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Conserved domains on  [gi|446866507|ref|WP_000943763|]
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MULTISPECIES: fosfomycin resistance bacillithiol transferase FosBx1 [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 1.83e-103

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: 291.34  E-value: 1.83e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   1 MLRGINHICFSVSNLENSIMFYEKVLEGELLVKGRKLAYFNICGVWIALNEETHIPRNEIHQSYTHIAFSVEKEDFKCLI 80
Cdd:NF041541   1 MLKGINHLCFSVSNLEKSITFYEKVLEGELLVKGRKLAYFNICGVWIALNEETHIPRNEIHQSYTHIAFSVEQEDFERLL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446866507  81 QRLEENDVHILQGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYRDEKPHMTFY 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 1.83e-103

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: 291.34  E-value: 1.83e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   1 MLRGINHICFSVSNLENSIMFYEKVLEGELLVKGRKLAYFNICGVWIALNEETHIPRNEIHQSYTHIAFSVEKEDFKCLI 80
Cdd:NF041541   1 MLKGINHLCFSVSNLEKSITFYEKVLEGELLVKGRKLAYFNICGVWIALNEETHIPRNEIHQSYTHIAFSVEQEDFERLL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446866507  81 QRLEENDVHILQGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYRDEKPHMTFY 138
Cdd:NF041541  81 QRLEENDVHILQGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREEKPHMTFY 138
PRK04101 PRK04101
metallothiol transferase FosB;
1-138 2.33e-101

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 286.07  E-value: 2.33e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   1 MLRGINHICFSVSNLENSIMFYEKVLEGELLVKGRKLAYFNICGVWIALNEETHIPRNEIHQSYTHIAFSVEKEDFKCLI 80
Cdd:PRK04101   1 MLKGINHICFSVSNLEKSIEFYEKVLGAKLLVKGRKTAYFDLNGLWIALNEEKDIPRNEIHQSYTHIAFSIEEEDFDHWY 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446866507  81 QRLEENDVHILQGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYRDEKPHMTFY 138
Cdd:PRK04101  81 QRLKENDVNILPGRERDERDKKSIYFTDPDGHKFEFHTGTLQDRLNYYKEEKPHMTFY 138
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 5-135 4.20e-76

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: 221.84  E-value: 4.20e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   5 INHICFSVSNLENSIMFYEKVLEGELLVKGRKLAYFNICGVWIALNEETHIPRNEIHQSYTHIAFSVEKEDFKCLIQRLE 84
Cdd:cd08363    1 INHITFSVSNLNKSIAFYKDVLDAKLLVLGEKTAYFDLNGLWLALNVQEDIPRNEISHSYTHIAFSIDEEDLDAFKERLK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446866507  85 ENDVHILQGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYRDEKPHM 135
Cdd:cd08363   81 DNGVNILEGRKRDILEGQSIYFTDPDGHLFELHTGTLEDRLEYYKEEKPHM 131
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 3-117 9.54e-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: 81.19  E-value: 9.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   3 RGINHICFSVSNLENSIMFYEKVLEGELLVK------GRKLAYFNIC-GVWIALNEETHIPRNEIHQSYTHIAFSVEkeD 75
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRtdfgdgGFGHAFLRLGdGTELELFEAPGAAPAPGGGGLHHLAFRVD--D 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446866507  76 FKCLIQRLEENDVHILQGRERDVRDCESIYFVDPDGHKFEFH 117
Cdd:COG0346   79 LDAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELV 120
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
4-116 1.04e-13

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 62.85  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507    4 GINHICFSVSNLENSIMFYEKVLEGELLVK-------GRKLAYFNICGVWIALNEETHIPRNEIHQSYTHIAFSV-EKED 75
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEEtdageegGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAfSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 446866507   76 FKCLIQRLEENDVHILQGRERDVRDCESIYFVDPDGHKFEF 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 1.83e-103

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: 291.34  E-value: 1.83e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   1 MLRGINHICFSVSNLENSIMFYEKVLEGELLVKGRKLAYFNICGVWIALNEETHIPRNEIHQSYTHIAFSVEKEDFKCLI 80
Cdd:NF041541   1 MLKGINHLCFSVSNLEKSITFYEKVLEGELLVKGRKLAYFNICGVWIALNEETHIPRNEIHQSYTHIAFSVEQEDFERLL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446866507  81 QRLEENDVHILQGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYRDEKPHMTFY 138
Cdd:NF041541  81 QRLEENDVHILQGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYREEKPHMTFY 138
PRK04101 PRK04101
metallothiol transferase FosB;
1-138 2.33e-101

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 286.07  E-value: 2.33e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   1 MLRGINHICFSVSNLENSIMFYEKVLEGELLVKGRKLAYFNICGVWIALNEETHIPRNEIHQSYTHIAFSVEKEDFKCLI 80
Cdd:PRK04101   1 MLKGINHICFSVSNLEKSIEFYEKVLGAKLLVKGRKTAYFDLNGLWIALNEEKDIPRNEIHQSYTHIAFSIEEEDFDHWY 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446866507  81 QRLEENDVHILQGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYRDEKPHMTFY 138
Cdd:PRK04101  81 QRLKENDVNILPGRERDERDKKSIYFTDPDGHKFEFHTGTLQDRLNYYKEEKPHMTFY 138
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 5-135 4.20e-76

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: 221.84  E-value: 4.20e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   5 INHICFSVSNLENSIMFYEKVLEGELLVKGRKLAYFNICGVWIALNEETHIPRNEIHQSYTHIAFSVEKEDFKCLIQRLE 84
Cdd:cd08363    1 INHITFSVSNLNKSIAFYKDVLDAKLLVLGEKTAYFDLNGLWLALNVQEDIPRNEISHSYTHIAFSIDEEDLDAFKERLK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446866507  85 ENDVHILQGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYYRDEKPHM 135
Cdd:cd08363   81 DNGVNILEGRKRDILEGQSIYFTDPDGHLFELHTGTLEDRLEYYKEEKPHM 131
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 4-130 1.21e-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: 124.32  E-value: 1.21e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   4 GINHICFSVSNLENSIMFYEKVLEGELLVKGRKLAYFNICGVWIALNEETHIPRneiHQSYTHIAFSVEKEDFKCLIQRL 83
Cdd:cd07244    1 GINHITLAVSDLERSLAFYVDLLGFKPHVRWDKGAYLTAGDLWLCLSLDPAAEP---SPDYTHIAFTVSEEDFEELSERL 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446866507  84 EENDVHILQ-GRERDvrdcESIYFVDPDGHKFEFHSGTLQDRLNYYRD 130
Cdd:cd07244   78 RAAGVKIWQeNSSEG----DSLYFLDPDGHKLELHVGSLESRLASLRE 121
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 7-121 2.28e-37

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: 123.44  E-value: 2.28e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   7 HICFSVSNLENSIMFYEKVLeGELLVKGR--------KLAYFNICGVWIALNEETHIPRneihQSYTHIAFSVEKEDFKC 78
Cdd:cd08345    1 HITLIVRDLEKSTAFLQDIF-GAREVYSSgdktfslsKEKFFLLGGLWIALMEGESLQE----RSYTHIAFQIQSEDFDR 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446866507  79 LIQRLEENDVHILQGRERDVRDCESIYFVDPDGHKFEFHSGTL 121
Cdd:cd08345   76 YAERLGALGVEMRPPRPRVEGEGRSIYFYDPDNHLFELHTGTL 118
FosX cd08364
fosfomycin resistant protein subfamily FosX; This subfamily family contains FosX, a fosfomycin ...
 3-128 2.58e-23

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: 88.10  E-value: 2.58e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   3 RGINHICFSVSNLENSIMFYEKVLEG-ELLVKGRKL------AYFNICGVWIALNE-ETHIPRneihqSYTHIAFSVEKE 74
Cdd:cd08364    2 EGISHITFIVKDLDRTAAFLTEIFGAeEVYDSGAETfslspeKFFLIGGLWIAIMEgEPLLER-----SYNHIAFKVSEG 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446866507  75 DFKCLIQRLEENDVHILQGRERDVRDCESIYFVDPDGHKFEFHSGTLQDRLNYY 128
Cdd:cd08364   77 DLDEYRARIKKLGLEIRPPRSRVQGEGRSLYFYDFDNHLFELHTGTLEERLARY 130
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 3-117 9.54e-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: 81.19  E-value: 9.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   3 RGINHICFSVSNLENSIMFYEKVLEGELLVK------GRKLAYFNIC-GVWIALNEETHIPRNEIHQSYTHIAFSVEkeD 75
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRtdfgdgGFGHAFLRLGdGTELELFEAPGAAPAPGGGGLHHLAFRVD--D 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446866507  76 FKCLIQRLEENDVHILQGRERDVRDCESIYFVDPDGHKFEFH 117
Cdd:COG0346   79 LDAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELV 120
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
2-116 3.15e-17

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 72.68  E-value: 3.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   2 LRGINHICFSVSNLENSIMFYEKVLEGELLVKGRKLAYFNICG--VWIALNEETHIPRNEIHQSYTHIAFSVE-KEDFKC 78
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGgeHLLVLEEAPGAPPRPGAAGLDHVAFRVPsRADLDA 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446866507  79 LIQRLEENDVHILQGRERDVRdcESIYFVDPDGHKFEF 116
Cdd:COG2514   81 ALARLAAAGVPVEGAVDHGVG--ESLYFRDPDGNLIEL 116
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 7-116 1.88e-14

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: 64.85  E-value: 1.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   7 HICFSVSNLENSIMFYEKVLEGELL--VKGRKLAYFNIC-GVWIALNEETHiPRNEIHQSYTHIAFSVEKEDFKCLIQRL 83
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVsrNEGGGFAFLRLGpGLRLALLEGPE-PERPGGGGLFHLAFEVDDVDEVDERLRE 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446866507  84 EENDVHILQGRERDVRDCESIYFVDPDGHKFEF 116
Cdd:cd06587   80 AGAEGELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
4-116 1.04e-13

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 62.85  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507    4 GINHICFSVSNLENSIMFYEKVLEGELLVK-------GRKLAYFNICGVWIALNEETHIPRNEIHQSYTHIAFSV-EKED 75
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEEtdageegGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAfSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 446866507   76 FKCLIQRLEENDVHILQGRERDVRDCESIYFVDPDGHKFEF 116
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-116 1.96e-07

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


Pssm-ID: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 46.54  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   5 INHICFSVSNLENSIMFYEKVLEGELLVK----GRKLAYFNICGVW----IALNEETHIPRNEIHQSYTHIAFSVekEDF 76
Cdd:cd07245    1 LDHVALACPDLERARRFYTDVLGLEEVPRppflKFGGAWLYLGGGQqihlVVEQNPSELPRPEHPGRDRHPSFSV--PDL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446866507  77 KCLIQRLEENDVHILQgRERDVRDCESIYFVDPDGHKFEF 116
Cdd:cd07245   79 DALKQRLKEAGIPYTE-STSPGGGVTQLFFRDPDGNRLEF 117
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-118 2.60e-07

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 46.17  E-value: 2.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   1 MLRGINHICFSVSNLENSIMFYEKVLEGELLVK---GRKLAYFNI-CGVWIALNEETHIPRNeihqSYTHIAFSVEkeDF 76
Cdd:COG3324    1 MPGTIVWVELPVDDLERAKAFYEEVFGWTFEDDagpGGDYAEFDTdGGQVGGLMPGAEEPGG----PGWLLYFAVD--DL 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446866507  77 KCLIQRLEENDVHILQGRERDVRDCESIYFVDPDGHKFEFHS 118
Cdd:COG3324   75 DAAVARVEAAGGTVLRPPTDIPPWGRFAVFRDPEGNRFGLWQ 116
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 9-119 4.41e-07

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


Pssm-ID: 319942  Cd Length: 122  Bit Score: 45.82  E-value: 4.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   9 CFSVSNLENSIMFYEKVLEGELLVKGRKLAYFNiCG---VWIALNEET-------HIPRNEIHQSyTHIAFSVEKEDFKC 78
Cdd:cd08354    5 CLYADDLDAAEAFYEDVLGLKPMLRSGRHAFFR-LGpqvLLVFDPGATskdvrtgEVPGHGASGH-GHFAFAVPTEELAA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446866507  79 LIQRLEENDVHIlQGRERDVRDCESIYFVDPDGHKFEFHSG 119
Cdd:cd08354   83 WEARLEAKGVPI-ESYTQWPEGGKSLYFRDPAGNLVELASA 122
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 2-115 1.99e-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: 41.06  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   2 LRGINHICFSVSNLENSIMFYEKVL--EGELLVKGRKLAYFNIcgVWIALNEETH--IPRNEIHQSYT-HIAFSVEKeDF 76
Cdd:cd07253    1 IKRLDHLVLTVKDIERTIDFYTKVLgmTVVTFKEGRKALRFGN--QKINLHQKGKefEPKASAPTPGSaDLCFITET-PI 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446866507  77 KCLIQRLEENDVHILQG---RERDVRDCESIYFVDPDGHKFE 115
Cdd:cd07253   78 DEVLEHLEACGVTIEEGpvkRTGALGPILSIYFRDPDGNLIE 119
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 4-116 2.71e-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: 40.76  E-value: 2.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   4 GINHICFSVSNLENSIMFYEKVLEGELLVKGRKLAYFNICG--VWIALNEETHIPRNEihQSYT---HIAFSV-EKEDFK 77
Cdd:cd07255    2 RIGRVTLKVADLERQSAFYQNVIGLSVLKQNASRAYLGVDGkqVLLVLEAIPDAVLAP--RSTTglyHFAILLpDRKALG 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446866507  78 CLIQRLEENdvHILQGrERDVRDCESIYFVDPDGHKFEF 116
Cdd:cd07255   80 RALAHLAEH--GPLIG-AADHGVSEAIYLSDPEGNGIEI 115
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 12-118 3.52e-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: 3.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507  12 VSNLENSIMFYEKVL---EGELLVKGRkLAYFNICGVWIALN---EETHIPRNEIHQSYTHIAFSVEkeDFKCLIQRLEE 85
Cdd:cd07264    8 VDDFAASLRFYRDVLglpPRFLHEEGE-YAEFDTGETKLALFsrkEMARSGGPDRRGSAFELGFEVD--DVEATVEELVE 84

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446866507  86 NDVHILQGRERDVRDCESIYFVDPDGHKFEFHS 118
Cdd:cd07264   85 RGAEFVREPANKPWGQTVAYVRDPDGNLIEICE 117
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-116 1.05e-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: 39.37  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   7 HICFSVSNLENSIMFYEKVLEGELLVKGRKLAYFNI--CGVWIALNEETHIPRNEIHqsytHIAFSVE-KEDFKCLIQRL 83
Cdd:cd07254    4 HLSLNVTDLERSIRFYSDLFGAEPAKRKADYAKFMLedPPLNLALLVNDRKEPYGLN----HLGIQVDsKEEVAALKARA 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446866507  84 EENDVHILQgrERDVRDC----ESIYFVDPDGHKFEF 116
Cdd:cd07254   80 EAAGLPVRK--EPRTTCCyavqDKFWLTDPDGNAWEF 114
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 7-116 4.81e-04

Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other prokaryotic glyoxalase I that uses nickel 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: 319965 [Multi-domain]  Cd Length: 122  Bit Score: 37.38  E-value: 4.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   7 HICFSVSNLENSIMFYEKVLEGELLvkgRKLAY----FNICGVWI------ALNEETH---IPRNEIHQSYTHIAFSVEk 73
Cdd:cd16358    3 HTMLRVGDLDRSIKFYTEVLGMKLL---RKRDYpegkYTLAFVGYgdedenTVLELTYnwgVDKYDLGTAYGHIAIGVE- 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446866507  74 eDFKCLIQRLEENDVHILqgRERD-VRDCESI--YFVDPDGHKFEF 116
Cdd:cd16358   79 -DVYETCERIRKKGGKVT--REPGpMKGGTTViaFVEDPDGYKIEL 121
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 5-109 3.54e-03

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: 35.24  E-value: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   5 INHICFSVSNLENSIMFYEKVL-----EGELLVK-GRKLAYFNICGVWI----ALNEETHI------PRNEIHqsytHIA 68
Cdd:cd07249    1 LDHIGIAVPDLDEALKFYEDVLgvkvsEPEELEEqGVRVAFLELGNTQIellePLGEDSPIakfldkKGGGLH----HIA 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446866507  69 FSVekEDFKCLIQRLEENDVHILQGRERDVRDCESIYFVDP 109
Cdd:cd07249   77 FEV--DDIDAAVEELKAQGVRLLSEGPRIGAHGKRVAFLHP 115
Glyoxalase_2 pfam12681
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 12-115 8.91e-03

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


Pssm-ID: 403776  Cd Length: 118  Bit Score: 33.92  E-value: 8.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446866507   12 VSNLENSIMFYEKVLEGELLVK-GRKLAYFNICGVWIALNEETHIPRNEIHQSyTHIAFSVEKEDFKCLIQRLEEND-VH 89
Cdd:pfam12681   8 VKDINISRKFYEDVLDQKIKLDfGENVSFEGGFAIQSDFKELIGIDLSIAEQS-NNFELYFEVADVDAFLQKIKEIGnIE 86

                          90       100
                  ....*....|....*....|....*.
gi 446866507   90 ILQGRERDVRDCESIYFVDPDGHKFE 115
Cdd:pfam12681  87 YLHELKEQPWGQRVFRFYDPDGHIIE 112
 
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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