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Conserved domains on  [gi|2473401057|gb|WEZ69570|]
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VOC family protein [Bacillus subtilis]

Protein Classification

VOC family protein( domain architecture ID 10170093)

vicinal oxygen chelate (VOC) family protein similar to Escherichia coli YaeR protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 4-127 1.99e-77

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: 224.34  E-value: 1.99e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   4 KSIHHIAIICSDYEKSKAFYVHKLGFQVIQETYREERGSYKLDLSLnGSYVIELFSFPDPPERQTRPEAAGLRHLAFTVG 83
Cdd:cd08352     1 KKIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDIKLDLAL-GGYQLELFIKPDAPARPSYPEALGLRHLAFKVE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2473401057  84 SLDKAVQELHEKGIETEPIRTDPLTGKRFTFFFDPDQLPLELYE 127
Cdd:cd08352    80 DVEATVAELKSLGIETEPIRVDDFTGKKFTFFFDPDGLPLELYE 123
 
Name Accession Description Interval E-value
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 4-127 1.99e-77

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: 224.34  E-value: 1.99e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   4 KSIHHIAIICSDYEKSKAFYVHKLGFQVIQETYREERGSYKLDLSLnGSYVIELFSFPDPPERQTRPEAAGLRHLAFTVG 83
Cdd:cd08352     1 KKIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDIKLDLAL-GGYQLELFIKPDAPARPSYPEALGLRHLAFKVE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2473401057  84 SLDKAVQELHEKGIETEPIRTDPLTGKRFTFFFDPDQLPLELYE 127
Cdd:cd08352    80 DVEATVAELKSLGIETEPIRVDDFTGKKFTFFFDPDGLPLELYE 123
PRK11478 PRK11478
VOC family protein;
3-128 5.83e-66

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 195.88  E-value: 5.83e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   3 LKSIHHIAIICSDYEKSKAFYVHKLGFQVIQETYREERGSYKLDLSLNGSYVIELFSFPDPPERQTRPEAAGLRHLAFTV 82
Cdd:PRK11478    4 LKQVHHIAIIATDYAVSKAFYCDILGFTLQSEVYREARDSWKGDLALNGQYVIELFSFPFPPERPSRPEACGLRHLAFSV 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2473401057  83 GSLDKAVQELHEKGIETEPIRTDPLTGKRFTFFFDPDQLPLELYEQ 128
Cdd:PRK11478   84 DDIDAAVAHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLELYEQ 129
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-127 3.45e-35

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: 117.79  E-value: 3.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   6 IHHIAIICSDYEKSKAFYVHKLGFQVIQETYREERGSYKLDLSLNGSYVIELFSFPDPperQTRPEAAGLRHLAFTVGSL 85
Cdd:COG0346     3 LHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTELELFEAPGA---APAPGGGGLHHLAFRVDDL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2473401057  86 DKAVQELHEKGIETEPIRTDPLTGKRFTFFFDPDQLPLELYE 127
Cdd:COG0346    80 DAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVE 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
5-125 8.16e-31

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 106.38  E-value: 8.16e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   5 SIHHIAIICSDYEKSKAFYVHKLGFQVIQETYREERGSYKLDLSLNGSYVIELFSFPDPPERQTRPEAAGLRHLAFTVGS 84
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2473401057  85 LDKAVQELHEKGIETEPIRTDPLTGKRFTFFFDPDQLPLEL 125
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 4-127 1.99e-77

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: 224.34  E-value: 1.99e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   4 KSIHHIAIICSDYEKSKAFYVHKLGFQVIQETYREERGSYKLDLSLnGSYVIELFSFPDPPERQTRPEAAGLRHLAFTVG 83
Cdd:cd08352     1 KKIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDIKLDLAL-GGYQLELFIKPDAPARPSYPEALGLRHLAFKVE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2473401057  84 SLDKAVQELHEKGIETEPIRTDPLTGKRFTFFFDPDQLPLELYE 127
Cdd:cd08352    80 DVEATVAELKSLGIETEPIRVDDFTGKKFTFFFDPDGLPLELYE 123
PRK11478 PRK11478
VOC family protein;
3-128 5.83e-66

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 195.88  E-value: 5.83e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   3 LKSIHHIAIICSDYEKSKAFYVHKLGFQVIQETYREERGSYKLDLSLNGSYVIELFSFPDPPERQTRPEAAGLRHLAFTV 82
Cdd:PRK11478    4 LKQVHHIAIIATDYAVSKAFYCDILGFTLQSEVYREARDSWKGDLALNGQYVIELFSFPFPPERPSRPEACGLRHLAFSV 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2473401057  83 GSLDKAVQELHEKGIETEPIRTDPLTGKRFTFFFDPDQLPLELYEQ 128
Cdd:PRK11478   84 DDIDAAVAHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLELYEQ 129
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-127 3.45e-35

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: 117.79  E-value: 3.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   6 IHHIAIICSDYEKSKAFYVHKLGFQVIQETYREERGSYKLDLSLNGSYVIELFSFPDPperQTRPEAAGLRHLAFTVGSL 85
Cdd:COG0346     3 LHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTELELFEAPGA---APAPGGGGLHHLAFRVDDL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2473401057  86 DKAVQELHEKGIETEPIRTDPLTGKRFTFFFDPDQLPLELYE 127
Cdd:COG0346    80 DAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVE 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
5-125 8.16e-31

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 106.38  E-value: 8.16e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   5 SIHHIAIICSDYEKSKAFYVHKLGFQVIQETYREERGSYKLDLSLNGSYVIELFSFPDPPERQTRPEAAGLRHLAFTVGS 84
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2473401057  85 LDKAVQELHEKGIETEPIRTDPLTGKRFTFFFDPDQLPLEL 125
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
3-126 3.39e-18

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 74.61  E-value: 3.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   3 LKSIHHIAIICSDYEKSKAFYVHKLGFQVIQetyREERGSYkldLSLNGSY-VIELFSFPDPPErqtRPEAAGLRHLAFT 81
Cdd:COG2514     1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVE---REGGRVY---LRADGGEhLLVLEEAPGAPP---RPGAAGLDHVAFR 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2473401057  82 VGS---LDKAVQELHEKGIETEPIrTDPLTGKRFtFFFDPDQLPLELY 126
Cdd:COG2514    72 VPSradLDAALARLAAAGVPVEGA-VDHGVGESL-YFRDPDGNLIELY 117
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 8-125 1.51e-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: 72.17  E-value: 1.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   8 HIAIICSDYEKSKAFYVHKLGFQVIqetyREERGSYKLDLSLNGSYVIELFSFPDPPerqtRPEAAGLRHLAFTVGSLDK 87
Cdd:cd06587     1 HVALRVPDLDASVAFYEEVLGFEVV----SRNEGGGFAFLRLGPGLRLALLEGPEPE----RPGGGGLFHLAFEVDDVDE 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2473401057  88 AVQELHEKGIETEPIRTDPLT--GKRFTFFFDPDQLPLEL 125
Cdd:cd06587    73 VDERLREAGAEGELVAPPVDDpwGGRSFYFRDPDGNLIEF 112
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 6-125 2.61e-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: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 64.26  E-value: 2.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   6 IHHIAIICSDYEKSKAFYVHKLGFQVIQetyREERGSYKLD-LSLNGSYVIELfSFPDPPERQTRPEAAG-LRHLAFTVG 83
Cdd:cd07245     1 LDHVALACPDLERARRFYTDVLGLEEVP---RPPFLKFGGAwLYLGGGQQIHL-VVEQNPSELPRPEHPGrDRHPSFSVP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2473401057  84 SLDKAVQELHEKGIETEPiRTDPLTGKRFTFFFDPDQLPLEL 125
Cdd:cd07245    77 DLDALKQRLKEAGIPYTE-STSPGGGVTQLFFRDPDGNRLEF 117
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 5-126 3.68e-12

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: 59.27  E-value: 3.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   5 SIHHIAIICSDYEKSKAFYVHKLGFQVI-QETYREERGS------YKLD-----------LSLNGSYVIELFSFPDPPER 66
Cdd:cd16361     1 GVNHVGITVPDLDAAVEFYTDVLGAEVVyRSTPLAEGDRgggemrAAGFvpgfarariamLRLGPGPGIELFEYKGPEQR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2473401057  67 QTRPEAA--GLRHLAFTVGSLDKAVQELHEKGIE--TEPIRT---DPLTGKRFTFFFDPDQLPLELY 126
Cdd:cd16361    81 APVPRNSdvGIFHFALQVDDVEAAAERLAAAGGKvlMGPREIpdgGPGKGNRMVYLRDPWGTLIELV 147
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 5-127 4.23e-12

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 58.49  E-value: 4.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   5 SIHHIAIICSDYEKSKAFYVHKLGFQVIQETyrEERGSYkLDLSLNGSYVIELFSFPDPPerqtrpeAAGLRHLAFTVGS 84
Cdd:COG3324     4 TIVWVELPVDDLERAKAFYEEVFGWTFEDDA--GPGGDY-AEFDTDGGQVGGLMPGAEEP-------GGPGWLLYFAVDD 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2473401057  85 LDKAVQELHEKGIE-TEPIRTDPLTGkRFTFFFDPDQLPLELYE 127
Cdd:COG3324    74 LDAAVARVEAAGGTvLRPPTDIPPWG-RFAVFRDPEGNRFGLWQ 116
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-114 5.26e-12

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 58.06  E-value: 5.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   7 HHIAIICSDYEKSKAFYVHKLGFQVIQEtYREERGSYKLDLSL--NGSYVIELFSfPDPPERQTRPEAAGLRHLAFTVGS 84
Cdd:pfam13669   1 HHVGIAVPDLDRALALWGALLGLGPEGD-YRSEPQNVDLAFALlgDGPVEVELIQ-PLDGDSPLARHGPGLHHLAYWVDD 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2473401057  85 LDKAVQELHEKGIE--TEPIRtDPLTGKRFTF 114
Cdd:pfam13669  79 LDAAVARLLDQGYRvaPKGPR-AGAAGRRVAF 109
VOC_like cd08353
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-99 1.31e-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: 319941  Cd Length: 142  Bit Score: 54.89  E-value: 1.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   3 LKSIHHIAIICSDYEKSKAFYVhKLGFQVIQETYRE----ER----GSYKLDLSL----NGSYVIELFSFPDPP----ER 66
Cdd:cd08353     1 IKRMDHVGIVVEDLDAAIAFFT-ELGLELEGRMTVEgewaDRvvglDGVRVEIAMlrtpDGHGRLELSKFLTPAaipgHR 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2473401057  67 QTRPEAAGLRHLAFTVGSLDKAVQELHEKGIET 99
Cdd:cd08353    80 PAPANALGLRHVAFAVDDIDAVVARLRKHGAEL 112
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 6-119 4.67e-10

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: 53.35  E-value: 4.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   6 IHHIAIICSDYEKSKAFYVHKLGFQVIQETYREERGsYKLDLSLNGSYVIEL---FSFPDPPERQTRPEAAGLRHLAFTV 82
Cdd:cd07249     1 LDHIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQG-VRVAFLELGNTQIELlepLGEDSPIAKFLDKKGGGLHHIAFEV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2473401057  83 GSLDKAVQELHEKGI----ETEPIRTDpltGKRFTFFFDPD 119
Cdd:cd07249    80 DDIDAAVEELKAQGVrllsEGPRIGAH---GKRVAFLHPKD 117
Glyoxalase_3 pfam13468
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 6-122 1.47e-09

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


Pssm-ID: 433233  Cd Length: 175  Bit Score: 53.11  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   6 IHHIAIICSDYEKSKAFYVHKLGFQVIQETYREERGSYKLDLSLNGSYvIELFSfPDPPERQTRPEAA----------GL 75
Cdd:pfam13468   1 LDHVVLAVPDLDEAAARFARALGFTVTPGGRHPGMGTANALIMFGDGY-LELLA-VDPEAPAPPRGRWfgldrladgeGL 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2473401057  76 RHLAFTVGSLDKAVQELHEKGIET-EPIRTDpltGKRFTF---FFDPDQLP 122
Cdd:pfam13468  79 LGWALRTDDIDAVAARLRAAGVEPgRRVRPD---GGDLRWrllFLADGALP 126
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-119 1.75e-09

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


Pssm-ID: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 51.53  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   8 HIAIICSDYEKSKAFYVHKLGFQVIQEtyrEERGSYK-LDLSLNGSYVIELFSFPD--PPERQTRPEAAG-LRHLAFTVG 83
Cdd:cd07263     1 QVMLYVDDQDKALDFYVEKLGFEVVED---VPMGGMRwVTVAPPGSPGTSLLLEPKahPAQMPQSPEAAGgTPGILLATD 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2473401057  84 SLDKAVQELHEKGIETEPIRTDPLTGkRFTFFFDPD 119
Cdd:cd07263    78 DIDATYERLTAAGVTFVQEPTQMGGG-RVANFRDPD 112
VOC_BsYyaH cd07241
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal ...
 5-95 5.49e-09

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: 50.49  E-value: 5.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   5 SIHHIAIICSDYEKSKAFYVHKLGfQVIQETYREERGSYK-LDLSLNGSYVIELFSFPDPPERQTRPEAAGLRHLAFTVG 83
Cdd:cd07241     1 KIEHVALWTNDLERMKDFYVKYFG-AESNDIYHNKKKGFRsYFLTFDSGARLELMSRPDVTDPDKEVERTGLAHIAFSVG 79

                          90
                  ....*....|..
gi 2473401057  84 SlDKAVQELHEK 95
Cdd:cd07241    80 S-KEAVDELTER 90
HPCD_N_class_II cd07266
N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 8-126 4.85e-08

N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily contains the N-terminal, non-catalytic, domain of HPCD. HPCD catalyses the second step in the degradation of 4-hydroxyphenylacetate to succinate and pyruvate. The aromatic ring of 4-hydroxyphenylacetate is opened by this dioxygenase to yield the 3,4-diol product, 2-hydroxy-5-carboxymethylmuconate semialdehyde. HPCD is a homotetramer and each monomer contains two structurally homologous barrel-shaped domains at the N- and C-terminus. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism. Most extradiol dioxygenases contain Fe(II) in their active site, but HPCD can be activated by either Mn(II) or Fe(II). These enzymes belong to the type I class II family of extradiol dioxygenases. The class III 3,4-dihydroxyphenylacetate 2,3-dioxygenases belong to a different superfamily.


Pssm-ID: 319927  Cd Length: 118  Bit Score: 47.79  E-value: 4.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   8 HIAIICSDYEKSKAFYVHKLGFQViqeTYREERGSYKLDLSLNGSYVIELfsfpdpperqTRPEAAGLRHLAFTVG---S 84
Cdd:cd07266     7 HAELVVTDLAASREFYVDTLGLHV---TDEDDNAIYLRGVEEFIHHTLVL----------RKAPEAAVGHLGFRVRdeaD 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2473401057  85 LDKAVQELHEKGIETEpIRTDPLTGK--RFTfffDPDQLPLELY 126
Cdd:cd07266    74 LDKAAAFYKELGLPTE-WREEPGQGRtlRVE---DPFGFPIEFY 113
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 8-119 1.18e-07

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: 46.93  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   8 HIAIICSDYEKSKAFYVHKLGFQVIQETYRE--ERGSYkldLSLN-GSYVIELFSFPDPPerqtrpeaAGLRHLAFTVGS 84
Cdd:cd08343     2 HVVLCSPDVEASRDFYTDVLGFRVSDRIVDPgvDGGAF---LHCDrGTDHHTVALAGGPH--------PGLHHVAFEVHD 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2473401057  85 LD---KAVQELHEKG--IETEPIRtDPLTGKRFTFFFDPD 119
Cdd:cd08343    71 LDdvgRGHDRLREKGykIEWGPGR-HGLGSQVFDYWFDPS 109
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 6-127 1.68e-07

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


Pssm-ID: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 46.56  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   6 IHHIAIICSDYEKSKAFYVHKLGFQViqETYREERGSYKLDlslNGSYVIELFSFPDPPERQTRPEAAGLRHLAFTVGSL 85
Cdd:cd07264     1 IAYIVLYVDDFAASLRFYRDVLGLPP--RFLHEEGEYAEFD---TGETKLALFSRKEMARSGGPDRRGSAFELGFEVDDV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2473401057  86 DKAVQELHEKGIE--TEPIRTDPltGKRFTFFFDPDQLPLELYE 127
Cdd:cd07264    76 EATVEELVERGAEfvREPANKPW--GQTVAYVRDPDGNLIEICE 117
VOC_BsYqjT cd07242
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; The vicinal ...
 6-125 3.29e-07

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: 45.94  E-value: 3.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   6 IHHIAIICSDYEKSKAFYVhKLGFQVIQETYREERG-SYKLDlslNGSYVI--ELFSFPDPPERQTRPeaaGLRHLAFTV 82
Cdd:cd07242     2 VSHVELAVSDLHRSFKWFE-WILGLGWKEYDTWSFGpSWKLS---GGSLLVvqQTDEFATPEFDRARV---GLNHLAFHA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2473401057  83 GS---LDKAVQELHEKGIETEPIRTDPLTGKRF---TFFFDPDQLPLEL 125
Cdd:cd07242    75 ESreaVDELTEKLAKIGGVRTYGDRHPFAGGPPhyaAFCEDPDGIKLEL 123
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 8-126 4.44e-06

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: 42.55  E-value: 4.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   8 HIAIICSDYEKSKAFYVHKLGFQVIQETYREERGSYKLDLSLNGSYVIELFSFPDPPERQtrpeaagLRHLAFTVGS--L 85
Cdd:cd08345     1 HITLIVRDLEKSTAFLQDIFGAREVYSSGDKTFSLSKEKFFLLGGLWIALMEGESLQERS-------YTHIAFQIQSedF 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2473401057  86 DKAVQELHEKGIETEPIRTDPLTGKRFTFFFDPDQLPLELY 126
Cdd:cd08345    74 DRYAERLGALGVEMRPPRPRVEGEGRSIYFYDPDNHLFELH 114
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 3-125 6.70e-05

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: 39.54  E-value: 6.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   3 LKSIHHIAIICSDYEKSKAFYVHKLGFQVIQEtyrEERGSYkldLSLNGS--YVIELfsfpdppeRQTrpEAAGLRHLAF 80
Cdd:cd08362     1 VTHLRYVALGVPDLAAEREFYTEVWGLEEVAE---DDDVVY---LRAEGSehHVLRL--------RQS--DENRLDLIAF 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2473401057  81 TVGS---LDKAVQELHEKG--IETEPIRTD-PLTGKRFTfFFDPDQLPLEL 125
Cdd:cd08362    65 AAATradVDALAARLAAAGvrILSEPGPLDdPGGGYGFR-FFDPDGRTIEV 114
MRD cd07235
Mitomycin C resistance protein (MRD); Mitomycin C (MC) is a naturally occurring antibiotic, ...
 9-119 1.49e-04

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: 38.63  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   9 IAIICSDYEKSKAFYvHKLGFQVIQETYREERGSYKLD----LSLNGSYVIELFSfpdpPERQtRPEAAGLRHLAF---T 81
Cdd:cd07235     4 IAIVVEDMAKSLEFY-RKLGFEVPEEADSAPHTEAALPggirLALDTEETIRSYD----PGWQ-APTGGGRFAIAFlcpT 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2473401057  82 VGSLDKAVQELHEKGIETEPIRTDPLTGKRFTFFFDPD 119
Cdd:cd07235    78 PAEVDAKYAELTGAGYEGHLKPWNAPWGQRYAIVKDPD 115
VOC_like cd08357
uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and ...
 7-124 2.41e-04

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


Pssm-ID: 319945 [Multi-domain]  Cd Length: 124  Bit Score: 38.13  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   7 HHIAIICSDYEKSKAFYVHKLGFqviqetyREERGSYK-LDLSLNGSYVIELFSfPDPPERQTRPEAAG---LRH--LAF 80
Cdd:cd08357     1 FHLAIPVRDLEAARDFYGDVLGC-------PEGRSSETwIDFNFFGHQVVAHLV-PNYASTSTNAVDGHsvpVPHfgLAL 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2473401057  81 TVGSLDKAVQELHEKGIE--TEP-IRTDPLTGKRFTFFF-DPDQLPLE 124
Cdd:cd08357    73 TVDDFDALAERLKAAGVKfyIEPyVRFEGEPGEQWTMFLlDPSGNALE 120
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 8-126 3.50e-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: 37.30  E-value: 3.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   8 HIAIICSDYEKSKAFYVHKLGfqvIQETYREERGSY-KLDLSLNGSYVIelfsfpdpperqTRPEAAGLRHLAFTVGS-- 84
Cdd:cd16360     1 YAELGVPDLEKALEFYTDVLG---LQVAKRDGNSVYlRGYEDEHHSLVL------------YEAPEAGLKHFAFEVASee 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2473401057  85 -LDKAVQELHEKGIETEpIRTDPLT--GKRFTFFFDPDQLPLELY 126
Cdd:cd16360    66 dLERAAASLTALGCDVT-WGPDGEVpgGGKGFRFQDPSGHLLELF 109
BphC2-C3-RGP6_C_like cd08348
The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus ...
 5-125 5.10e-04

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


Pssm-ID: 319936  Cd Length: 137  Bit Score: 37.50  E-value: 5.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   5 SIHHIAIICSD--YEKSKAFYVHKLGfqvIQETYREERGSYkldLSLNGS-YVIELFSFPD---PPERqtRPEAAGLRHL 78
Cdd:cd08348     1 KLAHFVLRTNPekFEAMVQWYLDILG---ARIVARNAKGCF---LSFDEEhHRIAIFGAPGgaqPPDK--RPTRVGLAHI 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2473401057  79 AFTVGSLDKAVQ---ELHEKGIE-TEPIRTDPLTGkrfTFFFDPDQLPLEL 125
Cdd:cd08348    73 AFTYASLDDLARnyaQLKERGIKpVWPVNHGVTTS---IYYRDPDGNMLEM 120
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 4-126 5.51e-04

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


Pssm-ID: 319918  Cd Length: 124  Bit Score: 37.29  E-value: 5.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   4 KSIHHIAIICSDYEKSKAFYVHKLGFQVIqetyreERGSYKLDLSLNGSYV-IELFSFPDPPERQtrPEAAGLRHLAF-- 80
Cdd:cd07255     1 TRIGRVTLKVADLERQSAFYQNVIGLSVL------KQNASRAYLGVDGKQVlLVLEAIPDAVLAP--RSTTGLYHFAIll 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2473401057  81 -TVGSLDKAVQELHEKGIETEPirTDPLTGKRFtFFFDPDQLPLELY 126
Cdd:cd07255    73 pDRKALGRALAHLAEHGPLIGA--ADHGVSEAI-YLSDPEGNGIEIY 116
PcpA_N_like cd08346
N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 5-125 6.08e-04

N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins; The N-terminal domain of Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) 2,6-dichloro-p-hydroquinone1,2-dioxygenase (PcpA), and similar proteins. PcpA is a key enzyme in the pentachlorophenol (PCP) degradation pathway, catalyzing the conversion of 2,6-dichloro-p-hydroquinone to 2-chloromaleylacetate. This domain 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: 319934  Cd Length: 124  Bit Score: 36.88  E-value: 6.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   5 SIHHIAIICSDYEKSKAFYVHKLGFQVIQET-YREERGSYKLDLS-LNGSYVIELFSFPDPPERQTRPEAAGLRHLAFTV 82
Cdd:cd08346     1 GIHHITAITGDAQENVDFYVKVLGLRLVKKTvNQDDPPMYHLYYGdELGSPGTLLTFFPWPLGGPGRRGTGQISRIGLRV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2473401057  83 --GSLDKAVQELHEKGIETEPIRTDplTGKRFTFFFDPDQLPLEL 125
Cdd:cd08346    81 pkGSLSFWAERLEKFGVPHSEVVTR--FGEKYLRFEDPDGTRLFL 123
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
11-119 7.20e-04

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 36.76  E-value: 7.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057  11 IICSDYEKSKAFYVHKLGFQVIQEtYREERGsyKLD---LSLNGSYVieLFSfpDPPERQTRPEAAGLrHLAFTVGSLDK 87
Cdd:COG2764     6 LVVDDAEEALEFYEDVFGFEVVFR-MTDPDG--KIMhaeLRIGGSVL--MLS--DAPPDSPAAEGNGV-SLSLYVDDVDA 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2473401057  88 AVQELHEKG--IETEPIRTDplTGKRFTFFFDPD 119
Cdd:COG2764    78 LFARLVAAGatVVMPLQDTF--WGDRFGMVRDPF 109
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 6-126 7.95e-04

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: 36.95  E-value: 7.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   6 IHHIAIICSDYEKSKAFYVHKLGFQVIQETyreERGSYkldLSLNGSYvIELFSFPDPPERQTRPEAAglrHLAFTVG-- 83
Cdd:cd08363     1 INHITFSVSNLNKSIAFYKDVLDAKLLVLG---EKTAY---FDLNGLW-LALNVQEDIPRNEISHSYT---HIAFSIDee 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2473401057  84 SLDKAVQELHEKGIETEPIRTDPLTGKRFTFFFDPDQLPLELY 126
Cdd:cd08363    71 DLDAFKERLKDNGVNILEGRKRDILEGQSIYFTDPDGHLFELH 113
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 3-100 1.03e-03

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: 36.44  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   3 LKSIHHIAIICSDYEKSKAFYVHKLGFQVIqeTYREERgsYKLDLslnGSYVIELFSFPDPPERQTRPEAAGLRHLAFTV 82
Cdd:cd07253     1 IKRLDHLVLTVKDIERTIDFYTKVLGMTVV--TFKEGR--KALRF---GNQKINLHQKGKEFEPKASAPTPGSADLCFIT 73

                          90
                  ....*....|....*....
gi 2473401057  83 G-SLDKAVQELHEKGIETE 100
Cdd:cd07253    74 EtPIDEVLEHLEACGVTIE 92
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 6-98 3.44e-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: 319923 [Multi-domain]  Cd Length: 121  Bit Score: 34.90  E-value: 3.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   6 IHHIAIICSDYEKSKAFY---VHKLGFQVIQETyrEERGSYkldlslnGSYVIELFSFPDPPERQTRPEAAGLrHLAFTV 82
Cdd:cd07262     1 ISHVTIGVNDLERSRAFYdaaLAPLGYKRGFED--GGRVGY-------GLEGGPDFWVTEPFDGEPATAGNGT-HVAFAA 70

                          90
                  ....*....|....*.
gi 2473401057  83 GSLDkAVQELHEKGIE 98
Cdd:cd07262    71 PSRA-AVDAFHAAALA 85
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 6-125 5.29e-03

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: 34.57  E-value: 5.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   6 IHHIAIICSDYEKSKAFYVHKLGFQVIQetyREERGSYkldLSLNGSYV-IELfsfpDPPERQTRPeaagLRHLAFTV-- 82
Cdd:cd07244     2 INHITLAVSDLERSLAFYVDLLGFKPHV---RWDKGAY---LTAGDLWLcLSL----DPAAEPSPD----YTHIAFTVse 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2473401057  83 GSLDKAVQELHEKGIETEPIRTDPltGKRFtFFFDPDQLPLEL 125
Cdd:cd07244    68 EDFEELSERLRAAGVKIWQENSSE--GDSL-YFLDPDGHKLEL 107
PRK04101 PRK04101
metallothiol transferase FosB;
3-126 6.15e-03

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 34.54  E-value: 6.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057   3 LKSIHHIAIICSDYEKSKAFYVHKLGFQVIqetYREERGSYkldLSLNGsYVIELFSFPDPPERQTRpeaAGLRHLAFTV 82
Cdd:PRK04101    2 LKGINHICFSVSNLEKSIEFYEKVLGAKLL---VKGRKTAY---FDLNG-LWIALNEEKDIPRNEIH---QSYTHIAFSI 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2473401057  83 G--SLDKAVQELHEKGIETEPIRTDPLTGKRFTFFFDPDQLPLELY 126
Cdd:PRK04101   72 EeeDFDHWYQRLKENDVNILPGRERDERDKKSIYFTDPDGHKFEFH 117
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 13-106 6.68e-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: 6.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473401057  13 CSDYEKSKAFYVHKLGFQViqeTYREERGSYkLDLSLNGsyvIELFSFPDPPERQTRPEAAglrhLAFTVGSLDKAVQEL 92
Cdd:cd08349     6 VRDIDKTLAFYVDVLGFEV---DYERPPPGY-AILSRGG---VELHLFEHPGLDPAGSGVA----AYIRVEDIDALHAEL 74

                          90
                  ....*....|....*.
gi 2473401057  93 HEKGI--ETEPIRTDP 106
Cdd:cd08349    75 KAAGLplFGIPRITPI 90
 
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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