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Conserved domains on  [gi|2127664848|gb|UEA90783|]
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VOC family protein [Parabacteroides johnsonii]

Protein Classification

VOC family protein( domain architecture ID 10001243)

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
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-122 1.19e-22

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: 85.81  E-value: 1.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848   6 RFDHFNINVLDLDRSIAFYGKALGLKEHHRKEAADGSFILVYLTDNEtGFLLELTWlRDRKEAYELGDNESHLCFRVAgD 85
Cdd:COG0346     2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGD-GTELELFE-APGAAPAPGGGGLHHLAFRVD-D 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2127664848  86 YDEIREYHRELGYICFE---NNEMGLY--FINDPDDYWIEIL 122
Cdd:COG0346    79 LDAAYARLRAAGVEIEGeprDRAYGYRsaYFRDPDGNLIELV 120
 
Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-122 1.19e-22

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: 85.81  E-value: 1.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848   6 RFDHFNINVLDLDRSIAFYGKALGLKEHHRKEAADGSFILVYLTDNEtGFLLELTWlRDRKEAYELGDNESHLCFRVAgD 85
Cdd:COG0346     2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGD-GTELELFE-APGAAPAPGGGGLHHLAFRVD-D 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2127664848  86 YDEIREYHRELGYICFE---NNEMGLY--FINDPDDYWIEIL 122
Cdd:COG0346    79 LDAAYARLRAAGVEIEGeprDRAYGYRsaYFRDPDGNLIELV 120
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 7-122 1.57e-20

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


Pssm-ID: 319900 [Multi-domain]  Cd Length: 142  Bit Score: 80.83  E-value: 1.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848   7 FDHFNINVLDLDRSIAFYGKALGLKEHHRKEAADGSFILVYLTDNETGFL---------------LELTW----LRDRKE 67
Cdd:cd07233     1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDPKDIpkdprtawvfsregtLELTHnwgtENDEDP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127664848  68 AYELGDNES----HLCFRVAgDYDEIREYHRELGYICF----ENNEMGLYFINDPDDYWIEIL 122
Cdd:cd07233    81 VYHNGNSDPrgfgHIGIAVD-DVYAACERFEELGVKFKkkpdDGKMKGIAFIKDPDGYWIEIL 142
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 4-126 4.89e-13

lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and glyoxalase I. Glyoxylase I is a homodimer in many species. In some eukaryotes, including yeasts and plants, the orthologous protein carries a tandem duplication, is twice as long, and hits this model twice. [Central intermediary metabolism, Amino sugars, Energy metabolism, Other]


Pssm-ID: 272886  Cd Length: 150  Bit Score: 61.75  E-value: 4.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848   4 KSRFDHFNINVLDLDRSIAFYGKALGLKEHHRKEAADGSFILVYL--TDNETGFLLELT--WlrdRKEAYELGDNESHLC 79
Cdd:TIGR00068  15 KRRLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLgyGDETSAAVIELThnW---GTEKYDLGNGFGHIA 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2127664848  80 FRVAGDYDEIREYHRELGYICFENNEM-----GLYFINDPDDYWIEILPAKQ 126
Cdd:TIGR00068  92 IGVDDVYKACERVRALGGNVVREPGPVkggttVIAFVEDPDGYKIELIQRKS 143
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
6-121 9.14e-10

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 52.45  E-value: 9.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848   6 RFDHFNINVLDLDRSIAFYGKALGLKEHHRKEA-ADGSFILVYLTDNETGFLLELTWLRDRKEAYELGDNESHLCFRVA- 83
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAgEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSVDd 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2127664848  84 --GDYDEIR----EYHRELGYICFENnemGLYFINDPDDYWIEI 121
Cdd:pfam00903  81 vdAAYDRLKaagvEIVREPGRHGWGG---RYSYFRDPDGNLIEL 121
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 14-125 1.26e-04

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 39.80  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848  14 VLDLDRSIAFYGKALGLKEHHRKEAADGSFILVYL--TDNET--GFLLELT-WLRDRKEAYELGDN---ES--------- 76
Cdd:PLN03042   35 IKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLgyEDSETapTDPPERTvWTFGRKATIELTHNwgtESdpefkgyhn 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127664848  77 ---------HLCFRVAGDYDEIREYHrELGyICF----ENNEM-GLYFINDPDDYWIEILPAK 125
Cdd:PLN03042  115 gnsdprgfgHIGITVDDVYKACERFE-KLG-VEFvkkpDDGKMkGLAFIKDPDGYWIEIFDLK 175
 
Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-122 1.19e-22

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: 85.81  E-value: 1.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848   6 RFDHFNINVLDLDRSIAFYGKALGLKEHHRKEAADGSFILVYLTDNEtGFLLELTWlRDRKEAYELGDNESHLCFRVAgD 85
Cdd:COG0346     2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGD-GTELELFE-APGAAPAPGGGGLHHLAFRVD-D 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2127664848  86 YDEIREYHRELGYICFE---NNEMGLY--FINDPDDYWIEIL 122
Cdd:COG0346    79 LDAAYARLRAAGVEIEGeprDRAYGYRsaYFRDPDGNLIELV 120
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 7-122 1.57e-20

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


Pssm-ID: 319900 [Multi-domain]  Cd Length: 142  Bit Score: 80.83  E-value: 1.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848   7 FDHFNINVLDLDRSIAFYGKALGLKEHHRKEAADGSFILVYLTDNETGFL---------------LELTW----LRDRKE 67
Cdd:cd07233     1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDPKDIpkdprtawvfsregtLELTHnwgtENDEDP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127664848  68 AYELGDNES----HLCFRVAgDYDEIREYHRELGYICF----ENNEMGLYFINDPDDYWIEIL 122
Cdd:cd07233    81 VYHNGNSDPrgfgHIGIAVD-DVYAACERFEELGVKFKkkpdDGKMKGIAFIKDPDGYWIEIL 142
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 4-126 4.89e-13

lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and glyoxalase I. Glyoxylase I is a homodimer in many species. In some eukaryotes, including yeasts and plants, the orthologous protein carries a tandem duplication, is twice as long, and hits this model twice. [Central intermediary metabolism, Amino sugars, Energy metabolism, Other]


Pssm-ID: 272886  Cd Length: 150  Bit Score: 61.75  E-value: 4.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848   4 KSRFDHFNINVLDLDRSIAFYGKALGLKEHHRKEAADGSFILVYL--TDNETGFLLELT--WlrdRKEAYELGDNESHLC 79
Cdd:TIGR00068  15 KRRLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLgyGDETSAAVIELThnW---GTEKYDLGNGFGHIA 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2127664848  80 FRVAGDYDEIREYHRELGYICFENNEM-----GLYFINDPDDYWIEILPAKQ 126
Cdd:TIGR00068  92 IGVDDVYKACERVRALGGNVVREPGPVkggttVIAFVEDPDGYKIELIQRKS 143
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 9-122 2.25e-11

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: 56.64  E-value: 2.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848   9 HFNINVLDLDRSIAFYGKALGLKEHHRKEAADGSFILVYL--TDNETGFLLELTWLRDRkEAYELGDNESHLCFRVAGDY 86
Cdd:cd16358     3 HTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVgyGDEDENTVLELTYNWGV-DKYDLGTAYGHIAIGVEDVY 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2127664848  87 DEIREYHRELGYICFENNEMG-----LYFINDPDDYWIEIL 122
Cdd:cd16358    82 ETCERIRKKGGKVTREPGPMKggttvIAFVEDPDGYKIELI 122
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
6-121 9.14e-10

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 52.45  E-value: 9.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848   6 RFDHFNINVLDLDRSIAFYGKALGLKEHHRKEA-ADGSFILVYLTDNETGFLLELTWLRDRKEAYELGDNESHLCFRVA- 83
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAgEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSVDd 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2127664848  84 --GDYDEIR----EYHRELGYICFENnemGLYFINDPDDYWIEI 121
Cdd:pfam00903  81 vdAAYDRLKaagvEIVREPGRHGWGG---RYSYFRDPDGNLIEL 121
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
6-121 2.82e-09

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 51.50  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848   6 RFDHFNINVLDLDRSIAFYGKALGLKEHHRKEAadgsfiLVYLTDNETGFLLELtWLRDRKEAYELGDNESHLCFRVA-- 83
Cdd:COG2514     3 RLGHVTLRVRDLERSAAFYTDVLGLEVVEREGG------RVYLRADGGEHLLVL-EEAPGAPPRPGAAGLDHVAFRVPsr 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2127664848  84 GDYDEIREYHRELGYICFENNEMG----LYFiNDPDDYWIEI 121
Cdd:COG2514    76 ADLDAALARLAAAGVPVEGAVDHGvgesLYF-RDPDGNLIEL 116
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 9-121 1.90e-07

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: 46.36  E-value: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848   9 HFNINVLDLDRSIAFYGKALGLKEhhRKEAADGSFILVYLTDNETgflLELTWLRDRKEAYELGDNesHLCFRVAGDYDE 88
Cdd:cd06587     1 HVALRVPDLDASVAFYEEVLGFEV--VSRNEGGGFAFLRLGPGLR---LALLEGPEPERPGGGGLF--HLAFEVDDVDEV 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2127664848  89 IREYHR-------ELGYICFENNEMGLYFInDPDDYWIEI 121
Cdd:cd06587    74 DERLREagaegelVAPPVDDPWGGRSFYFR-DPDGNLIEF 112
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-121 3.20e-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: 45.77  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848   7 FDHFNINVLDLDRSIAFYGKALGLKEHHRKEAADgsFILVYLtDNETGF---LLELTWlRDRKEAYELGDNESHLCFRVA 83
Cdd:cd07245     1 LDHVALACPDLERARRFYTDVLGLEEVPRPPFLK--FGGAWL-YLGGGQqihLVVEQN-PSELPRPEHPGRDRHPSFSVP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2127664848  84 gDYDEIREYHRELGYICFENNEMGLY----FINDPDDYWIEI 121
Cdd:cd07245    77 -DLDALKQRLKEAGIPYTESTSPGGGvtqlFFRDPDGNRLEF 117
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 6-122 3.44e-07

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 45.78  E-value: 3.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848   6 RFDHFNINVLDLDRSIAFYGKALGLKEHHRkEAADGSFILVYLTDNETGFLLeltwlrdrKEAYELGDNESHLCFRVAgD 85
Cdd:COG3324     4 TIVWVELPVDDLERAKAFYEEVFGWTFEDD-AGPGGDYAEFDTDGGQVGGLM--------PGAEEPGGPGWLLYFAVD-D 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2127664848  86 YDEIREYHRELGYIC----FENNEMGLYF-INDPDDYWIEIL 122
Cdd:COG3324    74 LDAAVARVEAAGGTVlrppTDIPPWGRFAvFRDPEGNRFGLW 115
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 7-129 1.10e-06

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: 44.20  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848   7 FDHFNINVLDLDRSIAFYGKALGLKEHHR--KEAadgsfilvYLTDNETGFLLELTWLRDRKEAYelgdneSHLCFRV-A 83
Cdd:cd07244     2 INHITLAVSDLERSLAFYVDLLGFKPHVRwdKGA--------YLTAGDLWLCLSLDPAAEPSPDY------THIAFTVsE 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2127664848  84 GDYDEIREYHRELGYICFENNEMG---LYFInDPDDYWIEIlpakqHIG 129
Cdd:cd07244    68 EDFEELSERLRAAGVKIWQENSSEgdsLYFL-DPDGHKLEL-----HVG 110
Glyoxalase_6 pfam18029
Glyoxalase-like domain; This entry comprises a diverse set of domains related to the ...
 9-97 8.16e-05

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: 39.29  E-value: 8.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848   9 HFNINVLDLDRSIAFYGKALGLKEHHRKEAADGSFILVYLTDNETGFLLEltwlrdRKEAYELGDNESHLCFRVAgDYDE 88
Cdd:pfam18029   1 AVVLDCADPAALAAFWSAALGWEVVPDDTALPDPDGGGPIGGGGPRLLFQ------RVPEPKPGKNRVHLDLAVD-DLEA 73


                  ....*....
gi 2127664848  89 IREYHRELG 97
Cdd:pfam18029  74 AVARLVALG 82
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 14-125 1.26e-04

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 39.80  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848  14 VLDLDRSIAFYGKALGLKEHHRKEAADGSFILVYL--TDNET--GFLLELT-WLRDRKEAYELGDN---ES--------- 76
Cdd:PLN03042   35 IKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLgyEDSETapTDPPERTvWTFGRKATIELTHNwgtESdpefkgyhn 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127664848  77 ---------HLCFRVAGDYDEIREYHrELGyICF----ENNEM-GLYFINDPDDYWIEILPAK 125
Cdd:PLN03042  115 gnsdprgfgHIGITVDDVYKACERFE-KLG-VEFvkkpDDGKMkGLAFIKDPDGYWIEIFDLK 175
PRK10291 PRK10291
glyoxalase I; Provisional
 12-125 1.65e-04

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 38.85  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848  12 INVLDLDRSIAFYGKALGLKEHHRKEAADGSFILVYL---TDNETGfLLELTWlRDRKEAYELGDNESHLCFRV---AGD 85
Cdd:PRK10291    2 LRVGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVgygPETEEA-VIELTY-NWGVDKYELGTAYGHIALSVdnaAEA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2127664848  86 YDEIRE----YHRELGYIcfENNEMGLYFINDPDDYWIEILPAK 125
Cdd:PRK10291   80 CEKIRQnggnVTREAGPV--KGGTTVIAFVEDPDGYKIELIEEK 121
PLN02300 PLN02300
lactoylglutathione lyase
 4-122 1.74e-04

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 39.76  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848   4 KSRFDHFNINVLDLDRSIAFYGKALGLKEHHRKEAADGSFILVYL--TDNETGFLLELTWlRDRKEAYELGDNESHLCFR 81
Cdd:PLN02300   22 KRRMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLgyGPEDSNFVVELTY-NYGVDKYDIGTGFGHFGIA 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2127664848  82 ---VAGDYDEIRE----YHRELGYIcfENNEMGLYFINDPDDYWIEIL 122
Cdd:PLN02300  101 vedVAKTVELVKAkggkVTREPGPV--KGGKSVIAFVKDPDGYKFELI 146
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 16-124 2.08e-04

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


Pssm-ID: 319942  Cd Length: 122  Bit Score: 38.12  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848  16 DLDRSIAFYGKALGLKEHHRKE-----AADGSFILVyltdnetgFLLELTWLRDRKEAY--ELGDNESHLCFRVagDYDE 88
Cdd:cd08354    10 DLDAAEAFYEDVLGLKPMLRSGrhaffRLGPQVLLV--------FDPGATSKDVRTGEVpgHGASGHGHFAFAV--PTEE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2127664848  89 IREYHREL--------GYICFENNEMGLYFiNDPDDYWIEILPA 124
Cdd:cd08354    80 LAAWEARLeakgvpieSYTQWPEGGKSLYF-RDPAGNLVELASA 122
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
8-100 5.36e-04

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 36.87  E-value: 5.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848   8 DHFNINVLDLDRSIAFYGKALGLKEHHRKEAADGSFILVYLTDNETGFLLEL-------TWLRDRKEAYelgdneSHLCF 80
Cdd:pfam13669   1 HHVGIAVPDLDRALALWGALLGLGPEGDYRSEPQNVDLAFALLGDGPVEVELiqpldgdSPLARHGPGL------HHLAY 74

                          90       100
                  ....*....|....*....|
gi 2127664848  81 RVAgDYDEIREYHRELGYIC 100
Cdd:pfam13669  75 WVD-DLDAAVARLLDQGYRV 93
PLN02300 PLN02300
lactoylglutathione lyase
 14-73 9.72e-04

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 37.45  E-value: 9.72e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2127664848  14 VLDLDRSIAFYGKALGLKEHHRKEAADGSFILVYL--TDNETGFLLELTWLRDRKEaYELGD 73
Cdd:PLN02300  162 VGDLDRSIKFYEKAFGMKLLRKRDNPEYKYTIAMMgyGPEDKTTVLELTYNYGVTE-YTKGN 222
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 8-98 4.11e-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: 34.86  E-value: 4.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848   8 DHFNINVLDLDRSIAFYGKALGLKEHHRKEAADGSFILVYLTDNETgfLLEL-----------TWLRDRKEayelGDNes 76
Cdd:cd07249     2 DHIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELGNT--QIELleplgedspiaKFLDKKGG----GLH-- 73

                          90       100
                  ....*....|....*....|..
gi 2127664848  77 HLCFRVaGDYDEIREYHRELGY 98
Cdd:cd07249    74 HIAFEV-DDIDAAVEELKAQGV 94
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 12-121 4.62e-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: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 34.61  E-value: 4.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127664848  12 INVLDLDRSIAFYGKALGLKehHRKEAADGSFILVylTDNETGflLELTWLRDRKEAYELGDNESH--LCFRVAgDYDEI 89
Cdd:cd07264     6 LYVDDFAASLRFYRDVLGLP--PRFLHEEGEYAEF--DTGETK--LALFSRKEMARSGGPDRRGSAfeLGFEVD-DVEAT 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2127664848  90 REYHRELGYICFE---NNEMGL--YFINDPDDYWIEI 121
Cdd:cd07264    79 VEELVERGAEFVRepaNKPWGQtvAYVRDPDGNLIEI 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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