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Conserved domains on  [gi|446834445|ref|WP_000911701|]
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MULTISPECIES: FosBx1 family fosfomycin resistance bacillithiol transferase [Bacillus]

Protein Classification

metallothiol transferase FosB( domain architecture ID 10012138)

metallothiol transferase FosB confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
fosBx1_fam super family cl49508
FosBx1 family fosfomycin resistance bacillithiol transferase; Members of this family, found in ...
 1-138 7.68e-100

FosBx1 family fosfomycin resistance bacillithiol transferase; Members of this family, found in Bacillus cereus and related species that synthesis bacillithiol rather than glutathione, are VOC family thiol transferases. They provide resistance to the antibiotic fosfomycin by transferring either bacillithiol or cysteine (but not glutathione) to fosfomycin, leaving it inactive. Note that this family is drawn rather narrowly, and several such families, all non-overlapping, appear in B. cereus and its close relatives. This family includes proteins that have been named FosBx1 (although the original source of that name is hard to trace), and the protein studied crystallographically by Thompson, et al. (see PMID:24004181).


The actual alignment was detected with superfamily member NF041541:

Pssm-ID: 469426  Cd Length: 138  Bit Score: 282.10  E-value: 7.68e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445   1 MLKGINHLCFSVSNLENSILFYERVLEGELLVKGRKLAYFNICGVWIALNEEAHIPRKEIHQSYTHLAFSVEQKDFERLL 80
Cdd:NF041541   1 MLKGINHLCFSVSNLEKSITFYEKVLEGELLVKGRKLAYFNICGVWIALNEETHIPRNEIHQSYTHIAFSVEQEDFERLL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446834445  81 HRLEENNVHILQGRERNVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREEKPHMTFY 138
Cdd:NF041541  81 QRLEENDVHILQGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREEKPHMTFY 138
 
Name Accession Description Interval E-value
fosBx1_fam NF041541
FosBx1 family fosfomycin resistance bacillithiol transferase; Members of this family, found in ...
 1-138 7.68e-100

FosBx1 family fosfomycin resistance bacillithiol transferase; Members of this family, found in Bacillus cereus and related species that synthesis bacillithiol rather than glutathione, are VOC family thiol transferases. They provide resistance to the antibiotic fosfomycin by transferring either bacillithiol or cysteine (but not glutathione) to fosfomycin, leaving it inactive. Note that this family is drawn rather narrowly, and several such families, all non-overlapping, appear in B. cereus and its close relatives. This family includes proteins that have been named FosBx1 (although the original source of that name is hard to trace), and the protein studied crystallographically by Thompson, et al. (see PMID:24004181).


Pssm-ID: 469426  Cd Length: 138  Bit Score: 282.10  E-value: 7.68e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445   1 MLKGINHLCFSVSNLENSILFYERVLEGELLVKGRKLAYFNICGVWIALNEEAHIPRKEIHQSYTHLAFSVEQKDFERLL 80
Cdd:NF041541   1 MLKGINHLCFSVSNLEKSITFYEKVLEGELLVKGRKLAYFNICGVWIALNEETHIPRNEIHQSYTHIAFSVEQEDFERLL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446834445  81 HRLEENNVHILQGRERNVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREEKPHMTFY 138
Cdd:NF041541  81 QRLEENDVHILQGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREEKPHMTFY 138
PRK04101 PRK04101
metallothiol transferase FosB;
1-138 2.04e-98

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 278.37  E-value: 2.04e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445   1 MLKGINHLCFSVSNLENSILFYERVLEGELLVKGRKLAYFNICGVWIALNEEAHIPRKEIHQSYTHLAFSVEQKDFERLL 80
Cdd:PRK04101   1 MLKGINHICFSVSNLEKSIEFYEKVLGAKLLVKGRKTAYFDLNGLWIALNEEKDIPRNEIHQSYTHIAFSIEEEDFDHWY 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446834445  81 HRLEENNVHILQGRERNVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREEKPHMTFY 138
Cdd:PRK04101  81 QRLKENDVNILPGRERDERDKKSIYFTDPDGHKFEFHTGTLQDRLNYYKEEKPHMTFY 138
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 5-135 7.45e-71

fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin resistant protein. FosB is a Mg(2+)-dependent L-cysteine thiol transferase. Fosfomycin inhibits the enzyme UDP-nacetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosB catalyzes the Mg(II) dependent addition of L-cysteine to the epoxide ring of fosfomycin, (1R,2S)-epoxypropylphosphonic acid, rendering it inactive. FosB is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319951 [Multi-domain]  Cd Length: 131  Bit Score: 208.74  E-value: 7.45e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445   5 INHLCFSVSNLENSILFYERVLEGELLVKGRKLAYFNICGVWIALNEEAHIPRKEIHQSYTHLAFSVEQKDFERLLHRLE 84
Cdd:cd08363    1 INHITFSVSNLNKSIAFYKDVLDAKLLVLGEKTAYFDLNGLWLALNVQEDIPRNEISHSYTHIAFSIDEEDLDAFKERLK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446834445  85 ENNVHILQGRERNVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREEKPHM 135
Cdd:cd08363   81 DNGVNILEGRKRDILEGQSIYFTDPDGHLFELHTGTLEDRLEYYKEEKPHM 131
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 3-117 5.68e-21

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: 81.96  E-value: 5.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445   3 KGINHLCFSVSNLENSILFYERVLEGELLVK------GRKLAYFNIC-GVWIALNEEAHIPRKEIHQSYTHLAFSVEqkD 75
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRtdfgdgGFGHAFLRLGdGTELELFEAPGAAPAPGGGGLHHLAFRVD--D 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446834445  76 FERLLHRLEENNVHILQGRERNVRDCESIYFVDPDGHKFEFH 117
Cdd:COG0346   79 LDAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELV 120
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
4-116 2.50e-13

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 62.08  E-value: 2.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445    4 GINHLCFSVSNLENSILFYERVLEGELLVK-------GRKLAYFNICGVWIALNEEAHIPRKEIHQSYTHLAFSVEQK-D 75
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEEtdageegGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSVdD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 446834445   76 FERLLHRLEENNVHILQGRERNVRDCESIYFVDPDGHKFEF 116
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
fosBx1_fam NF041541
FosBx1 family fosfomycin resistance bacillithiol transferase; Members of this family, found in ...
 1-138 7.68e-100

FosBx1 family fosfomycin resistance bacillithiol transferase; Members of this family, found in Bacillus cereus and related species that synthesis bacillithiol rather than glutathione, are VOC family thiol transferases. They provide resistance to the antibiotic fosfomycin by transferring either bacillithiol or cysteine (but not glutathione) to fosfomycin, leaving it inactive. Note that this family is drawn rather narrowly, and several such families, all non-overlapping, appear in B. cereus and its close relatives. This family includes proteins that have been named FosBx1 (although the original source of that name is hard to trace), and the protein studied crystallographically by Thompson, et al. (see PMID:24004181).


Pssm-ID: 469426  Cd Length: 138  Bit Score: 282.10  E-value: 7.68e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445   1 MLKGINHLCFSVSNLENSILFYERVLEGELLVKGRKLAYFNICGVWIALNEEAHIPRKEIHQSYTHLAFSVEQKDFERLL 80
Cdd:NF041541   1 MLKGINHLCFSVSNLEKSITFYEKVLEGELLVKGRKLAYFNICGVWIALNEETHIPRNEIHQSYTHIAFSVEQEDFERLL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446834445  81 HRLEENNVHILQGRERNVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREEKPHMTFY 138
Cdd:NF041541  81 QRLEENDVHILQGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREEKPHMTFY 138
PRK04101 PRK04101
metallothiol transferase FosB;
1-138 2.04e-98

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 278.37  E-value: 2.04e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445   1 MLKGINHLCFSVSNLENSILFYERVLEGELLVKGRKLAYFNICGVWIALNEEAHIPRKEIHQSYTHLAFSVEQKDFERLL 80
Cdd:PRK04101   1 MLKGINHICFSVSNLEKSIEFYEKVLGAKLLVKGRKTAYFDLNGLWIALNEEKDIPRNEIHQSYTHIAFSIEEEDFDHWY 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446834445  81 HRLEENNVHILQGRERNVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREEKPHMTFY 138
Cdd:PRK04101  81 QRLKENDVNILPGRERDERDKKSIYFTDPDGHKFEFHTGTLQDRLNYYKEEKPHMTFY 138
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 5-135 7.45e-71

fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin resistant protein. FosB is a Mg(2+)-dependent L-cysteine thiol transferase. Fosfomycin inhibits the enzyme UDP-nacetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosB catalyzes the Mg(II) dependent addition of L-cysteine to the epoxide ring of fosfomycin, (1R,2S)-epoxypropylphosphonic acid, rendering it inactive. FosB is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319951 [Multi-domain]  Cd Length: 131  Bit Score: 208.74  E-value: 7.45e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445   5 INHLCFSVSNLENSILFYERVLEGELLVKGRKLAYFNICGVWIALNEEAHIPRKEIHQSYTHLAFSVEQKDFERLLHRLE 84
Cdd:cd08363    1 INHITFSVSNLNKSIAFYKDVLDAKLLVLGEKTAYFDLNGLWLALNVQEDIPRNEISHSYTHIAFSIDEEDLDAFKERLK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446834445  85 ENNVHILQGRERNVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREEKPHM 135
Cdd:cd08363   81 DNGVNILEGRKRDILEGQSIYFTDPDGHLFELHTGTLEDRLEYYKEEKPHM 131
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 4-130 2.17e-37

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: 123.55  E-value: 2.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445   4 GINHLCFSVSNLENSILFYERVLEGELLVKGRKLAYFNICGVWIALNEEAHIPRkeiHQSYTHLAFSVEQKDFERLLHRL 83
Cdd:cd07244    1 GINHITLAVSDLERSLAFYVDLLGFKPHVRWDKGAYLTAGDLWLCLSLDPAAEP---SPDYTHIAFTVSEEDFEELSERL 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446834445  84 EENNVHILQgreRNVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYRE 130
Cdd:cd07244   78 RAAGVKIWQ---ENSSEGDSLYFLDPDGHKLELHVGSLESRLASLRE 121
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 7-121 1.15e-34

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: 116.50  E-value: 1.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445   7 HLCFSVSNLENSILFYERVLeGELLVKGR--------KLAYFNICGVWIALNEEAHIPRkeihQSYTHLAFSVEQKDFER 78
Cdd:cd08345    1 HITLIVRDLEKSTAFLQDIF-GAREVYSSgdktfslsKEKFFLLGGLWIALMEGESLQE----RSYTHIAFQIQSEDFDR 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446834445  79 LLHRLEENNVHILQGRERNVRDCESIYFVDPDGHKFEFHSGTL 121
Cdd:cd08345   76 YAERLGALGVEMRPPRPRVEGEGRSIYFYDPDNHLFELHTGTL 118
FosX cd08364
fosfomycin resistant protein subfamily FosX; This subfamily family contains FosX, a fosfomycin ...
 3-128 1.57e-22

fosfomycin resistant protein subfamily FosX; This subfamily family contains FosX, a fosfomycin resistant protein. FosX is a Mn(II)-dependent fosfomycin-specific epoxide hydrolase. Fosfomycin inhibits the enzyme UDP-Nacetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosX catalyzes the addition of a water molecule to the C1 position of the antibiotic with inversion of the configuration at C1 in the presence of Mn(II). The hydrated fosfomycin loses the inhibition activity. FosX is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319952  Cd Length: 130  Bit Score: 85.79  E-value: 1.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445   3 KGINHLCFSVSNLENSILFYERVLEG-ELLVKGRKL------AYFNICGVWIALNEEAHIPRKeihqSYTHLAFSVEQKD 75
Cdd:cd08364    2 EGISHITFIVKDLDRTAAFLTEIFGAeEVYDSGAETfslspeKFFLIGGLWIAIMEGEPLLER----SYNHIAFKVSEGD 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446834445  76 FERLLHRLEENNVHILQGRERNVRDCESIYFVDPDGHKFEFHSGTLQDRLNYY 128
Cdd:cd08364   78 LDEYRARIKKLGLEIRPPRSRVQGEGRSLYFYDFDNHLFELHTGTLEERLARY 130
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 3-117 5.68e-21

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: 81.96  E-value: 5.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445   3 KGINHLCFSVSNLENSILFYERVLEGELLVK------GRKLAYFNIC-GVWIALNEEAHIPRKEIHQSYTHLAFSVEqkD 75
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRtdfgdgGFGHAFLRLGdGTELELFEAPGAAPAPGGGGLHHLAFRVD--D 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446834445  76 FERLLHRLEENNVHILQGRERNVRDCESIYFVDPDGHKFEFH 117
Cdd:COG0346   79 LDAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELV 120
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
2-116 3.72e-18

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 74.99  E-value: 3.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445   2 LKGINHLCFSVSNLENSILFYERVLEGELLVKGRKLAYFNICG--VWIALNEEAHIPRKEIHQSYTHLAFSVE-QKDFER 78
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGgeHLLVLEEAPGAPPRPGAAGLDHVAFRVPsRADLDA 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446834445  79 LLHRLEENNVHILQGRERNVRdcESIYFVDPDGHKFEF 116
Cdd:COG2514   81 ALARLAAAGVPVEGAVDHGVG--ESLYFRDPDGNLIEL 116
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 7-116 1.02e-13

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: 62.93  E-value: 1.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445   7 HLCFSVSNLENSILFYERVLEGELL--VKGRKLAYFNIC-GVWIALNEEAHiPRKEIHQSYTHLAFSVEQKDFERLLHRL 83
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVsrNEGGGFAFLRLGpGLRLALLEGPE-PERPGGGGLFHLAFEVDDVDEVDERLRE 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446834445  84 EENNVHILQGRERNVRDCESIYFVDPDGHKFEF 116
Cdd:cd06587   80 AGAEGELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
4-116 2.50e-13

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 62.08  E-value: 2.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445    4 GINHLCFSVSNLENSILFYERVLEGELLVK-------GRKLAYFNICGVWIALNEEAHIPRKEIHQSYTHLAFSVEQK-D 75
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEEtdageegGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSVdD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 446834445   76 FERLLHRLEENNVHILQGRERNVRDCESIYFVDPDGHKFEF 116
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-118 1.44e-09

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 52.33  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445   1 MLKGINHLCFSVSNLENSILFYERVLEGELLVK---GRKLAYFNI-CGVWIALNEEAHIPRKeihqSYTHLAFSVEqkDF 76
Cdd:COG3324    1 MPGTIVWVELPVDDLERAKAFYEEVFGWTFEDDagpGGDYAEFDTdGGQVGGLMPGAEEPGG----PGWLLYFAVD--DL 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446834445  77 ERLLHRLEENNVHILQGRERNVRDCESIYFVDPDGHKFEFHS 118
Cdd:COG3324   75 DAAVARVEAAGGTVLRPPTDIPPWGRFAVFRDPEGNRFGLWQ 116
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 3-116 7.09e-06

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: 42.30  E-value: 7.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445   3 KGINHLCFSVSNLENSILFYERVLEGELLVKGRKLAYFNICG--VWIALNEEAHIPRKEihQSYT---HLAFSV-EQKDF 76
Cdd:cd07255    1 TRIGRVTLKVADLERQSAFYQNVIGLSVLKQNASRAYLGVDGkqVLLVLEAIPDAVLAP--RSTTglyHFAILLpDRKAL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446834445  77 ERLLHRLEENNVHIlQGRERNVRdcESIYFVDPDGHKFEF 116
Cdd:cd07255   79 GRALAHLAEHGPLI-GAADHGVS--EAIYLSDPEGNGIEI 115
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 9-119 1.57e-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: 319942  Cd Length: 122  Bit Score: 41.58  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445   9 CFSVSNLENSILFYERVLEGELLVKGRKLAYFNIC-GVWIALNEEA--------HIPRKEIHQSyTHLAFSVEQKDFERL 79
Cdd:cd08354    5 CLYADDLDAAEAFYEDVLGLKPMLRSGRHAFFRLGpQVLLVFDPGAtskdvrtgEVPGHGASGH-GHFAFAVPTEELAAW 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446834445  80 LHRLEENNVHIlQGRERNVRDCESIYFVDPDGHKFEFHSG 119
Cdd:cd08354   84 EARLEAKGVPI-ESYTQWPEGGKSLYFRDPAGNLVELASA 122
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 2-115 1.69e-05

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: 41.44  E-value: 1.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445   2 LKGINHLCFSVSNLENSILFYERVL--EGELLVKGRKLAYFNIcgVWIALNEEAH--IPRKEIHQSYT-HLAFSVEqKDF 76
Cdd:cd07253    1 IKRLDHLVLTVKDIERTIDFYTKVLgmTVVTFKEGRKALRFGN--QKINLHQKGKefEPKASAPTPGSaDLCFITE-TPI 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446834445  77 ERLLHRLEENNVHILQGRERN---VRDCESIYFVDPDGHKFE 115
Cdd:cd07253   78 DEVLEHLEACGVTIEEGPVKRtgaLGPILSIYFRDPDGNLIE 119
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 12-118 2.19e-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: 41.16  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445  12 VSNLENSILFYERVL---EGELLVKGRkLAYFNICGVWIALN---EEAHIPRKEIHQSYTHLAFSVEqkDFERLLHRLEE 85
Cdd:cd07264    8 VDDFAASLRFYRDVLglpPRFLHEEGE-YAEFDTGETKLALFsrkEMARSGGPDRRGSAFELGFEVD--DVEATVEELVE 84

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446834445  86 NNVHILQGRERNVRDCESIYFVDPDGHKFEFHS 118
Cdd:cd07264   85 RGAEFVREPANKPWGQTVAYVRDPDGNLIEICE 117
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-116 4.04e-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: 40.38  E-value: 4.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445   5 INHLCFSVSNLENSILFYERVLEGELLVK----GRKLAYFNICGVW----IALNEEAHIPRKEIHQSYTHLAFSVEqkDF 76
Cdd:cd07245    1 LDHVALACPDLERARRFYTDVLGLEEVPRppflKFGGAWLYLGGGQqihlVVEQNPSELPRPEHPGRDRHPSFSVP--DL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446834445  77 ERLLHRLEENNVHILQgRERNVRDCESIYFVDPDGHKFEF 116
Cdd:cd07245   79 DALKQRLKEAGIPYTE-STSPGGGVTQLFFRDPDGNRLEF 117
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-116 1.45e-04

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


Pssm-ID: 319917 [Multi-domain]  Cd Length: 120  Bit Score: 38.98  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445   7 HLCFSVSNLENSILFYERVLEGELLVKGRKLAYFNI--CGVWIALNEEahiPRKEIHQSYtHLAFSVEQKD-FERLLHRL 83
Cdd:cd07254    4 HLSLNVTDLERSIRFYSDLFGAEPAKRKADYAKFMLedPPLNLALLVN---DRKEPYGLN-HLGIQVDSKEeVAALKARA 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446834445  84 EENNVHILQgrERNVRDC----ESIYFVDPDGHKFEF 116
Cdd:cd07254   80 EAAGLPVRK--EPRTTCCyavqDKFWLTDPDGNAWEF 114
ChaP_like cd08351
ChaP, an enzyme involved in the biosynthesis of the antitumor agent chartreusin (cha), and ...
 66-116 7.02e-04

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


Pssm-ID: 319939  Cd Length: 118  Bit Score: 37.10  E-value: 7.02e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446834445  66 HLAFSVEQKDFERLLHRLEENNV-------HILQGRERNVRDCESIYFVDPDGHKFEF 116
Cdd:cd08351   59 HYAFLVSDDEFDAILARIRARGLeywadpqHREPGEINHNDGGRGVYFRDPDGHLLEI 116
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 3-117 5.93e-03

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: 34.44  E-value: 5.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446834445   3 KGINHLCFSVSNLENSILFYERVLEGELL------VKGRKLAYFNICGVWIAL----NEEAHIPRKEiHQSYTHLAFSVE 72
Cdd:cd08352    1 KKIHHIAIICSDYEKSKDFYVDKLGFEIIrehyrpERNDIKLDLALGGYQLELfikpDAPARPSYPE-ALGLRHLAFKVE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446834445  73 qkDFERLLHRLEENNVhilqgrernvrDCESI-----------YFVDPDGHKFEFH 117
Cdd:cd08352   80 --DVEATVAELKSLGI-----------ETEPIrvddftgkkftFFFDPDGLPLELY 122
 
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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