLSldpAAEPSPDYThiAFTVSE-------------EDFE 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2124874145  79 TVIKRMREQGVSIigepkvkpWGQTVA-----YIADPDGHYIEI 117
Cdd:cd07244    72 ELSERLRAAGVKI--------WQENSSegdslYFLDPDGHKLEL 107
PRK04101 PRK04101
metallothiol transferase FosB;
8-116 4.32e-07

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 45.71  E-value: 4.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   8 VSDSKRAIHFYRDILG--LPIRAEHGTYveFETGSTILALNTREsarditalDIP--ETSASNT---FEIGfvTENVETV 80
Cdd:PRK04101   12 VSNLEKSIEFYEKVLGakLLVKGRKTAY--FDLNGLWIALNEEK--------DIPrnEIHQSYThiaFSIE--EEDFDHW 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2124874145  81 IKRMREQGVSII-GEPKVKPWGQTVaYIADPDGHYIE 116
Cdd:PRK04101   80 YQRLKENDVNILpGRERDERDKKSI-YFTDPDGHKFE 115
VOC_like cd08359
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 17-117 7.54e-07

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


Pssm-ID: 319947 [Multi-domain]  Cd Length: 119  Bit Score: 44.70  E-value: 7.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145  17 FYRDILGLPIRAEHGTYVEFE----TGSTILALNTRESArditaldIPETSASNTFE--IGFVTENVETVIKRMREQGVS 90
Cdd:cd08359    18 FYVKHFGFRVIFDSDWYVSLRraerHGFELAIMDGQHGA-------VPAASQTQSSGliINFEVDDADAEYERLTQAGLE 90

                          90       100
                  ....*....|....*....|....*..
gi 2124874145  91 IIGEPKVKPWGQTVAYIADPDGHYIEI 117
Cdd:cd08359    91 FLEPPRDEPWGQRRFIVRDPNGVLIDV 117
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 8-117 2.37e-06

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: 43.30  E-value: 2.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   8 VSDSKRAIHFYRDILGLPIRAEH-----GTY-VEFETGSTILALNTRESARDitALDIPEtsASNTFEIGFVTENVETVI 81
Cdd:cd08352    10 CSDYEKSKDFYVDKLGFEIIREHyrperNDIkLDLALGGYQLELFIKPDAPA--RPSYPE--ALGLRHLAFKVEDVEATV 85

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2124874145  82 KRMREQGVSIigEP-KVKPW-GQTVAYIADPDGHYIEI 117
Cdd:cd08352    86 AELKSLGIET--EPiRVDDFtGKKFTFFFDPDGLPLEL 121
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 8-119 8.16e-06

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: 42.32  E-value: 8.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   8 VSDSKRAIHFYRDILGL------------PIRAEHGTYVEFETGSTILA-----------LNTRESARDITALDIPETSA 64
Cdd:cd16361     9 VPDLDAAVEFYTDVLGAevvyrstplaegDRGGGEMRAAGFVPGFARARiamlrlgpgpgIELFEYKGPEQRAPVPRNSD 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145  65 SNTFEIGFVTENVETVIKRMREQGVSIIGEPKVKPWGQ-----TVAYIADPDGHYIEICS 119
Cdd:cd16361    89 VGIFHFALQVDDVEAAAERLAAAGGKVLMGPREIPDGGpgkgnRMVYLRDPWGTLIELVS 148
VOC_like cd16355
uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily; The vicinal oxygen ...
 5-113 1.39e-05

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: 41.32  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   5 ILYVSDSKRAIHFYRDILGLPIRAEHGTYVEFETGST-----ILALNTRESARDITALDIPETSASNTFEIgfVTENVET 79
Cdd:cd16355     4 VLNVSDIPASFAWFEKVLGFQKDWDWGDPPTFGSVGSgeceiFLCQGGQGGSLRLGPCGDALPSYGAWMSV--WVDDVDA 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2124874145  80 VIKRMREQGVSIIGEPKVKPWGQTVAYIADPDGH 113
Cdd:cd16355    82 LHRECRARGADIRQPPTDMPWGMREMHVRHPDGH 115
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 1-117 1.52e-05

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: 41.23  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   1 MKYLILYVSDSKRAIHFYRDILGLPIRAEHgtyvEFETGSTILALNTRESARDITALDIPETSASNTFEIG-------FV 73
Cdd:cd16358     1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKR----DYPEGKYTLAFVGYGDEDENTVLELTYNWGVDKYDLGtayghiaIG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2124874145  74 TENVETVIKRMREQGVSIIGEPKVKPWGQTV-AYIADPDGHYIEI 117
Cdd:cd16358    77 VEDVYETCERIRKKGGKVTREPGPMKGGTTViAFVEDPDGYKIEL 121
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 6-117 1.54e-05

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: 41.54  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   6 LYVSDSKRAIHFYRDILGLPI--RAEHGT------YVEFETGSTILALNTRESARDITAL------------DIPETSAS 65
Cdd:cd07233     6 LRVKDPKKSLKFYTEVLGMKLlrKKDFPEmkfslyFLGYEDPKDIPKDPRTAWVFSREGTlelthnwgtendEDPVYHNG 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145  66 NT-----FEIGFVTENVETVIKRMREQGVSIIGEP---KVKpwgqTVAYIADPDGHYIEI 117
Cdd:cd07233    86 NSdprgfGHIGIAVDDVYAACERFEELGVKFKKKPddgKMK----GIAFIKDPDGYWIEI 141
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 8-118 1.73e-05

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: 41.02  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   8 VSDSKRAIHFYRDILGLP-----IRAEHGTYVEF-ETGSTILALntresardITALDipETSASNTFE---------IGF 72
Cdd:cd07249     8 VPDLDEALKFYEDVLGVKvsepeELEEQGVRVAFlELGNTQIEL--------LEPLG--EDSPIAKFLdkkggglhhIAF 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2124874145  73 VTENVETVIKRMREQGVSIIGE-PKVKPWGQTVAYI--ADPDGHYIEIC 118
Cdd:cd07249    78 EVDDIDAAVEELKAQGVRLLSEgPRIGAHGKRVAFLhpKDTGGVLIELV 126
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-117 4.16e-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: 39.99  E-value: 4.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   8 VSDSKRAIHFYRDILGLPI--RAEHGTY--VEFETGS-TILALNTRESARDITALDIPETSAsntfEIGFVTENVETVIK 82
Cdd:cd07245     8 CPDLERARRFYTDVLGLEEvpRPPFLKFggAWLYLGGgQQIHLVVEQNPSELPRPEHPGRDR----HPSFSVPDLDALKQ 83

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2124874145  83 RMREQGVSIIgEPKVKPWGQTVAYIADPDGHYIEI 117
Cdd:cd07245    84 RLKEAGIPYT-ESTSPGGGVTQLFFRDPDGNRLEF 117
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 4-116 1.97e-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: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   4 LILYVSDSKRAIHFYRDILGLPIraehgTYVEFETGSTILALNTRESARDITALDIPETSASNTFEIGFVTENVETVIK- 82
Cdd:cd08343     3 VVLCSPDVEASRDFYTDVLGFRV-----SDRIVDPGVDGGAFLHCDRGTDHHTVALAGGPHPGLHHVAFEVHDLDDVGRg 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2124874145  83 --RMREQGVSI-IGEPKVKPWGQTVAYIADPDGHYIE 116
Cdd:cd08343    78 hdRLREKGYKIeWGPGRHGLGSQVFDYWFDPSGNRVE 114
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 3-116 2.45e-04

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


Pssm-ID: 319933  Cd Length: 118  Bit Score: 37.92  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   3 YLILYVSDSKRAIHFYRDILGLPIRAEHGTYVE-------FETGSTILALNTREsarditalDIPETSaSNTFEIGFVTE 75
Cdd:cd08345     1 HITLIVRDLEKSTAFLQDIFGAREVYSSGDKTFslskekfFLLGGLWIALMEGE--------SLQERS-YTHIAFQIQSE 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2124874145  76 NVETVIKRMREQGVSII-GEPKVKPWGQTVaYIADPDGHYIE 116
Cdd:cd08345    72 DFDRYAERLGALGVEMRpPRPRVEGEGRSI-YFYDPDNHLFE 112
ChaP_like cd08351
ChaP, an enzyme involved in the biosynthesis of the antitumor agent chartreusin (cha), and ...
 5-117 2.46e-04

ChaP, an enzyme involved in the biosynthesis of the antitumor agent chartreusin (cha), and similar proteins; ChaP is an enzyme involved in the biosynthesis of the potent antitumor agent chartreusin (cha). Cha is an aromatic polyketide glycoside produced by Streptomyces chartreusis. ChaP may play a role as a meta-cleavage dioxygenase in the oxidative rearrangement of the anthracyclic polyketide. ChaP belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases.


Pssm-ID: 319939  Cd Length: 118  Bit Score: 37.87  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   5 ILYVSDSKRAIHFYRDILGLPIRAEHGTYVEFETGSTILaLNTRESARDIT----ALDIPETsasnTFEIGFvtenvetv 80
Cdd:cd08351     7 IVPARDKEASARFLAEILGLPAPPPWGPFAPVRLNNGLT-LDFADPRGEIApqhyAFLVSDD----EFDAIL-------- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2124874145  81 iKRMREQGVSIIGEPKVKPWGQT-------VAYIADPDGHYIEI 117
Cdd:cd08351    74 -ARIRARGLEYWADPQHREPGEInhndggrGVYFRDPDGHLLEI 116
PRK10291 PRK10291
glyoxalase I; Provisional
 5-117 4.52e-04

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 37.31  E-value: 4.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   5 ILYVSDSKRAIHFYRDILGLP-IRAEHGTYVEFETGSTILALNTRESARDIT-ALDIPETSASNTF-EIGFVTENVETVI 81
Cdd:PRK10291    1 MLRVGDLQRSIDFYTNVLGMKlLRTSENPEYKYSLAFVGYGPETEEAVIELTyNWGVDKYELGTAYgHIALSVDNAAEAC 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2124874145  82 KRMREQGVSIIGEPKVKPWGQTV-AYIADPDGHYIEI 117
Cdd:PRK10291   81 EKIRQNGGNVTREAGPVKGGTTViAFVEDPDGYKIEL 117
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-117 5.00e-04

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


Pssm-ID: 319917 [Multi-domain]  Cd Length: 120  Bit Score: 37.06  E-value: 5.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   3 YLILYVSDSKRAIHFYRDILGLPIRAEHGTYVEF--ETGSTILALNTResarditaldiPETSASNTFEIGFVTENVETV 80
Cdd:cd07254     4 HLSLNVTDLERSIRFYSDLFGAEPAKRKADYAKFmlEDPPLNLALLVN-----------DRKEPYGLNHLGIQVDSKEEV 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2124874145  81 I---KRMREQGVSIIGEPKVKpWGQTVA---YIADPDGHYIEI 117
Cdd:cd07254    73 AalkARAEAAGLPVRKEPRTT-CCYAVQdkfWLTDPDGNAWEF 114
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 70-117 5.68e-04

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 37.49  E-value: 5.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2124874145  70 IGFVTENVETVIKRMREQGVSIIGEP---KVKpwgqTVAYIADPDGHYIEI 117
Cdd:PLN03042  125 IGITVDDVYKACERFEKLGVEFVKKPddgKMK----GLAFIKDPDGYWIEI 171
Glyoxalase_6 pfam18029
Glyoxalase-like domain; This entry comprises a diverse set of domains related to the ...
 8-118 8.86e-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: 36.20  E-value: 8.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   8 VSDSKRAIHFYRDILGLPIRAEHGTYVEFETGSTILALNTR---ESARDitaldipETSASNTFEIGFVTENVETVIKRM 84
Cdd:pfam18029   6 CADPAALAAFWSAALGWEVVPDDTALPDPDGGGPIGGGGPRllfQRVPE-------PKPGKNRVHLDLAVDDLEAAVARL 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2124874145  85 REQGVSIIGEPkvKPWGQTVAYIADPDGHyiEIC 118
Cdd:pfam18029  79 VALGATVLDDG--DDPDGGRWVLADPEGN--EFC 108
PLN02367 PLN02367
lactoylglutathione lyase
 70-117 1.28e-03

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 36.90  E-value: 1.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2124874145  70 IGFVTENVETVIKRMREQGVSIIGEP---KVKpwgqTVAYIADPDGHYIEI 117
Cdd:PLN02367  173 IGITVDDVYKACERFEELGVEFVKKPndgKMK----GIAFIKDPDGYWIEI 219
VOC_BsYyaH cd07241
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal ...
 75-117 2.33e-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: 35.46  E-value: 2.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2124874145  75 ENVETVIKRMREQGVSIIGEPKVKPWGQTVAYIADPDGHYIEI 117
Cdd:cd07241    82 EAVDELTERLRADGYAVVGGPRTTGDGYYESVILDPEGNRIEI 124
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 2-119 3.76e-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: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   2 KYLILYVSDSKRAIHFYRDILGLPIRAEHGTYVEFE-TGSTILALNTRESARDitALDIPETSASNTFEigfvtenVETV 80
Cdd:cd08362     5 RYVALGVPDLAAEREFYTEVWGLEEVAEDDDVVYLRaEGSEHHVLRLRQSDEN--RLDLIAFAAATRAD-------VDAL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2124874145  81 IKRMREQGVSIIGEPKV--KPWGQTVAYIADPDGHYIEICS 119
Cdd:cd08362    76 AARLAAAGVRILSEPGPldDPGGGYGFRFFDPDGRTIEVSA 116
VOC_like cd08357
uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and ...
 8-117 3.98e-03

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: 34.67  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124874145   8 VSDSKRAIHFYRDILGLPIRAEHGTYVEFET-GSTILALNTRESARDITALDIPETSASNTFEIGFVTENVETVIKRMRE 86
Cdd:cd08357     7 VRDLEAARDFYGDVLGCPEGRSSETWIDFNFfGHQVVAHLVPNYASTSTNAVDGHSVPVPHFGLALTVDDFDALAERLKA 86

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2124874145  87 QGVSIIGEPKV----KPWGQTVAYIADPDGHYIEI 117
Cdd:cd08357    87 AGVKFYIEPYVrfegEPGEQWTMFLLDPSGNALEF 121
 
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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