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Conserved domains on  [gi|636259617|gb|KDK37588|]
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hypothetical protein AF15_00202 [Klebsiella pneumoniae CHS 59]

Protein Classification

VOC family protein( domain architecture ID 10793579)

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
PRK11478 PRK11478
VOC family protein;
1-129 8.48e-99

VOC family protein;


:

Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 278.70  E-value: 8.48e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   1 MLGLKRVHHIAIIATDYARSKAFYCDILGFTLQSEFYRAERDSWKGDLALNGEYVIELFSFPFPPARPSRPEACGLRHLA 80
Cdd:PRK11478   1 MLGLKQVHHIAIIATDYAVSKAFYCDILGFTLQSEVYREARDSWKGDLALNGQYVIELFSFPFPPERPSRPEACGLRHLA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 636259617  81 FSVDDIDAAVAHLTAHGVECEAIRVDPFTGKRFTFFSDPDDLPLEIYQQ 129
Cdd:PRK11478  81 FSVDDIDAAVAHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLELYEQ 129
 
Name Accession Description Interval E-value
PRK11478 PRK11478
VOC family protein;
1-129 8.48e-99

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 278.70  E-value: 8.48e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   1 MLGLKRVHHIAIIATDYARSKAFYCDILGFTLQSEFYRAERDSWKGDLALNGEYVIELFSFPFPPARPSRPEACGLRHLA 80
Cdd:PRK11478   1 MLGLKQVHHIAIIATDYAVSKAFYCDILGFTLQSEVYREARDSWKGDLALNGQYVIELFSFPFPPERPSRPEACGLRHLA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 636259617  81 FSVDDIDAAVAHLTAHGVECEAIRVDPFTGKRFTFFSDPDDLPLEIYQQ 129
Cdd:PRK11478  81 FSVDDIDAAVAHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLELYEQ 129
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 5-128 1.05e-76

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: 222.80  E-value: 1.05e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   5 KRVHHIAIIATDYARSKAFYCDILGFTLQSEFYRAERDSWKGDLALnGEYVIELFSFPFPPARPSRPEACGLRHLAFSVD 84
Cdd:cd08352    1 KKIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDIKLDLAL-GGYQLELFIKPDAPARPSYPEALGLRHLAFKVE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 636259617  85 DIDAAVAHLTAHGVECEAIRVDPFTGKRFTFFSDPDDLPLEIYQ 128
Cdd:cd08352   80 DVEATVAELKSLGIETEPIRVDDFTGKKFTFFFDPDGLPLELYE 123
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 5-128 2.72e-36

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: 120.48  E-value: 2.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   5 KRVHHIAIIATDYARSKAFYCDILGFTLQSEFYRAERDSWKGDLALNGEYVIELFSFPfppARPSRPEACGLRHLAFSVD 84
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTELELFEAP---GAAPAPGGGGLHHLAFRVD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 636259617  85 DIDAAVAHLTAHGVECEAIRVDPFTGKRFTFFSDPDDLPLEIYQ 128
Cdd:COG0346   78 DLDAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVE 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
6-126 4.31e-32

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 109.84  E-value: 4.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617    6 RVHHIAIIATDYARSKAFYCDILGFTLQSEFYRAERDSWKGDLALNGEYVIELFSFPFPPARPSRPEACGLRHLAFSVDD 85
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 636259617   86 IDAAVAHLTAHGVECEAIRVDPFTGKRFTFFSDPDDLPLEI 126
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
 6-100 1.02e-06

methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA epimerase (EC 5.1.99.1), also called methylmalonyl-CoA racemase. This enzyme converts (2R)-methylmalonyl-CoA to (2S)-methylmalonyl-CoA, which is then a substrate for methylmalonyl-CoA mutase (TIGR00642). It is known in bacteria, archaea, and as a mitochondrial protein in animals. It is closely related to lactoylglutathione lyase (TIGR00068), which is also called glyoxylase I, and is also a homodimer.


Pssm-ID: 213772 [Multi-domain]  Cd Length: 128  Bit Score: 44.62  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617    6 RVHHIAIIATDYARSKAFYCDILGFTLQSEFYRAERDSWKGDLALnGEYVIELFSfPF----PPARPSRPEACGLRHLAF 81
Cdd:TIGR03081   1 RIDHVGIAVPDLEEAAKFYEDVLGAQVSEIEELPEQGVKVVFIAL-GNTKVELLE-PLgedsPIAKFLEKNGGGIHHIAI 78

                          90
                  ....*....|....*....
gi 636259617   82 SVDDIDAAVAHLTAHGVEC 100
Cdd:TIGR03081  79 EVDDIEAALETLKEKGVRL 97
 
Name Accession Description Interval E-value
PRK11478 PRK11478
VOC family protein;
1-129 8.48e-99

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 278.70  E-value: 8.48e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   1 MLGLKRVHHIAIIATDYARSKAFYCDILGFTLQSEFYRAERDSWKGDLALNGEYVIELFSFPFPPARPSRPEACGLRHLA 80
Cdd:PRK11478   1 MLGLKQVHHIAIIATDYAVSKAFYCDILGFTLQSEVYREARDSWKGDLALNGQYVIELFSFPFPPERPSRPEACGLRHLA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 636259617  81 FSVDDIDAAVAHLTAHGVECEAIRVDPFTGKRFTFFSDPDDLPLEIYQQ 129
Cdd:PRK11478  81 FSVDDIDAAVAHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLELYEQ 129
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 5-128 1.05e-76

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: 222.80  E-value: 1.05e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   5 KRVHHIAIIATDYARSKAFYCDILGFTLQSEFYRAERDSWKGDLALnGEYVIELFSFPFPPARPSRPEACGLRHLAFSVD 84
Cdd:cd08352    1 KKIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDIKLDLAL-GGYQLELFIKPDAPARPSYPEALGLRHLAFKVE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 636259617  85 DIDAAVAHLTAHGVECEAIRVDPFTGKRFTFFSDPDDLPLEIYQ 128
Cdd:cd08352   80 DVEATVAELKSLGIETEPIRVDDFTGKKFTFFFDPDGLPLELYE 123
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 5-128 2.72e-36

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: 120.48  E-value: 2.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   5 KRVHHIAIIATDYARSKAFYCDILGFTLQSEFYRAERDSWKGDLALNGEYVIELFSFPfppARPSRPEACGLRHLAFSVD 84
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTELELFEAP---GAAPAPGGGGLHHLAFRVD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 636259617  85 DIDAAVAHLTAHGVECEAIRVDPFTGKRFTFFSDPDDLPLEIYQ 128
Cdd:COG0346   78 DLDAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVE 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
6-126 4.31e-32

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 109.84  E-value: 4.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617    6 RVHHIAIIATDYARSKAFYCDILGFTLQSEFYRAERDSWKGDLALNGEYVIELFSFPFPPARPSRPEACGLRHLAFSVDD 85
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 636259617   86 IDAAVAHLTAHGVECEAIRVDPFTGKRFTFFSDPDDLPLEI 126
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
4-127 2.43e-20

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 80.39  E-value: 2.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   4 LKRVHHIAIIATDYARSKAFYCDILGFTLQSE-----FYRAErdswkgdlalNGEYVIELFSFPFPPARPSRPeacGLRH 78
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEReggrvYLRAD----------GGEHLLVLEEAPGAPPRPGAA---GLDH 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 636259617  79 LAFSVD---DIDAAVAHLTAHGVECEAIrVDPFTGKRFtFFSDPDDLPLEIY 127
Cdd:COG2514   68 VAFRVPsraDLDAALARLAAAGVPVEGA-VDHGVGESL-YFRDPDGNLIELY 117
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 9-126 1.01e-16

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: 70.25  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   9 HIAIIATDYARSKAFYCDILGFTLqseFYRAERDSWKGdLALNGEYVIELFSFPFPPARPSRpeacGLRHLAFSVDDIDA 88
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEV---VSRNEGGGFAF-LRLGPGLRLALLEGPEPERPGGG----GLFHLAFEVDDVDE 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 636259617  89 AVAHLTAHGVECEAI--RVDPFTGKRFTFFSDPDDLPLEI 126
Cdd:cd06587   73 VDERLREAGAEGELVapPVDDPWGGRSFYFRDPDGNLIEF 112
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-126 1.11e-16

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


Pssm-ID: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 70.42  E-value: 1.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   7 VHHIAIIATDYARSKAFYCDILGFTlqsEFYRAERDSWKGD-LALNGEYVIELfSFPFPPARPSRPEACG-LRHLAFSVD 84
Cdd:cd07245    1 LDHVALACPDLERARRFYTDVLGLE---EVPRPPFLKFGGAwLYLGGGQQIHL-VVEQNPSELPRPEHPGrDRHPSFSVP 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 636259617  85 DIDAAVAHLTAHGVECEAiRVDPFTGKRFTFFSDPDDLPLEI 126
Cdd:cd07245   77 DLDALKQRLKEAGIPYTE-STSPGGGVTQLFFRDPDGNRLEF 117
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 6-128 1.42e-16

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: 70.82  E-value: 1.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   6 RVHHIAIIATDYARSKAFYCDILGFTL--QSeFYRAERDSWKGDLALNGEYV-----------------IELFSFPFPPA 66
Cdd:cd16361    1 GVNHVGITVPDLDAAVEFYTDVLGAEVvyRS-TPLAEGDRGGGEMRAAGFVPgfarariamlrlgpgpgIELFEYKGPEQ 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 636259617  67 RPSRPEAC--GLRHLAFSVDDIDAAVAHLTAHGVEC-----EAIRVDPFTGKRFTFFSDPDDLPLEIYQ 128
Cdd:cd16361   80 RAPVPRNSdvGIFHFALQVDDVEAAAERLAAAGGKVlmgprEIPDGGPGKGNRMVYLRDPWGTLIELVS 148
VOC_like cd08353
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 4-99 5.95e-16

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


Pssm-ID: 319941  Cd Length: 142  Bit Score: 69.14  E-value: 5.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   4 LKRVHHIAIIATDYARSKAFYCDiLGFTLQ------SEFyrAER----DSWKGDLAL----NGEYVIELFSFPFPPA--- 66
Cdd:cd08353    1 IKRMDHVGIVVEDLDAAIAFFTE-LGLELEgrmtveGEW--ADRvvglDGVRVEIAMlrtpDGHGRLELSKFLTPAAipg 77

                         90       100       110
                 ....*....|....*....|....*....|....
gi 636259617  67 -RPSRPEACGLRHLAFSVDDIDAAVAHLTAHGVE 99
Cdd:cd08353   78 hRPAPANALGLRHVAFAVDDIDAVVARLRKHGAE 111
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 6-128 6.63e-16

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 68.12  E-value: 6.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   6 RVHHIAIIATDYARSKAFYCDILGFTLQSEFyraerdSWKGD---LALNGEYVIELFSFPFPPARPSRpeacglrHLAFS 82
Cdd:COG3324    4 TIVWVELPVDDLERAKAFYEEVFGWTFEDDA------GPGGDyaeFDTDGGQVGGLMPGAEEPGGPGW-------LLYFA 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 636259617  83 VDDIDAAVAHLTAHGVECEAIRVDPFTGKRFTFFSDPDDLPLEIYQ 128
Cdd:COG3324   71 VDDLDAAVARVEAAGGTVLRPPTDIPPWGRFAVFRDPEGNRFGLWQ 116
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
8-115 1.62e-14

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 64.61  E-value: 1.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617    8 HHIAIIATDYARSKAFYCDILGFTlQSEFYRAERDSWKGDLAL--NGEYVIELFSfPFPPARPSRPEACGLRHLAFSVDD 85
Cdd:pfam13669   1 HHVGIAVPDLDRALALWGALLGLG-PEGDYRSEPQNVDLAFALlgDGPVEVELIQ-PLDGDSPLARHGPGLHHLAYWVDD 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 636259617   86 IDAAVAHLTAHGVEC--EAIRvDPFTGKRFTF 115
Cdd:pfam13669  79 LDAAVARLLDQGYRVapKGPR-AGAAGRRVAF 109
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 7-121 3.23e-11

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: 56.43  E-value: 3.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   7 VHHIAIIATDYARSKAFYCDILGFTLQSEFYRAERDSWKgDLALNGEYVIEL---FSFPFPPARPSRPEACGLRHLAFSV 83
Cdd:cd07249    1 LDHIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQGVRV-AFLELGNTQIELlepLGEDSPIAKFLDKKGGGLHHIAFEV 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 636259617  84 DDIDAAVAHLTAHGVEC-EAIRVDPFTGKRFTFFsDPDD 121
Cdd:cd07249   80 DDIDAAVEELKAQGVRLlSEGPRIGAHGKRVAFL-HPKD 117
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 9-128 8.21e-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: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 52.33  E-value: 8.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   9 HIAIIATDYARSKAFYCDILGFTLqsefyRAERDSWKGDLALNGEYVIELFSFPfPPARPSRPEACG-LRHLAFSVDDID 87
Cdd:cd07264    3 YIVLYVDDFAASLRFYRDVLGLPP-----RFLHEEGEYAEFDTGETKLALFSRK-EMARSGGPDRRGsAFELGFEVDDVE 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 636259617  88 AAVAHLTAHGVE-CEAIRVDPFtGKRFTFFSDPDDLPLEIYQ 128
Cdd:cd07264   77 ATVEELVERGAEfVREPANKPW-GQTVAYVRDPDGNLIEICE 117
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 9-121 2.90e-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: 51.14  E-value: 2.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   9 HIAIIATDYARSKAFYCDILGFTLQSEFYrAERDSW-----KGDlalnGEYVIELFSFPFPPARPSRPEACG-LRHLAFS 82
Cdd:cd07263    1 QVMLYVDDQDKALDFYVEKLGFEVVEDVP-MGGMRWvtvapPGS----PGTSLLLEPKAHPAQMPQSPEAAGgTPGILLA 75

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 636259617  83 VDDIDAAVAHLTAHGVECEAIRVDPFTGkRFTFFSDPDD 121
Cdd:cd07263   76 TDDIDATYERLTAAGVTFVQEPTQMGGG-RVANFRDPDG 113
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 5-127 4.29e-08

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: 48.08  E-value: 4.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   5 KRVHHIAIIATDYARSKAFYCDILGFTLqsefyrAERDSWKGDLALNGEYV-IELFSFPFPPARPsrPEACGLRHLAFSV 83
Cdd:cd07255    1 TRIGRVTLKVADLERQSAFYQNVIGLSV------LKQNASRAYLGVDGKQVlLVLEAIPDAVLAP--RSTTGLYHFAILL 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 636259617  84 DD---IDAAVAHLTA---------HGVEcEAIrvdpftgkrftFFSDPDDLPLEIY 127
Cdd:cd07255   73 PDrkaLGRALAHLAEhgpligaadHGVS-EAI-----------YLSDPEGNGIEIY 116
Glyoxalase_3 pfam13468
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 7-123 5.03e-08

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


Pssm-ID: 433233  Cd Length: 175  Bit Score: 48.87  E-value: 5.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617    7 VHHIAIIATDYARSKAFYCDILGFTLQSEFYRAERDSWKGDLALNGEYvIELFS---------FPFPPARPSRPEACGLR 77
Cdd:pfam13468   1 LDHVVLAVPDLDEAAARFARALGFTVTPGGRHPGMGTANALIMFGDGY-LELLAvdpeapappRGRWFGLDRLADGEGLL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 636259617   78 HLAFSVDDIDAAVAHLTAHGVEcEAIRVDPfTGKRFTF---FSDPDDLP 123
Cdd:pfam13468  80 GWALRTDDIDAVAARLRAAGVE-PGRRVRP-DGGDLRWrllFLADGALP 126
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 12-120 1.60e-07

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: 46.49  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617  12 IIATDYARSKAFYCDILGFTLQSEFyraerdswkgdlALNGEYVieLFSFPFPP----ARPSRPEACGLRHLA--FSVDD 85
Cdd:cd07247    6 LPTTDLERAKAFYGAVFGWTFEDEG------------DGGGDYA--LFTAGGGAvgglMRAPEEVAGAPPGWLiyFAVDD 71

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 636259617  86 IDAAVAHLTAHGVECEAIRVDPFTGKRFTFFSDPD 120
Cdd:cd07247   72 LDAALARVEAAGGKVVVPPTDIPGGGRFAVFADPE 106
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 3-99 6.13e-07

4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and metabolism, General function prediction only];


Pssm-ID: 442418 [Multi-domain]  Cd Length: 333  Bit Score: 46.81  E-value: 6.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   3 GLKRVHHIAII--ATDYARSKAFYCDILGFTLQSEF-----YRAER----DSWKGD--LALNGeyvielfsfpfpPARPS 69
Cdd:COG3185  143 GLTRIDHIGIAvpRGDLDEWVLFYEDVLGFEEIREEdiedpYQGVRsavlQSPDGKvrIPLNE------------PTSPD 210

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 636259617  70 RPEA--------CGLRHLAFSVDDIDAAVAHLTAHGVE 99
Cdd:COG3185  211 SQIAeflekyrgEGIQHIAFATDDIEATVAALRARGVR 248
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
 6-100 1.02e-06

methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA epimerase (EC 5.1.99.1), also called methylmalonyl-CoA racemase. This enzyme converts (2R)-methylmalonyl-CoA to (2S)-methylmalonyl-CoA, which is then a substrate for methylmalonyl-CoA mutase (TIGR00642). It is known in bacteria, archaea, and as a mitochondrial protein in animals. It is closely related to lactoylglutathione lyase (TIGR00068), which is also called glyoxylase I, and is also a homodimer.


Pssm-ID: 213772 [Multi-domain]  Cd Length: 128  Bit Score: 44.62  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617    6 RVHHIAIIATDYARSKAFYCDILGFTLQSEFYRAERDSWKGDLALnGEYVIELFSfPF----PPARPSRPEACGLRHLAF 81
Cdd:TIGR03081   1 RIDHVGIAVPDLEEAAKFYEDVLGAQVSEIEELPEQGVKVVFIAL-GNTKVELLE-PLgedsPIAKFLEKNGGGIHHIAI 78

                          90
                  ....*....|....*....
gi 636259617   82 SVDDIDAAVAHLTAHGVEC 100
Cdd:TIGR03081  79 EVDDIEAALETLKEKGVRL 97
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
12-128 1.29e-06

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 44.08  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617  12 IIATDYARSKAFYCDILGFTLQSEFYRAERDSWKGDLALnGEYVIELFSfpfppARPSRPEACGLR-HLAFSVDDIDAAV 90
Cdd:COG2764    6 LVVDDAEEALEFYEDVFGFEVVFRMTDPDGKIMHAELRI-GGSVLMLSD-----APPDSPAAEGNGvSLSLYVDDVDALF 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 636259617  91 AHLTAHGVEceaIRVDP---FTGKRFTFFSDPDDLPLEIYQ 128
Cdd:COG2764   80 ARLVAAGAT---VVMPLqdtFWGDRFGMVRDPFGVLWMINT 117
VOC_like cd08357
uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and ...
 8-126 1.43e-06

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: 44.30  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   8 HHIAIIATDYARSKAFYCDILGFTlqsEFYRAERdsWKgDLALNGEYVIELFSFPFPPA--RPSRPEACGLRH--LAFSV 83
Cdd:cd08357    1 FHLAIPVRDLEAARDFYGDVLGCP---EGRSSET--WI-DFNFFGHQVVAHLVPNYASTstNAVDGHSVPVPHfgLALTV 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 636259617  84 DDIDAAVAHLTAHGVECE---AIRVDPFTGKRFT-FFSDPDDLPLEI 126
Cdd:cd08357   75 DDFDALAERLKAAGVKFYiepYVRFEGEPGEQWTmFLLDPSGNALEF 121
HPCD_N_class_II cd07266
N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 6-127 1.52e-06

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: 43.94  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   6 RVHHIAIIATDYARSKAFYCDILGFTLQSE-----FYRAERDswkgdlalNGEYVIELFSFPFPparpsrpeacGLRHLA 80
Cdd:cd07266    4 RLAHAELVVTDLAASREFYVDTLGLHVTDEddnaiYLRGVEE--------FIHHTLVLRKAPEA----------AVGHLG 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 636259617  81 FSV---DDIDAAVAHLTAHGVECEaIRVDPFTGKRFTfFSDPDDLPLEIY 127
Cdd:cd07266   66 FRVrdeADLDKAAAFYKELGLPTE-WREEPGQGRTLR-VEDPFGFPIEFY 113
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 9-127 4.14e-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: 42.93  E-value: 4.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   9 HIAIIATDYARSKAFYCDILGFtlqsefyRAERDSWKGDLALNGEYVIELFSFPFPPARPSRPEACGLRHLAFSVDDIDA 88
Cdd:cd08345    1 HITLIVRDLEKSTAFLQDIFGA-------REVYSSGDKTFSLSKEKFFLLGGLWIALMEGESLQERSYTHIAFQIQSEDF 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 636259617  89 AV--AHLTAHGVECEAIRVDPFTGKRFTFFSDPDDLPLEIY 127
Cdd:cd08345   74 DRyaERLGALGVEMRPPRPRVEGEGRSIYFYDPDNHLFELH 114
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 16-98 5.34e-06

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: 42.21  E-value: 5.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617  16 DYARSKAFYCDILGFTLQsefYRAERDSWkGDLALNGeyvIELFSFPFPPARPSRPE-ACGLRhlafsVDDIDAAVAHLT 94
Cdd:cd08349    8 DIDKTLAFYVDVLGFEVD---YERPPPGY-AILSRGG---VELHLFEHPGLDPAGSGvAAYIR-----VEDIDALHAELK 75


                 ....
gi 636259617  95 AHGV 98
Cdd:cd08349   76 AAGL 79
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 4-126 5.64e-06

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: 42.24  E-value: 5.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   4 LKRVHHIAIIATDYARSKAFYCDILGFTLQSE-----FYRAERDSwkgdlalngEYVIELfsfpfppaRPSrpEACGLRH 78
Cdd:cd08362    1 VTHLRYVALGVPDLAAEREFYTEVWGLEEVAEdddvvYLRAEGSE---------HHVLRL--------RQS--DENRLDL 61

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 636259617  79 LAFSVD---DIDAAVAHLTAHGVECE---AIRVDPFTGKRFTFFsDPDDLPLEI 126
Cdd:cd08362   62 IAFAAAtraDVDALAARLAAAGVRILsepGPLDDPGGGYGFRFF-DPDGRTIEV 114
BphC-JF8_N_like cd09013
N-terminal, non-catalytic, domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 4-127 6.10e-05

N-terminal, non-catalytic, domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase) from Bacillus sp. JF8, and similar proteins; 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, a key step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). BphC belongs to the type I extradiol dioxygenase family, which requires a metal ion in the active site in its catalytic mechanism. Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. This subfamily of BphC is represented by the enzyme purified from the thermophilic biphenyl and naphthalene degrader, Bacillus sp. JF8. The members in this family of BphC enzymes may use either Mn(II) or Fe(II) as cofactors. The enzyme purified from Bacillus sp. JF8 is Mn(II)-dependent, however, the enzyme from Rhodococcus jostii RHAI has Fe(II) bound to it. BphC_JF8 is thermostable and its optimum activity is at 85 degrees C. The enzymes in this family have an internal duplication. This family represents the N-terminal repeat.


Pssm-ID: 319955  Cd Length: 121  Bit Score: 39.64  E-value: 6.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   4 LKRVHHIAIIATDYARSKAFYCDILGFTL-----QSEFYRAERDSWKGDLALNgeyvielfsfpfpparpSRPEAcGLRH 78
Cdd:cd09013    4 LAQLAHVELLTPKPEESLWFFTDVLGLEEthregQSVYLRAWGDWEHHTLKLT-----------------ESPEA-GLGH 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 636259617  79 LAFSVD---DIDAAVAHLTAHGVECEAIRVDPFTGKRFTfFSDPDDLPLEIY 127
Cdd:cd09013   66 IAWRASspeALERRVAALEASGVGIGWIDGDLGQGPAYR-FQSPDGHPMEIY 116
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 16-126 1.08e-04

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


Pssm-ID: 319900 [Multi-domain]  Cd Length: 142  Bit Score: 39.23  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617  16 DYARSKAFYCDILGFTL--QSEF----------------------YRAERDSWKGDLALNGEYVIElfSFPFPPARPSRP 71
Cdd:cd07233   10 DPKKSLKFYTEVLGMKLlrKKDFpemkfslyflgyedpkdipkdpRTAWVFSREGTLELTHNWGTE--NDEDPVYHNGNS 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 636259617  72 EACGLRHLAFSVDDIDAAVAHLTAHGVECeAIRVDPFTGKRFTFFSDPDDLPLEI 126
Cdd:cd07233   88 DPRGFGHIGIAVDDVYAACERFEELGVKF-KKKPDDGKMKGIAFIKDPDGYWIEI 141
Glyoxalase_6 pfam18029
Glyoxalase-like domain; This entry comprises a diverse set of domains related to the ...
 9-120 1.12e-04

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


Pssm-ID: 436220  Cd Length: 110  Bit Score: 38.90  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617    9 HIAIIATDYARSKAFYCDILGFTLQSEFYRAERDSWKGDLALNGEYVieLFsfpfppARPSRPEACGLR-HLAFSVDDID 87
Cdd:pfam18029   1 AVVLDCADPAALAAFWSAALGWEVVPDDTALPDPDGGGPIGGGGPRL--LF------QRVPEPKPGKNRvHLDLAVDDLE 72

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 636259617   88 AAVAHLTAHGveceAIRVDPFTGKRFTF--FSDPD 120
Cdd:pfam18029  73 AAVARLVALG----ATVLDDGDDPDGGRwvLADPE 103
HPPD_C_like cd07250
C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate synthase ...
 4-100 3.16e-04

C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate synthase (HmaS); HppD and HmaS are non-heme iron-dependent dioxygenases, which modify a common substrate, 4-hydroxyphenylpyruvate (HPP), but yield different products. HPPD catalyzes the second reaction in tyrosine catabolism, the conversion of 4-hydroxyphenylpyruvate to homogentisate (2,5-dihydroxyphenylacetic acid, HG). HmaS converts HPP to 4-hydroxymandelate, a committed step in the formation of hydroxyphenylglycerine, a structural component of nonproteinogenic macrocyclic peptide antibiotics, such as vancomycin. If the emphasis is on catalytic chemistry, HPPD and HmaS are classified as members of a large family of alpha-keto acid dependent mononuclear non-heme iron oxygenases most of which require Fe(II), molecular oxygen, and an alpha-keto acid (typically alpha-ketoglutarate) to either oxygenate or oxidize a third substrate. Both enzymes are exceptions in that they require two, instead of three, substrates, do not use alpha-ketoglutarate, and incorporate both atoms of dioxygen into the aromatic product. Both HPPD and HmaS exhibit duplicate beta barrel topology in their N- and C-terminal domains which share sequence similarity, suggestive of a gene duplication. Each protein has only one catalytic site located in at the C-terminal domain. This HPPD_C_like domain represents the C-terminal domain.


Pssm-ID: 319913  Cd Length: 194  Bit Score: 38.69  E-value: 3.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   4 LKRVHHIAIIATDYARSKA--FYCDILGFTLQSEFyrAERDSWKGDLALNGEYVI---ELFSFPFP-PARPSRP------ 71
Cdd:cd07250    1 LTRIDHVVGNVPDGEMDPAveWYEKCLGFHRFWEF--DDEDIGTEYSGLRSIVLAnpnETIKLPLNePAPGKRKsqiqef 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 636259617  72 ----EACGLRHLAFSVDDIDAAVAHLTAHGVEC 100
Cdd:cd07250   79 ldyhGGAGVQHIALNTDDIFATVRALRARGVEF 111
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 9-126 3.90e-04

fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin resistant protein. FosA is a Mn(II) and K(+)-dependent glutathione transferase. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosA, catalyzes the addition of glutathione to the antibiotic fosfomycin, (1R,2S)-epoxypropylphosphonic acid, making it inactive. FosA is a Mn(II) dependent enzyme. It is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319908 [Multi-domain]  Cd Length: 121  Bit Score: 37.65  E-value: 3.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   9 HIAIIATDYARSKAFYCDILGFTLQSEFYRAER----DSWkgdLALNGEyvielfsfpfPPARPSRPeacgLRHLAFSVD 84
Cdd:cd07244    4 HITLAVSDLERSLAFYVDLLGFKPHVRWDKGAYltagDLW---LCLSLD----------PAAEPSPD----YTHIAFTVS 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 636259617  85 --DIDAAVAHLTAHGVECEAIRVDPftGKRFtFFSDPDDLPLEI 126
Cdd:cd07244   67 eeDFEELSERLRAAGVKIWQENSSE--GDSL-YFLDPDGHKLEL 107
VOC_like cd07238
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 12-119 4.06e-04

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


Pssm-ID: 319903  Cd Length: 112  Bit Score: 37.46  E-value: 4.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617  12 IIATDYARSKAFYCDILGFTLqsefyrAERDSWKGDLALNGEYVIELFSFPFPPARPSRPEacglrhLAFSVDDIDAAVA 91
Cdd:cd07238    6 IATADPERAAAFYGDHLGLPL------VMDHGWIVTFASPGNAHAQISLAREGGSGTVVPD------LSIEVDDVDAVHA 73

                         90       100
                 ....*....|....*....|....*...
gi 636259617  92 HLTAHGVECEAIRVDPFTGKRFTFFSDP 119
Cdd:cd07238   74 RVVAAGLRIEYGPTTEAWGVRRFFVRDP 101
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 9-120 6.26e-04

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


Pssm-ID: 319931  Cd Length: 132  Bit Score: 37.30  E-value: 6.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   9 HIAIIATDYARSKAFYCDILGFTLqsefyrAERDSWKGDLAL------NGEYVIELFSFPFPPArpsrpeacGLRHLAFS 82
Cdd:cd08343    2 HVVLCSPDVEASRDFYTDVLGFRV------SDRIVDPGVDGGaflhcdRGTDHHTVALAGGPHP--------GLHHVAFE 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 636259617  83 VDDIDA---AVAHLTAHGVECEA-IRVDPFTGKRFTFFSDPD 120
Cdd:cd08343   68 VHDLDDvgrGHDRLREKGYKIEWgPGRHGLGSQVFDYWFDPS 109
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 11-126 6.34e-04

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


Pssm-ID: 319942  Cd Length: 122  Bit Score: 36.96  E-value: 6.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617  11 AIIATDYARSKAFYCDILGFTL-----QSEFYRAerdswkgdlalnGEYVIELFSfPFPPARPSRPE------ACGLRHL 79
Cdd:cd08354    5 CLYADDLDAAEAFYEDVLGLKPmlrsgRHAFFRL------------GPQVLLVFD-PGATSKDVRTGevpghgASGHGHF 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 636259617  80 AFSV--DDIDAAVAHLTAHGVECEAIRVDPFTGKRFtFFSDPDDLPLEI 126
Cdd:cd08354   72 AFAVptEELAAWEARLEAKGVPIESYTQWPEGGKSL-YFRDPAGNLVEL 119
VOC_like cd09011
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 12-126 7.38e-04

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


Pssm-ID: 319953  Cd Length: 122  Bit Score: 36.68  E-value: 7.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617  12 IIATDYARSKAFYCDILGFTLQSEFyrAERDSWKGDLALNGEYVIELFSFPFPparpsRPEACGLRH--LAFSVDDIDAA 89
Cdd:cd09011    8 LVVKDIEKSKKFYEDVLGQKILLDF--GENVVFEGGFALQEKKSWLETIIISD-----LSIKQQSNNfeLYFEVDDFDAF 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 636259617  90 VAHLTAHGvecEAIRVDPFT----GKRFTFFSDPDDLPLEI 126
Cdd:cd09011   81 FEKLNPHK---DIEFIHPILehpwGQRVFRFYDPDGHIIEI 118
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 9-127 7.56e-04

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


Pssm-ID: 319967  Cd Length: 111  Bit Score: 36.53  E-value: 7.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   9 HIAIIATDYARSKAFYCDILGftlqseFYRAERDswkGDLALNGEYVIELFSFPFPPArpsrPEAcGLRHLAFSV---DD 85
Cdd:cd16360    1 YAELGVPDLEKALEFYTDVLG------LQVAKRD---GNSVYLRGYEDEHHSLVLYEA----PEA-GLKHFAFEVaseED 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 636259617  86 IDAAVAHLTAHGVECEAIR-VDPFTGKRFTFFSDPDDLPLEIY 127
Cdd:cd16360   67 LERAAASLTALGCDVTWGPdGEVPGGGKGFRFQDPSGHLLELF 109
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 4-101 9.04e-04

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: 9.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   4 LKRVHHIAIIATDYARSKAFYCDILGFTLQsEFYraerdswKGDLALN-GEYVIELFSF--PFPPaRPSRPEAcGLRHLA 80
Cdd:cd07253    1 IKRLDHLVLTVKDIERTIDFYTKVLGMTVV-TFK-------EGRKALRfGNQKINLHQKgkEFEP-KASAPTP-GSADLC 70

                         90       100
                 ....*....|....*....|..
gi 636259617  81 FSVD-DIDAAVAHLTAHGVECE 101
Cdd:cd07253   71 FITEtPIDEVLEHLEACGVTIE 92
VOC_like cd08359
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 12-128 1.51e-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: 319947 [Multi-domain]  Cd Length: 119  Bit Score: 35.84  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617  12 IIATDYARSKAFYCDILGF--TLQSEFY----RAERDSWKGDLALNGEyvielfsfPFPPArPSRPEACGLrHLAFSVDD 85
Cdd:cd08359    7 IVTEDVAATAAFYVKHFGFrvIFDSDWYvslrRAERHGFELAIMDGQH--------GAVPA-ASQTQSSGL-IINFEVDD 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 636259617  86 IDAAVAHLTAHGVE-CEAIRVDPFtGKRFTFFSDPDDLPLEIYQ 128
Cdd:cd08359   77 ADAEYERLTQAGLEfLEPPRDEPW-GQRRFIVRDPNGVLIDVIQ 119
VOC_BsYqjT cd07242
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; The vicinal ...
 7-126 1.55e-03

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: 35.93  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   7 VHHIAIIATDYARSKAFYCDILGFTLQsefyraERDSW---KGDLALNGEYVIELFSFPF--PPARPSRPeacGLRHLAF 81
Cdd:cd07242    2 VSHVELAVSDLHRSFKWFEWILGLGWK------EYDTWsfgPSWKLSGGSLLVVQQTDEFatPEFDRARV---GLNHLAF 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 636259617  82 SVD---DIDAAVAHLTAHGVECEAIRVDPFTGKRF---TFFSDPDDLPLEI 126
Cdd:cd07242   73 HAEsreAVDELTEKLAKIGGVRTYGDRHPFAGGPPhyaAFCEDPDGIKLEL 123
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-128 1.72e-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: 319917 [Multi-domain]  Cd Length: 120  Bit Score: 35.90  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   5 KRVHhIAIIATDYARSKAFYCDILGftlqsefyrAERDSWKGDLAlngEYVIELFSFPFPPARPSRPEACGLRHLAFSVD 84
Cdd:cd07254    1 KRFH-LSLNVTDLERSIRFYSDLFG---------AEPAKRKADYA---KFMLEDPPLNLALLVNDRKEPYGLNHLGIQVD 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 636259617  85 DIDAAVAH---LTAHGVEceaIRVDPFTGKRFT-----FFSDPDDLPLEIYQ 128
Cdd:cd07254   68 SKEEVAALkarAEAAGLP---VRKEPRTTCCYAvqdkfWLTDPDGNAWEFYA 116
MRD cd07235
Mitomycin C resistance protein (MRD); Mitomycin C (MC) is a naturally occurring antibiotic, ...
 10-120 3.17e-03

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: 35.17  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617  10 IAIIATDYARSKAFYcDILGFTLQSEFYRAERDSWKGD----LALNGEYVIELFsFPFPParpsRPEACGLRHLAFSVD- 84
Cdd:cd07235    4 IAIVVEDMAKSLEFY-RKLGFEVPEEADSAPHTEAALPggirLALDTEETIRSY-DPGWQ----APTGGGRFAIAFLCPt 77

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 636259617  85 --DIDAAVAHLTAHGVECEAIRVDPFTGKRFTFFSDPD 120
Cdd:cd07235   78 paEVDAKYAELTGAGYEGHLKPWNAPWGQRYAIVKDPD 115
VOC_CChe_VCA0619_like cd08356
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; uncharacterized subfamily of ...
 14-119 3.76e-03

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; uncharacterized subfamily of vicinal oxygen chelate (VOC) family contains Vibrio cholerae VCA0619 and similar proteins. The 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: 319944  Cd Length: 113  Bit Score: 34.58  E-value: 3.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617  14 ATDYARSKAFYCDiLGFTLQSEFyraerdswkGDLAL--NGEYVIELFSFPfpparpsRPEACGLRHLAFSVDDIDAAVA 91
Cdd:cd08356    9 AKDFELSKAFYQA-LGFELASEE---------GGVAYfrLGDCSFLLQDFY-------EKEHAENFMMHLLVEDVDAWHQ 71

                         90       100       110
                 ....*....|....*....|....*....|....
gi 636259617  92 HLTA------HGVECEAIRVDPFTGKRFTFFsDP 119
Cdd:cd08356   72 HVKTlglaerYGVKVTDPTDQPWGMRDFVLT-DP 104
PcpA_N_like cd08346
N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 8-126 3.86e-03

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: 34.96  E-value: 3.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   8 HHIAIIATDYARSKAFYCDILGFTL--QSEFYRAER--DSWKGDLAlnGEYVIELFSFPFPPARPSRPEACGLRHLAFSV 83
Cdd:cd08346    3 HHITAITGDAQENVDFYVKVLGLRLvkKTVNQDDPPmyHLYYGDEL--GSPGTLLTFFPWPLGGPGRRGTGQISRIGLRV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 636259617  84 --DDIDAAVAHLTAHGVeceairvdPFTGKRFTF------FSDPDDLPLEI 126
Cdd:cd08346   81 pkGSLSFWAERLEKFGV--------PHSEVVTRFgekylrFEDPDGTRLFL 123
Glyoxalase_2 pfam12681
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 10-126 4.24e-03

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


Pssm-ID: 403776  Cd Length: 118  Bit Score: 34.69  E-value: 4.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   10 IAIIATDYARSKAFYCDILGFTLQSEFyrAERDSWKGDLALNgEYVIELFSFPFPPARPSRPeacglRHLAFSVDDIDAA 89
Cdd:pfam12681   4 PLLVVKDINISRKFYEDVLDQKIKLDF--GENVSFEGGFAIQ-SDFKELIGIDLSIAEQSNN-----FELYFEVADVDAF 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 636259617   90 VAHLTAHG-VE-CEAIRVDPFtGKRFTFFSDPDDLPLEI 126
Cdd:pfam12681  76 LQKIKEIGnIEyLHELKEQPW-GQRVFRFYDPDGHIIEI 113
PsjN_like cd16356
Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme ...
 12-126 5.43e-03

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


Pssm-ID: 319963  Cd Length: 119  Bit Score: 34.32  E-value: 5.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617  12 IIATDYARSKAFYCDILGF----TLQSEFYRAERDSwKGDLALNGEYVIELFSFPFPPARPSRPEACGLRhlAFSVDDID 87
Cdd:cd16356    4 IFTADIVALSDFYSELFGLeeifEIRSPIFRGLRTG-DSCLGFNAPEAYELLGLPEFSDTPGIRILLTFD--VDDVEAVD 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 636259617  88 AAVAHLTAHGVECEAIRVDPFTGKRFTFFSDPDDLPLEI 126
Cdd:cd16356   81 RLVPRAAALGATLIKPPYDTYYGWYQAVLLDPEGNVFRI 119
THT_oxygenase_C cd07257
The C-terminal domain of 2,4,5-trihydroxytoluene (THT) oxygenase; This subfamily contains the ...
 6-97 5.92e-03

The C-terminal domain of 2,4,5-trihydroxytoluene (THT) oxygenase; This subfamily contains the C-terminal, catalytic, domain of THT oxygenase. THT oxygenase is an extradiol dioxygenase in the 2,4-dinitrotoluene (DNT) degradation pathway. It catalyzes the conversion of 2,4,5-trihydroxytoluene to an unstable ring fission product, 2,4-dihydroxy-5-methyl-6-oxo-2,4-hexadienoic acid. The native protein was determined to be a dimer by gel filtration. The enzyme belongs to the type I family of extradiol dioxygenases which contains two structurally homologous barrel-shaped domains at the N- and C-terminus of each monomer. The active-site metal is located in the C-terminal barrel. Fe(II) is required for its catalytic activity.


Pssm-ID: 319920  Cd Length: 152  Bit Score: 34.62  E-value: 5.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636259617   6 RVHHIAIIATDYARSKAFYCDILGFtLQSEFYRAERDSWKG---DLALNGEYVIE--LFSFPFPPARPSrpeacglrHLA 80
Cdd:cd07257    1 KLGHVGLEVNDFEATFDWYTKTFGL-KPSDVIYLPDGKTVGsflHLDRGSEYVDHhsFFFAQGPRPKVH--------HAA 71

                         90       100
                 ....*....|....*....|
gi 636259617  81 FSVDDIDAAVA---HLTAHG 97
Cdd:cd07257   72 FEVHDFDSQVLghdWLREKG 91
VOC_BsYyaH cd07241
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal ...
 6-83 7.97e-03

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


Pssm-ID: 319905  Cd Length: 125  Bit Score: 33.92  E-value: 7.97e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 636259617   6 RVHHIAIIATDYARSKAFYCDILGFTlQSEFYRAERDSWKGD-LALNGEYVIELFSFPFPPARPSRPEACGLRHLAFSV 83
Cdd:cd07241    1 KIEHVALWTNDLERMKDFYVKYFGAE-SNDIYHNKKKGFRSYfLTFDSGARLELMSRPDVTDPDKEVERTGLAHIAFSV 78
 
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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