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Conserved domains on  [gi|211959465|gb|EEA94663|]
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glyoxalase/bleomycin resistance protein/dioxygenase [Pseudovibrio sp. JE062]

Protein Classification

VOC family protein( domain architecture ID 10163552)

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

PubMed:  21820381

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 2-120 4.53e-48

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: 319923 [Multi-domain]  Cd Length: 121  Bit Score: 149.69  E-value: 4.53e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465   2 IGYITLGTNDLERACSFYDAILGKMGATRVFENNrlYAWSFG-EGKPLIVLNTPYDGQEASIGNGTMVALRVEDRETVEN 80
Cdd:cd07262    1 ISHVTIGVNDLERSRAFYDAALAPLGYKRGFEDG--GRVGYGlEGGPDFWVTEPFDGEPATAGNGTHVAFAAPSRAAVDA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 211959465  81 LHALALQLGGKDEGPPGPR---GEAFYGAYCRDLDGNKLNFHC 120
Cdd:cd07262   79 FHAAALAAGGTDNGAPGLRphyHPGYYAAYVRDPDGNKIEAVC 121
 
Name Accession Description Interval E-value
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 2-120 4.53e-48

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: 319923 [Multi-domain]  Cd Length: 121  Bit Score: 149.69  E-value: 4.53e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465   2 IGYITLGTNDLERACSFYDAILGKMGATRVFENNrlYAWSFG-EGKPLIVLNTPYDGQEASIGNGTMVALRVEDRETVEN 80
Cdd:cd07262    1 ISHVTIGVNDLERSRAFYDAALAPLGYKRGFEDG--GRVGYGlEGGPDFWVTEPFDGEPATAGNGTHVAFAAPSRAAVDA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 211959465  81 LHALALQLGGKDEGPPGPR---GEAFYGAYCRDLDGNKLNFHC 120
Cdd:cd07262   79 FHAAALAAGGTDNGAPGLRphyHPGYYAAYVRDPDGNKIEAVC 121
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-116 2.16e-18

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: 74.64  E-value: 2.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465   1 MIGYITLGTNDLERACSFYDAILGkmgATRVFENN------RLYAWSFGEGKPLIVLNTPYDGQEASIGNGTMVALRVED 74
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLG---LELVKRTDfgdggfGHAFLRLGDGTELELFEAPGAAPAPGGGGLHHLAFRVDD 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 211959465  75 retVENLHALALQLGGKDEGPPGPRGEAFYGAYCRDLDGNKL 116
Cdd:COG0346   79 ---LDAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLI 117
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-118 1.74e-09

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 51.29  E-value: 1.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465    2 IGYITLGTNDLERACSFYDAILGkMGATRVFENNRLYAW---SFGEGKPLIVLNTPYDGQEASIGNGTM-VALRVEDRET 77
Cdd:pfam00903   2 IDHVALRVGDLEKSLDFYTDVLG-FKLVEETDAGEEGGLrsaFFLAGGRVLELLLNETPPPAAAGFGGHhIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 211959465   78 VENLHALALQLGGKDEGPPGPRGEAFYGAYCRDLDGNKLNF 118
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 2-120 4.53e-48

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: 319923 [Multi-domain]  Cd Length: 121  Bit Score: 149.69  E-value: 4.53e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465   2 IGYITLGTNDLERACSFYDAILGKMGATRVFENNrlYAWSFG-EGKPLIVLNTPYDGQEASIGNGTMVALRVEDRETVEN 80
Cdd:cd07262    1 ISHVTIGVNDLERSRAFYDAALAPLGYKRGFEDG--GRVGYGlEGGPDFWVTEPFDGEPATAGNGTHVAFAAPSRAAVDA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 211959465  81 LHALALQLGGKDEGPPGPR---GEAFYGAYCRDLDGNKLNFHC 120
Cdd:cd07262   79 FHAAALAAGGTDNGAPGLRphyHPGYYAAYVRDPDGNKIEAVC 121
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-116 2.16e-18

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: 74.64  E-value: 2.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465   1 MIGYITLGTNDLERACSFYDAILGkmgATRVFENN------RLYAWSFGEGKPLIVLNTPYDGQEASIGNGTMVALRVED 74
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLG---LELVKRTDfgdggfGHAFLRLGDGTELELFEAPGAAPAPGGGGLHHLAFRVDD 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 211959465  75 retVENLHALALQLGGKDEGPPGPRGEAFYGAYCRDLDGNKL 116
Cdd:COG0346   79 ---LDAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLI 117
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-119 4.76e-14

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 63.12  E-value: 4.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465   1 MIGYITLGTNDLERACSFYDAILGkMGATRVFENNRLYA-WSFGEGKPLIVlntpYDGQEASIGNGTMVALRVEDretVE 79
Cdd:COG3324    4 TIVWVELPVDDLERAKAFYEEVFG-WTFEDDAGPGGDYAeFDTDGGQVGGL----MPGAEEPGGPGWLLYFAVDD---LD 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 211959465  80 NLHALALQLGGKDEGPPGPRGEAFYGAYCRDLDGNKLNFH 119
Cdd:COG3324   76 AAVARVEAAGGTVLRPPTDIPPWGRFAVFRDPEGNRFGLW 115
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 4-118 3.55e-13

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 61.00  E-value: 3.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465   4 YITLGTNDLERACSFYDAIlgkmGATRV--FENNRLYAWSFGEGKPLIVLNTPY-------DGQEASIGNGTMVALRVED 74
Cdd:COG3607    6 FVNLPVADLERSRAFYEAL----GFTFNpqFSDEGAACFVLGEGIVLMLLPREKfatftgkPIADATGFTEVLLALNVES 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 211959465  75 RETVENLHALALQLGGKDEGPPGPRGeAFYGAYCRDLDGNKLNF 118
Cdd:COG3607   82 REEVDALVAKALAAGGTVLKPPQDVG-GMYSGYFADPDGHLWEV 124
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 4-118 1.49e-12

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: 59.08  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465   4 YITLGTNDLERACSFYDAILGkMGATRVFENNRLYAWSFGEGkPLIVLNTPYDGQEASIGNGTMVALRVEDRETVENLHA 83
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLG-FEVVSRNEGGGFAFLRLGPG-LRLALLEGPEPERPGGGGLFHLAFEVDDVDEVDERLR 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 211959465  84 LALQLGGKDEGPPGPRGEaFYGAYCRDLDGNKLNF 118
Cdd:cd06587   79 EAGAEGELVAPPVDDPWG-GRSFYFRDPDGNLIEF 112
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
2-116 3.73e-10

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 53.42  E-value: 3.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465   2 IGYITLGTNDLERACSFYDAILgkmGATRVFENNRLYAWSFGEGKPLIVLNTPYDGQEASIGNG-TMVALRVEDRETVEN 80
Cdd:COG2514    4 LGHVTLRVRDLERSAAFYTDVL---GLEVVEREGGRVYLRADGGEHLLVLEEAPGAPPRPGAAGlDHVAFRVPSRADLDA 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 211959465  81 LHALALQLGGKDEGPPGPRGeaFYGAYCRDLDGNKL 116
Cdd:COG2514   81 ALARLAAAGVPVEGAVDHGV--GESLYFRDPDGNLI 114
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-118 1.74e-09

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 51.29  E-value: 1.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465    2 IGYITLGTNDLERACSFYDAILGkMGATRVFENNRLYAW---SFGEGKPLIVLNTPYDGQEASIGNGTM-VALRVEDRET 77
Cdd:pfam00903   2 IDHVALRVGDLEKSLDFYTDVLG-FKLVEETDAGEEGGLrsaFFLAGGRVLELLLNETPPPAAAGFGGHhIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 211959465   78 VENLHALALQLGGKDEGPPGPRGEAFYGAYCRDLDGNKLNF 118
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 2-114 7.45e-07

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


Pssm-ID: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 44.63  E-value: 7.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465   2 IGYITLGTNDLERACSFYDAILGKmgATRVFENNRLYAwSFGEGKPLIVLNTPYDGQE----ASIGNGTMVALRVEDRE- 76
Cdd:cd07264    1 IAYIVLYVDDFAASLRFYRDVLGL--PPRFLHEEGEYA-EFDTGETKLALFSRKEMARsggpDRRGSAFELGFEVDDVEa 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 211959465  77 TVENLHAL-ALQLGGKDEGPPGPRgeafyGAYCRDLDGN 114
Cdd:cd07264   78 TVEELVERgAEFVREPANKPWGQT-----VAYVRDPDGN 111
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
4-120 3.79e-06

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 42.54  E-value: 3.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465   4 YITLGTNDLERACSFYDAILGkmgATRVFEnnrlyaWSFGEGKPL----------IVLNTPYDGQEASIGNGTMVALRVE 73
Cdd:COG2764    3 TPYLVVDDAEEALEFYEDVFG---FEVVFR------MTDPDGKIMhaelriggsvLMLSDAPPDSPAAEGNGVSLSLYVD 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 211959465  74 DretVENLHALALQLGGKDEGPPGprgEAFYG---AYCRDLDGNKLNFHC 120
Cdd:COG2764   74 D---VDALFARLVAAGATVVMPLQ---DTFWGdrfGMVRDPFGVLWMINT 117
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-113 5.91e-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: 319914 [Multi-domain]  Cd Length: 120  Bit Score: 42.28  E-value: 5.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465   5 ITLGTNDLERACSFYDAilgkMGATRVFENNRLYAWSFGEGKPLIVLntPYDGQEASIG--------NGTMVALRVEDRE 76
Cdd:cd07251    2 ITLGVRDLERSARFYEA----LGWKPNLDPNDGVVFFQLGGTVLALY--PRDALAEDAGvsvtgagfSGVTLAHNVRSRE 75

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 211959465  77 TVENLHALALQLGGKDEGPPGPRGEAFYGAYCRDLDG 113
Cdd:cd07251   76 EVDQLLAKAVAAGGKILKPPQEVFWGGYSGYFADPDG 112
VOC_BsYyaH cd07241
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal ...
 2-116 2.38e-05

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


Pssm-ID: 319905  Cd Length: 125  Bit Score: 40.47  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465   2 IGYITLGTNDLERACSFYDAILGKMgATRVFENN----RLYAWSFGEGKPLIVLNTPY-DGQEASIGNG--TMVALRVED 74
Cdd:cd07241    2 IEHVALWTNDLERMKDFYVKYFGAE-SNDIYHNKkkgfRSYFLTFDSGARLELMSRPDvTDPDKEVERTglAHIAFSVGS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 211959465  75 RETVENLHALALQLGGKDEGPPGPRGEAFYGAYCRDLDGNKL 116
Cdd:cd07241   81 KEAVDELTERLRADGYAVVGGPRTTGDGYYESVILDPEGNRI 122
VOC_BsYqjT cd07242
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; The vicinal ...
 2-116 4.77e-05

vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; 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: 319906  Cd Length: 126  Bit Score: 39.78  E-value: 4.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465   2 IGYITLGTNDLERACSFYDAILGkMGATRVFENNRLYAWSFGEGKPLIVLNTPYDG----QEASIGNGTMvALRVEDRET 77
Cdd:cd07242    2 VSHVELAVSDLHRSFKWFEWILG-LGWKEYDTWSFGPSWKLSGGSLLVVQQTDEFAtpefDRARVGLNHL-AFHAESREA 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 211959465  78 VENLHALALQLGGK---DEGPPGPRGEAFYGAYCRDLDGNKL 116
Cdd:cd07242   80 VDELTEKLAKIGGVrtyGDRHPFAGGPPHYAAFCEDPDGIKL 121
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 2-119 7.12e-05

N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth disturbances caused by high osmolarity and a high concentration of A-factor, a microbial hormone, during the early growth phase in Streptomyces griseus. A-factor (2-isocapryloyl-3R-hydroxymethyl-gamma-butyrolactone) controls morphological differentiation and secondary metabolism in Streptomyces griseus. It is a chemical signaling molecule that at a very low concentration acts as a switch for yellow pigment production, aerial mycelium formation, streptomycin production, and streptomycin resistance. The structure and amino acid sequence of SgaA are closely related to a group of antibiotics resistance proteins, including bleomycin resistance protein, mitomycin resistance protein, and fosfomycin resistance proteins. SgaA might also function as a streptomycin resistance protein.


Pssm-ID: 319911 [Multi-domain]  Cd Length: 114  Bit Score: 39.17  E-value: 7.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465   2 IGYITLGTNDLERACSFYDAILG----KMGAtrvfENNRLYAWSFGEGKPLIVLNTPYDGQEAsiGNGTMVALRVEDret 77
Cdd:cd07247    1 PVWFELPTTDLERAKAFYGAVFGwtfeDEGD----GGGDYALFTAGGGAVGGLMRAPEEVAGA--PPGWLIYFAVDD--- 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 211959465  78 VENLHALALQLGGKDEGPPGPRGEAFYGAYCRDLDGNKLNFH 119
Cdd:cd07247   72 LDAALARVEAAGGKVVVPPTDIPGGGRFAVFADPEGNRFGLW 113
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 4-103 2.37e-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: 37.68  E-value: 2.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465   4 YITLGTNDLERACSFYDAILGKMGATRvfENNRLYAWSFGEGKPLIVLntpYDGQEASIGNgtmVALRVEDRETVENLHA 83
Cdd:cd16360    1 YAELGVPDLEKALEFYTDVLGLQVAKR--DGNSVYLRGYEDEHHSLVL---YEAPEAGLKH---FAFEVASEEDLERAAA 72

                         90       100
                 ....*....|....*....|....*
gi 211959465  84 LALQLG-----GKDEGPPGpRGEAF 103
Cdd:cd16360   73 SLTALGcdvtwGPDGEVPG-GGKGF 96
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 2-120 7.23e-04

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


Pssm-ID: 319918  Cd Length: 124  Bit Score: 36.52  E-value: 7.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465   2 IGYITLGTNDLERACSFYDAILG----KMGATRVfennrlyAWSFGEGKPLIVLN-TPYDGQEASIGNGTM-VALRVEDR 75
Cdd:cd07255    3 IGRVTLKVADLERQSAFYQNVIGlsvlKQNASRA-------YLGVDGKQVLLVLEaIPDAVLAPRSTTGLYhFAILLPDR 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 211959465  76 ETVENLHALALQ----LGGKDEGppgpRGEAFygaYCRDLDGNKLNFHC 120
Cdd:cd07255   76 KALGRALAHLAEhgplIGAADHG----VSEAI---YLSDPEGNGIEIYA 117
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 11-118 5.28e-03

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


Pssm-ID: 319937 [Multi-domain]  Cd Length: 114  Bit Score: 34.12  E-value: 5.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465  11 DLERACSFYDAILG-KMGATRVFE--------NNRLYAWSFGEGKPLivlntpydgqeasiGNGTMVALRVEDretVENL 81
Cdd:cd08349    8 DIDKTLAFYVDVLGfEVDYERPPPgyailsrgGVELHLFEHPGLDPA--------------GSGVAAYIRVED---IDAL 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 211959465  82 HALALQLGGKDEGPP--GPRGEAFYGAYC---RDLDGNKLNF 118
Cdd:cd08349   71 HAELKAAGLPLFGIPriTPIEDKPWGMREfavVDPDGNLLRF 112
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 4-119 6.77e-03

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


Pssm-ID: 319933  Cd Length: 118  Bit Score: 34.07  E-value: 6.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465   4 YITLGTNDLERACSFYDAILGK-MGATRVFENNRLYAWSFGE-GKPLIVLNTPYDGQEASIgngTMVALRVEDretvENL 81
Cdd:cd08345    1 HITLIVRDLEKSTAFLQDIFGArEVYSSGDKTFSLSKEKFFLlGGLWIALMEGESLQERSY---THIAFQIQS----EDF 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 211959465  82 HALALQLG--GKDEGPPGPR----GEAFygaYCRDLDGNKLNFH 119
Cdd:cd08345   74 DRYAERLGalGVEMRPPRPRvegeGRSI---YFYDPDNHLFELH 114
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 11-118 7.47e-03

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


Pssm-ID: 319942  Cd Length: 122  Bit Score: 33.88  E-value: 7.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211959465  11 DLERACSFYDAILgkmGATRVFENNRLYAWSFGEGKPLI---------VLNTPYDGQEASigNGTMVALRVEDRETVE-- 79
Cdd:cd08354   10 DLDAAEAFYEDVL---GLKPMLRSGRHAFFRLGPQVLLVfdpgatskdVRTGEVPGHGAS--GHGHFAFAVPTEELAAwe 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 211959465  80 -NLHALALQLGGKDEGPPGprGEAFygaYCRDLDGNKLNF 118
Cdd:cd08354   85 aRLEAKGVPIESYTQWPEG--GKSL---YFRDPAGNLVEL 119
 
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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