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Conserved domains on  [gi|757781992|ref|WP_043000576|]
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MULTISPECIES: VOC family protein [Citrobacter]

Protein Classification

VOC family protein( domain architecture ID 50733)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VOC super family cl14632
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 2-126 5.83e-49

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


The actual alignment was detected with superfamily member cd07241:

Pssm-ID: 472697  Cd Length: 125  Bit Score: 152.56  E-value: 5.83e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992   2 KIAHMALWTTELEAQARFWTGFFGGTLNEKYISKNnPGFESYFVRIGDDIAIELMTKPALRALRPDNQTTGWVHLAIAVG 81
Cdd:cd07241    1 KIEHVALWTNDLERMKDFYVKYFGAESNDIYHNKK-KGFRSYFLTFDSGARLELMSRPDVTDPDKEVERTGLAHIAFSVG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 757781992  82 SAKKVDALAKKARALGI-LVSPPRTTGDGYYEAVIKDPDGNFIEIV 126
Cdd:cd07241   80 SKEAVDELTERLRADGYaVVGGPRTTGDGYYESVILDPEGNRIEIT 125
 
Name Accession Description Interval E-value
VOC_BsYyaH cd07241
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal ...
 2-126 5.83e-49

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: 152.56  E-value: 5.83e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992   2 KIAHMALWTTELEAQARFWTGFFGGTLNEKYISKNnPGFESYFVRIGDDIAIELMTKPALRALRPDNQTTGWVHLAIAVG 81
Cdd:cd07241    1 KIEHVALWTNDLERMKDFYVKYFGAESNDIYHNKK-KGFRSYFLTFDSGARLELMSRPDVTDPDKEVERTGLAHIAFSVG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 757781992  82 SAKKVDALAKKARALGI-LVSPPRTTGDGYYEAVIKDPDGNFIEIV 126
Cdd:cd07241   80 SKEAVDELTERLRADGYaVVGGPRTTGDGYYESVILDPEGNRIEIT 125
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-127 5.73e-26

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: 94.29  E-value: 5.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992   1 MKIAHMALWTTELEAQARFWTGFFGGTLNEKYiSKNNPGFESYFVRIGDDIAIELMTKPALRalrPDNQTTGWVHLAIAV 80
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRT-DFGDGGFGHAFLRLGDGTELELFEAPGAA---PAPGGGGLHHLAFRV 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 757781992  81 GSakkVDALAKKARALGI-LVSPPRTTGDGYYEAVIKDPDGNFIEIVE 127
Cdd:COG0346   77 DD---LDAAYARLRAAGVeIEGEPRDRAYGYRSAYFRDPDGNLIELVE 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-125 1.59e-13

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 62.08  E-value: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992    2 KIAHMALWTTELEAQARFWTGFFGGTLNEKYiSKNNPGFESYFVRIGDDIAIELMTKPALRALRPDNQTTGWVHLAIAVG 81
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEET-DAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSVD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 757781992   82 sakKVDALAKKARALGI-LVSPPRTTGDGYYEAVIKDPDGNFIEI 125
Cdd:pfam00903  80 ---DVDAAYDRLKAAGVeIVREPGRHGWGGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
VOC_BsYyaH cd07241
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal ...
 2-126 5.83e-49

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: 152.56  E-value: 5.83e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992   2 KIAHMALWTTELEAQARFWTGFFGGTLNEKYISKNnPGFESYFVRIGDDIAIELMTKPALRALRPDNQTTGWVHLAIAVG 81
Cdd:cd07241    1 KIEHVALWTNDLERMKDFYVKYFGAESNDIYHNKK-KGFRSYFLTFDSGARLELMSRPDVTDPDKEVERTGLAHIAFSVG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 757781992  82 SAKKVDALAKKARALGI-LVSPPRTTGDGYYEAVIKDPDGNFIEIV 126
Cdd:cd07241   80 SKEAVDELTERLRADGYaVVGGPRTTGDGYYESVILDPEGNRIEIT 125
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-127 5.73e-26

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: 94.29  E-value: 5.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992   1 MKIAHMALWTTELEAQARFWTGFFGGTLNEKYiSKNNPGFESYFVRIGDDIAIELMTKPALRalrPDNQTTGWVHLAIAV 80
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRT-DFGDGGFGHAFLRLGDGTELELFEAPGAA---PAPGGGGLHHLAFRV 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 757781992  81 GSakkVDALAKKARALGI-LVSPPRTTGDGYYEAVIKDPDGNFIEIVE 127
Cdd:COG0346   77 DD---LDAAYARLRAAGVeIEGEPRDRAYGYRSAYFRDPDGNLIELVE 121
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 5-125 5.58e-20

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: 78.72  E-value: 5.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992   5 HMALWTTELEAQARFWTGFFGGTLNEKyisknNPGFESYFVRIGDDIAIELMTkpalRALRPDNQTTGWVHLAIAVGSAK 84
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSR-----NEGGGFAFLRLGPGLRLALLE----GPEPERPGGGGLFHLAFEVDDVD 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 757781992  85 KVDALAKKARALGILVSPPRTTGDGYYEAVIKDPDGNFIEI 125
Cdd:cd06587   72 EVDERLREAGAEGELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
1-126 1.47e-14

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 65.36  E-value: 1.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992   1 MKIAHMALWTTELEAQARFWTGFFGGTLNEKYisknnpGFESYFVRIGDDIAIELMTKPalrALRPDNQTTGWVHLAIAV 80
Cdd:COG2514    2 TRLGHVTLRVRDLERSAAFYTDVLGLEVVERE------GGRVYLRADGGEHLLVLEEAP---GAPPRPGAAGLDHVAFRV 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 757781992  81 GSAKKVDALAKKARALGILVSPPRTTGDGyyEAV-IKDPDGNFIEIV 126
Cdd:COG2514   73 PSRADLDAALARLAAAGVPVEGAVDHGVG--ESLyFRDPDGNLIELY 117
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-127 2.53e-14

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 64.27  E-value: 2.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992   1 MKIAHMALWTTELEAQARFWTGFFGGTLNEKYisknNPGFESYFVRIGDDIAIELMTkpalralRPDNQTTGWVHLAIAV 80
Cdd:COG3324    3 GTIVWVELPVDDLERAKAFYEEVFGWTFEDDA----GPGGDYAEFDTDGGQVGGLMP-------GAEEPGGPGWLLYFAV 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 757781992  81 GSakkVDALAKKARALGI-LVSPPRTTGDGYYEAVIKDPDGNFIEIVE 127
Cdd:COG3324   72 DD---LDAAVARVEAAGGtVLRPPTDIPPWGRFAVFRDPEGNRFGLWQ 116
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 13-126 9.39e-14

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 62.92  E-value: 9.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992  13 LEAQARFWTGFfGGTLNEKYiskNNPGFEsyFVRIGDDIAIELMTKPALRAL--RP--DNQTTGWVHLAIAVGSAKKVDA 88
Cdd:COG3607   14 LERSRAFYEAL-GFTFNPQF---SDEGAA--CFVLGEGIVLMLLPREKFATFtgKPiaDATGFTEVLLALNVESREEVDA 87

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 757781992  89 LAKKARALGI-LVSPPRTTGDGYYeAVIKDPDGNFIEIV 126
Cdd:COG3607   88 LVAKALAAGGtVLKPPQDVGGMYS-GYFADPDGHLWEVA 125
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-125 1.59e-13

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 62.08  E-value: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992    2 KIAHMALWTTELEAQARFWTGFFGGTLNEKYiSKNNPGFESYFVRIGDDIAIELMTKPALRALRPDNQTTGWVHLAIAVG 81
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEET-DAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSVD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 757781992   82 sakKVDALAKKARALGI-LVSPPRTTGDGYYEAVIKDPDGNFIEI 125
Cdd:pfam00903  80 ---DVDAAYDRLKAAGVeIVREPGRHGWGGRYSYFRDPDGNLIEL 121
VOC_BsYqjT cd07242
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; The vicinal ...
 3-126 2.38e-08

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: 48.64  E-value: 2.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992   3 IAHMALWTTELEAQARFWT-----GFFGGTLNEKYISKNNPGFESYFVRIGDDiaielMTKPALRALRPdnqttGWVHLA 77
Cdd:cd07242    2 VSHVELAVSDLHRSFKWFEwilglGWKEYDTWSFGPSWKLSGGSLLVVQQTDE-----FATPEFDRARV-----GLNHLA 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 757781992  78 IAVGSAKKVDALAKKARALGILVSP----PRTTGDGYYEAVIKDPDGNFIEIV 126
Cdd:cd07242   72 FHAESREAVDELTEKLAKIGGVRTYgdrhPFAGGPPHYAAFCEDPDGIKLELV 124
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 5-126 1.21e-07

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: 46.86  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992   5 HMALWTTELEAQARFWTGFFGgtLNEKYISKNN-----PGFESYFVRIGDDiaielmTKPALRalrpdnqttgwvHLAIA 79
Cdd:cd08362    6 YVALGVPDLAAEREFYTEVWG--LEEVAEDDDVvylraEGSEHHVLRLRQS------DENRLD------------LIAFA 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 757781992  80 VGSAKKVDALAKKARALGI-LVSPPRTTGD--GYYEAVIKDPDGNFIEIV 126
Cdd:cd08362   66 AATRADVDALAARLAAAGVrILSEPGPLDDpgGGYGFRFFDPDGRTIEVS 115
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 2-126 1.31e-07

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: 47.33  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992   2 KIAHMALWTTELEAQARFWTGFFGGTL----------NEKYISKNNPGFESYF-------VRIGDDIAIEL--MTKPALR 62
Cdd:cd16361    1 GVNHVGITVPDLDAAVEFYTDVLGAEVvyrstplaegDRGGGEMRAAGFVPGFarariamLRLGPGPGIELfeYKGPEQR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992  63 ALRPDNQTTGWVHLAIAVgsaKKVDALAKK-ARALGILVSPPRTTGD-----GYYEAVIKDPDGNFIEIV 126
Cdd:cd16361   81 APVPRNSDVGIFHFALQV---DDVEAAAERlAAAGGKVLMGPREIPDggpgkGNRMVYLRDPWGTLIELV 147
PsjN_like cd16356
Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme ...
 8-125 2.82e-07

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: 45.88  E-value: 2.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992   8 LWTTELEAQARFWTGFFGGtlnEKYISKNNPGFESyfVRIGDDIaIELMTKPALRAL---RPDNQTTGWVHLAIAVGSAK 84
Cdd:cd16356    4 IFTADIVALSDFYSELFGL---EEIFEIRSPIFRG--LRTGDSC-LGFNAPEAYELLglpEFSDTPGIRILLTFDVDDVE 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 757781992  85 KVDALAKKARALG-ILVSPPRTTGDGYYEAVIKDPDGNFIEI 125
Cdd:cd16356   78 AVDRLVPRAAALGaTLIKPPYDTYYGWYQAVLLDPEGNVFRI 119
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-125 1.96e-06

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


Pssm-ID: 319917 [Multi-domain]  Cd Length: 120  Bit Score: 43.60  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992   5 HMALWTTELEAQARFWTGFFGGTlnekyISKNNPGFESYFVrigDDIAIELmtkpALRAlRPDNQTTGWVHLAIAVGSAK 84
Cdd:cd07254    4 HLSLNVTDLERSIRFYSDLFGAE-----PAKRKADYAKFML---EDPPLNL----ALLV-NDRKEPYGLNHLGIQVDSKE 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 757781992  85 KVDALAKKARALGI-LVSPPRTT-----GDGYYeavIKDPDGNFIEI 125
Cdd:cd07254   71 EVAALKARAEAAGLpVRKEPRTTccyavQDKFW---LTDPDGNAWEF 114
Glyoxalase_6 pfam18029
Glyoxalase-like domain; This entry comprises a diverse set of domains related to the ...
 10-121 2.23e-06

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: 43.14  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992   10 TTELEAQARFWTGFFGGTLnekyisknnpGFESYFVRIGDDIAIELMTKPALRALRPDNQTTGW--VHLAIAVGSakkVD 87
Cdd:pfam18029   6 CADPAALAAFWSAALGWEV----------VPDDTALPDPDGGGPIGGGGPRLLFQRVPEPKPGKnrVHLDLAVDD---LE 72

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 757781992   88 ALAKKARALG-ILVSPPRttGDGYYEAVIKDPDGN 121
Cdd:pfam18029  73 AAVARLVALGaTVLDDGD--DPDGGRWVLADPEGN 105
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 1-125 1.83e-05

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: 41.14  E-value: 1.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992   1 MKIAHMALWTTELEAQARFWTGFFGGTLNEKYISKnnpgfeSYFVRIGDDIAIELMTKPALRaLRPDNqTTGWVHLAIAV 80
Cdd:cd07255    1 TRIGRVTLKVADLERQSAFYQNVIGLSVLKQNASR------AYLGVDGKQVLLVLEAIPDAV-LAPRS-TTGLYHFAILL 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 757781992  81 GSAKKVDALAKKARALGILVSPprttGD-GYYEAVI-KDPDGNFIEI 125
Cdd:cd07255   73 PDRKALGRALAHLAEHGPLIGA----ADhGVSEAIYlSDPEGNGIEI 115
VOC_like cd09012
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 10-126 2.44e-05

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


Pssm-ID: 319954  Cd Length: 127  Bit Score: 40.83  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992  10 TTELEAQARFWTGFfGGTLNEKYISKNNPGFesyfvRIGDDIAIELMTKPALRALRP-----DNQTTGWVHLAIAVGSAK 84
Cdd:cd09012    8 VTDLEASTAFYEAL-GFKKNPQFSDEHASCM-----VVSDNIFVMLLAHDRFKTFIPepiavDAKKSTEVLLTLSAKSRQ 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 757781992  85 KVDALAKKARALGILVSPPRTTGD--GYYEAVIKDPDGNFIEIV 126
Cdd:cd09012   82 EVDAFVDKAVEAGGKADPYVNGGDegFMYGRSFEDLDGHLWEVV 125
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-127 2.76e-05

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


Pssm-ID: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 40.39  E-value: 2.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992   3 IAHMALWTTELEAQARFWTGFFGgtLNEKYISKNNPGFEsyfVRIGDdIAIELMT-KPALRALRPDNQTTgwvHLAIAVg 81
Cdd:cd07264    1 IAYIVLYVDDFAASLRFYRDVLG--LPPRFLHEEGEYAE---FDTGE-TKLALFSrKEMARSGGPDRRGS---AFELGF- 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 757781992  82 SAKKVDALAKKARALGI-LVSPPRTTGDGYYEAVIKDPDGNFIEIVE 127
Cdd:cd07264   71 EVDDVEATVEELVERGAeFVREPANKPWGQTVAYVRDPDGNLIEICE 117
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-125 4.91e-05

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


Pssm-ID: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 39.99  E-value: 4.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992   5 HMALWTTELEAQARFWTGFFGGTLNEKyisKNNPGFESYFVRIGDDIAIELMTKPALRALRPDNQTTGWVHLAIAVGSak 84
Cdd:cd07245    3 HVALACPDLERARRFYTDVLGLEEVPR---PPFLKFGGAWLYLGGGQQIHLVVEQNPSELPRPEHPGRDRHPSFSVPD-- 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 757781992  85 kVDALAKKARALGILVsPPRTTGDGYYEAV-IKDPDGNFIEI 125
Cdd:cd07245   78 -LDALKQRLKEAGIPY-TESTSPGGGVTQLfFRDPDGNRLEF 117
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 74-126 6.62e-05

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


Pssm-ID: 319923 [Multi-domain]  Cd Length: 121  Bit Score: 39.52  E-value: 6.62e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 757781992  74 VHLAIAVGSAKKVDALAKKARALG---ILVSPPR-TTGDGYYEAVIKDPDGNFIEIV 126
Cdd:cd07262   64 THVAFAAPSRAAVDAFHAAALAAGgtdNGAPGLRpHYHPGYYAAYVRDPDGNKIEAV 120
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 1-127 2.90e-04

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: 37.91  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992   1 MKIAHMALWTTELEAQARFWTGFFGGTLNEKYISknnPGFESYF--VRIGDDIaIELMTKPALRALRPDNQTTGWVHLAI 78
Cdd:cd08352    1 KKIHHIAIICSDYEKSKDFYVDKLGFEIIREHYR---PERNDIKldLALGGYQ-LELFIKPDAPARPSYPEALGLRHLAF 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 757781992  79 AVGSakkVDALAKKARALGILVSPPRT---TGDGYyeAVIKDPDGNFIEIVE 127
Cdd:cd08352   77 KVED---VEATVAELKSLGIETEPIRVddfTGKKF--TFFFDPDGLPLELYE 123
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 76-126 2.35e-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: 319914 [Multi-domain]  Cd Length: 120  Bit Score: 35.35  E-value: 2.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 757781992  76 LAIAVGSAKKVDAL-AKKARALGILVSPPRTTGDGYYEAVIKDPDGNFIEIV 126
Cdd:cd07251   67 LAHNVRSREEVDQLlAKAVAAGGKILKPPQEVFWGGYSGYFADPDGHIWEVA 118
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 5-124 2.61e-03

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


Pssm-ID: 319933  Cd Length: 118  Bit Score: 35.23  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992   5 HMALWTTELEAQARFWTGFFGGTLNEKYISKNNPGFESYFVRIGDdIAIELMTKPALralrpdnQTTGWVHLAIAVGSAK 84
Cdd:cd08345    1 HITLIVRDLEKSTAFLQDIFGAREVYSSGDKTFSLSKEKFFLLGG-LWIALMEGESL-------QERSYTHIAFQIQSED 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 757781992  85 kVDALAKKARALGILVSPPRTT----GDGYYeavIKDPDGNFIE 124
Cdd:cd08345   73 -FDRYAERLGALGVEMRPPRPRvegeGRSIY---FYDPDNHLFE 112
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 3-121 3.61e-03

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: 34.55  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992   3 IAHMALWTTELEAQARFWTGFFGGTLNEkyiskNNPGFESY-FVRIGDDIAIELMTKPALRALRPdnqtTGWVHLaIAVG 81
Cdd:cd07247    1 PVWFELPTTDLERAKAFYGAVFGWTFED-----EGDGGGDYaLFTAGGGAVGGLMRAPEEVAGAP----PGWLIY-FAVD 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 757781992  82 SakkVDALAKKARALG-ILVSPPRTTGDGYYEAVIKDPDGN 121
Cdd:cd07247   71 D---LDAALARVEAAGgKVVVPPTDIPGGGRFAVFADPEGN 108
EhpR_like cd07261
phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter ...
 69-125 7.05e-03

phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter agglomerans confers resistance by binding D-alanyl-griseoluteic acid and acting as a chaperone involved in exporting the antibiotic rather than by altering it chemically. EhpR is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319922  Cd Length: 114  Bit Score: 33.91  E-value: 7.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 757781992  69 QTTGWVHLAIAVGSAKKVDALAKKARALGILVSPPRTTGDGYYEAVIKDPDGNFIEI 125
Cdd:cd07261   56 VTGGGAELSFMVPSGEQVDEVYAEWKAMGIPIIQEPTTMDFGYTFVATDPDGHRLRV 112
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
14-125 8.48e-03

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 33.68  E-value: 8.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757781992  14 EAQARFWTGFFGGTlnEKYISKNNPGFESY-FVRIGDdiaIELMtkpaLRALRPDNQTTGWVHLAIAVgSAKKVDALAKK 92
Cdd:COG2764   12 EEALEFYEDVFGFE--VVFRMTDPDGKIMHaELRIGG---SVLM----LSDAPPDSPAAEGNGVSLSL-YVDDVDALFAR 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 757781992  93 ARALG-ILVSPPRTTGDGYYEAVIKDPDGNFIEI 125
Cdd:COG2764   82 LVAAGaTVVMPLQDTFWGDRFGMVRDPFGVLWMI 115
 
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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