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Conserved domains on  [gi|493989954|ref|WP_006932701|]
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VOC family protein [Roseibium aggregatum]

Protein Classification

VOC family protein( domain architecture ID 50733)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VOC super family cl14632
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 6-127 2.37e-30

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


The actual alignment was detected with superfamily member TIGR00068:

Pssm-ID: 472697  Cd Length: 150  Bit Score: 106.43  E-value: 2.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954    6 HSMIRVLDEHRSLSFYEKAFGLTVADRLDFPD--FTLIYLS--NSETGFELELTVNKGrTEPYDLGDGYGHLAFSVDDLD 81
Cdd:TIGR00068  20 HTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEmkFSLAFLGygDETSAAVIELTHNWG-TEKYDLGNGFGHIAIGVDDVY 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 493989954   82 SEHARFEAAGLN-PRKLVDFAPGGDVIArffFVADPDGYQIEVLQRG 127
Cdd:TIGR00068  99 KACERVRALGGNvVREPGPVKGGTTVIA---FVEDPDGYKIELIQRK 142
 
Name Accession Description Interval E-value
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 6-127 2.37e-30

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: 106.43  E-value: 2.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954    6 HSMIRVLDEHRSLSFYEKAFGLTVADRLDFPD--FTLIYLS--NSETGFELELTVNKGrTEPYDLGDGYGHLAFSVDDLD 81
Cdd:TIGR00068  20 HTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEmkFSLAFLGygDETSAAVIELTHNWG-TEKYDLGNGFGHIAIGVDDVY 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 493989954   82 SEHARFEAAGLN-PRKLVDFAPGGDVIArffFVADPDGYQIEVLQRG 127
Cdd:TIGR00068  99 KACERVRALGGNvVREPGPVKGGTTVIA---FVEDPDGYKIELIQRK 142
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-128 1.46e-27

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: 98.53  E-value: 1.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   6 HSMIRVLDEHRSLSFYEKAFGLTVADRLDFPD--FTLIYLSNSEtGFELELTVNKGrTEPYDLGDGYGHLAFSVDDLDSE 83
Cdd:COG0346    5 HVTLRVSDLEASLAFYTDVLGLELVKRTDFGDggFGHAFLRLGD-GTELELFEAPG-AAPAPGGGGLHHLAFRVDDLDAA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 493989954  84 HARFEAAGLNPRKLVDFAPGGdviARFFFVADPDGYQIEVLQRGG 128
Cdd:COG0346   83 YARLRAAGVEIEGEPRDRAYG---YRSAYFRDPDGNLIELVEPPP 124
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 5-124 3.98e-24

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: 89.38  E-value: 3.98e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   5 IHSMIRVLDEHRSLSFYEKAFGLTVADRLDFPD--FTLIYL--SNSETGFELELTVNKGRTEpYDLGDGYGHLAFSVDDL 80
Cdd:cd16358    2 LHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEgkYTLAFVgyGDEDENTVLELTYNWGVDK-YDLGTAYGHIAIGVEDV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 493989954  81 DSEHARFEAAGLNPRKLVDFAPGGD-VIArffFVADPDGYQIEVL 124
Cdd:cd16358   81 YETCERIRKKGGKVTREPGPMKGGTtVIA---FVEDPDGYKIELI 122
PLN02300 PLN02300
lactoylglutathione lyase
 5-131 8.15e-17

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 74.05  E-value: 8.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   5 IHSMIRVLDEHRSLSFYEKAFGLTVADRLDFPD--FTLIYLS--NSETGFELELTVNKGrTEPYDLGDGYGHLAFSVDDL 80
Cdd:PLN02300  26 LHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEekYTNAFLGygPEDSNFVVELTYNYG-VDKYDIGTGFGHFGIAVEDV 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493989954  81 DSEHARFEAAGLN-PRKLVDFAPGGDVIArffFVADPDGYQIEVLQRGGRYE 131
Cdd:PLN02300 105 AKTVELVKAKGGKvTREPGPVKGGKSVIA---FVKDPDGYKFELIQRGPTPE 153
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
6-123 1.91e-15

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 67.09  E-value: 1.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954    6 HSMIRVLDEHRSLSFYEKAFGLTVADRLDFPDF---TLIYLSNSETGFELELTVNKGRTEPYDLGDGYGHLAFSVDDLDS 82
Cdd:pfam00903   4 HVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEgglRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSVDDVDA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 493989954   83 EHARFEAAGLNPRKLVDFAPGGdviARFFFVADPDGYQIEV 123
Cdd:pfam00903  84 AYDRLKAAGVEIVREPGRHGWG---GRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 6-127 2.37e-30

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: 106.43  E-value: 2.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954    6 HSMIRVLDEHRSLSFYEKAFGLTVADRLDFPD--FTLIYLS--NSETGFELELTVNKGrTEPYDLGDGYGHLAFSVDDLD 81
Cdd:TIGR00068  20 HTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEmkFSLAFLGygDETSAAVIELTHNWG-TEKYDLGNGFGHIAIGVDDVY 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 493989954   82 SEHARFEAAGLN-PRKLVDFAPGGDVIArffFVADPDGYQIEVLQRG 127
Cdd:TIGR00068  99 KACERVRALGGNvVREPGPVKGGTTVIA---FVEDPDGYKIELIQRK 142
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-128 1.46e-27

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: 98.53  E-value: 1.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   6 HSMIRVLDEHRSLSFYEKAFGLTVADRLDFPD--FTLIYLSNSEtGFELELTVNKGrTEPYDLGDGYGHLAFSVDDLDSE 83
Cdd:COG0346    5 HVTLRVSDLEASLAFYTDVLGLELVKRTDFGDggFGHAFLRLGD-GTELELFEAPG-AAPAPGGGGLHHLAFRVDDLDAA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 493989954  84 HARFEAAGLNPRKLVDFAPGGdviARFFFVADPDGYQIEVLQRGG 128
Cdd:COG0346   83 YARLRAAGVEIEGEPRDRAYG---YRSAYFRDPDGNLIELVEPPP 124
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 5-124 3.98e-24

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: 89.38  E-value: 3.98e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   5 IHSMIRVLDEHRSLSFYEKAFGLTVADRLDFPD--FTLIYL--SNSETGFELELTVNKGRTEpYDLGDGYGHLAFSVDDL 80
Cdd:cd16358    2 LHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEgkYTLAFVgyGDEDENTVLELTYNWGVDK-YDLGTAYGHIAIGVEDV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 493989954  81 DSEHARFEAAGLNPRKLVDFAPGGD-VIArffFVADPDGYQIEVL 124
Cdd:cd16358   81 YETCERIRKKGGKVTREPGPMKGGTtVIA---FVEDPDGYKIELI 122
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 6-124 5.60e-24

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: 89.69  E-value: 5.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   6 HSMIRVLDEHRSLSFYEKAFGLTVADRLDFPD--FTLIYLSNSETGFE---------------LELTVNKG----RTEPY 64
Cdd:cd07233    3 HTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEmkFSLYFLGYEDPKDIpkdprtawvfsregtLELTHNWGtendEDPVY 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493989954  65 DLGD----GYGHLAFSVDDLDSEHARFEAAGLNPRKLVDFAPGGDvIArffFVADPDGYQIEVL 124
Cdd:cd07233   83 HNGNsdprGFGHIGIAVDDVYAACERFEELGVKFKKKPDDGKMKG-IA---FIKDPDGYWIEIL 142
PLN02300 PLN02300
lactoylglutathione lyase
 5-131 8.15e-17

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 74.05  E-value: 8.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   5 IHSMIRVLDEHRSLSFYEKAFGLTVADRLDFPD--FTLIYLS--NSETGFELELTVNKGrTEPYDLGDGYGHLAFSVDDL 80
Cdd:PLN02300  26 LHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEekYTNAFLGygPEDSNFVVELTYNYG-VDKYDIGTGFGHFGIAVEDV 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493989954  81 DSEHARFEAAGLN-PRKLVDFAPGGDVIArffFVADPDGYQIEVLQRGGRYE 131
Cdd:PLN02300 105 AKTVELVKAKGGKvTREPGPVKGGKSVIA---FVKDPDGYKFELIQRGPTPE 153
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 6-123 9.09e-16

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


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 67.94  E-value: 9.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   6 HSMIRVLDEHRSLSFYEKAFGLTVADRLDFPDFTLIYLSNsetGFELELTVNKGRTEPYdlGDGYGHLAFSVDDLDSEHA 85
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGFAFLRLGP---GLRLALLEGPEPERPG--GGGLFHLAFEVDDVDEVDE 75

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 493989954  86 RFEAAGLNPRKLVDFAPGGDViARFFFVADPDGYQIEV 123
Cdd:cd06587   76 RLREAGAEGELVAPPVDDPWG-GRSFYFRDPDGNLIEF 112
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
6-123 1.91e-15

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 67.09  E-value: 1.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954    6 HSMIRVLDEHRSLSFYEKAFGLTVADRLDFPDF---TLIYLSNSETGFELELTVNKGRTEPYDLGDGYGHLAFSVDDLDS 82
Cdd:pfam00903   4 HVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEgglRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSVDDVDA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 493989954   83 EHARFEAAGLNPRKLVDFAPGGdviARFFFVADPDGYQIEV 123
Cdd:pfam00903  84 AYDRLKAAGVEIVREPGRHGWG---GRYSYFRDPDGNLIEL 121
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 7-124 3.17e-15

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 68.31  E-value: 3.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   7 SMIRVLDEHRSLSFYEKAFGLTVADRLDFPD--FTLIYLS--NSETGFE---------------LELTVNKG-RTEP--- 63
Cdd:PLN03042  31 TMFRIKDPKASLDFYSRVLGMSLLKRLDFPEmkFSLYFLGyeDSETAPTdppertvwtfgrkatIELTHNWGtESDPefk 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493989954  64 -YDLGD----GYGHLAFSVDDLDSEHARFEAAGlnprklVDFA--PGGDVIARFFFVADPDGYQIEVL 124
Cdd:PLN03042 111 gYHNGNsdprGFGHIGITVDDVYKACERFEKLG------VEFVkkPDDGKMKGLAFIKDPDGYWIEIF 172
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-128 3.99e-15

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 66.20  E-value: 3.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   1 MAKAIHSMIRVLDEHRSLSFYEKAFGLTVADRLDFP-DFTLIylsnsETGFELELTVNKGRTEPydlGDGYGHLAFSVDD 79
Cdd:COG3324    2 PGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPGgDYAEF-----DTDGGQVGGLMPGAEEP---GGPGWLLYFAVDD 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 493989954  80 LDSEHARFEAAGLNP-RKLVDFAPGGdviaRFFFVADPDGYQIEVLQRGG 128
Cdd:COG3324   74 LDAAVARVEAAGGTVlRPPTDIPPWG----RFAVFRDPEGNRFGLWQPAA 119
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 6-123 4.39e-14

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: 63.49  E-value: 4.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   6 HSMIRVLDEHRSLSFYEKAFGLTVADRLDFPDFTLIYLsNSETGFELELTVNKGRTEPYDLGDGY--GHLAFSVDDLDSE 83
Cdd:cd07245    3 HVALACPDLERARRFYTDVLGLEEVPRPPFLKFGGAWL-YLGGGQQIHLVVEQNPSELPRPEHPGrdRHPSFSVPDLDAL 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 493989954  84 HARFEAAGLNPRKLVDFAPGgdvIARFFFvADPDGYQIEV 123
Cdd:cd07245   82 KQRLKEAGIPYTESTSPGGG---VTQLFF-RDPDGNRLEF 117
PLN02367 PLN02367
lactoylglutathione lyase
 6-124 7.50e-14

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 65.41  E-value: 7.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   6 HSMIRVLDEHRSLSFYEKAFGLTVADRLDFPD--FTLIYLSNSETG-----------------FELELTVNKG-RTEP-- 63
Cdd:PLN02367  78 QTMYRIKDPKASLDFYSRVLGMSLLKRLDFPEmkFSLYFMGYEDTAsaptdptertvwtfgqkATIELTHNWGtESDPdf 157

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493989954  64 --YDLGD----GYGHLAFSVDDLDSEHARFEAAGlnprklVDFA--PGGDVIARFFFVADPDGYQIEVL 124
Cdd:PLN02367 158 kgYHNGNseprGFGHIGITVDDVYKACERFEELG------VEFVkkPNDGKMKGIAFIKDPDGYWIEIF 220
PRK10291 PRK10291
glyoxalase I; Provisional
 8-125 2.95e-13

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 61.96  E-value: 2.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   8 MIRVLDEHRSLSFYEKAFGLTVADRLDFPDF--TLIYLSNSETGFE--LELTVNKGrTEPYDLGDGYGHLAFSVDDLDSE 83
Cdd:PRK10291   1 MLRVGDLQRSIDFYTNVLGMKLLRTSENPEYkySLAFVGYGPETEEavIELTYNWG-VDKYELGTAYGHIALSVDNAAEA 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 493989954  84 HARFEAAGLNPRKLVDFAPGGDVIarFFFVADPDGYQIEVLQ 125
Cdd:PRK10291  80 CEKIRQNGGNVTREAGPVKGGTTV--IAFVEDPDGYKIELIE 119
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
6-131 1.59e-11

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 57.66  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   6 HSMIRVLDEHRSLSFYEKAFGLTVADRLDfpdfTLIYLSNSETGFELELTVNKGrTEPYDLGDGYGHLAFSVD---DLDS 82
Cdd:COG2514    6 HVTLRVRDLERSAAFYTDVLGLEVVEREG----GRVYLRADGGEHLLVLEEAPG-APPRPGAAGLDHVAFRVPsraDLDA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 493989954  83 EHARFEAAGLNPRKLVDFAPGgdviaRFFFVADPDGYQIEVLQRGGRYE 131
Cdd:COG2514   81 ALARLAAAGVPVEGAVDHGVG-----ESLYFRDPDGNLIELYTDRPRFE 124
PLN02300 PLN02300
lactoylglutathione lyase
 8-80 1.01e-10

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 57.48  E-value: 1.01e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493989954   8 MIRVLDEHRSLSFYEKAFGLTVADRLDFPD--FTLIYL--SNSETGFELELTVNKGRTEpYDLGDGYGHLAFSVDDL 80
Cdd:PLN02300 159 MLRVGDLDRSIKFYEKAFGMKLLRKRDNPEykYTIAMMgyGPEDKTTVLELTYNYGVTE-YTKGNAYAQIAIGTDDV 234
VOC_like cd08359
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 20-125 1.43e-09

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


Pssm-ID: 319947 [Multi-domain]  Cd Length: 119  Bit Score: 52.02  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954  20 FYEKAFGLTVADRLDFpdftLIYLSNSE-TGFELELTVNKGRTEPYDL-GDGYGH-LAFSVDDLDSEHARFEAAGLNPRK 96
Cdd:cd08359   18 FYVKHFGFRVIFDSDW----YVSLRRAErHGFELAIMDGQHGAVPAASqTQSSGLiINFEVDDADAEYERLTQAGLEFLE 93

                         90       100
                 ....*....|....*....|....*....
gi 493989954  97 LVDFAPGGDviaRFFFVADPDGYQIEVLQ 125
Cdd:cd08359   94 PPRDEPWGQ---RRFIVRDPNGVLIDVIQ 119
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-126 4.68e-09

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


Pssm-ID: 319917 [Multi-domain]  Cd Length: 120  Bit Score: 50.54  E-value: 4.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   3 KAIHSMIRVLDEHRSLSFYEKAFGLTVADRL-DFPDFTLiylsnSETGFELELTVNkGRTEPYdlgdGYGHLAFSVDDLD 81
Cdd:cd07254    1 KRFHLSLNVTDLERSIRFYSDLFGAEPAKRKaDYAKFML-----EDPPLNLALLVN-DRKEPY----GLNHLGIQVDSKE 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493989954  82 SEHA---RFEAAGLNPRKLVD----FAPGGDviarfFFVADPDGYQIEVLQR 126
Cdd:cd07254   71 EVAAlkaRAEAAGLPVRKEPRttccYAVQDK-----FWLTDPDGNAWEFYAT 117
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
4-126 2.45e-08

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 48.70  E-value: 2.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   4 AIHSMIRVLDEHRSLSFYEKAFGLTVADRLDFPDFTLIYlsnsetgfeLELTVNKGR--------TEPYDLGDGYgHLAF 75
Cdd:COG2764    1 SVTPYLVVDDAEEALEFYEDVFGFEVVFRMTDPDGKIMH---------AELRIGGSVlmlsdappDSPAAEGNGV-SLSL 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493989954  76 SVDDLDSEHARFEAAGLNP-RKLVDFAPGgdviARFFFVADPDGYQIEVLQR 126
Cdd:COG2764   71 YVDDVDALFARLVAAGATVvMPLQDTFWG----DRFGMVRDPFGVLWMINTP 118
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-125 1.59e-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: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 46.52  E-value: 1.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   8 MIRVLDEHRSLSFYEKAFGLTVADRLDFPDFTLIYLSNSE-TGFELELTVNK---GRTEPYDLGDGYGHLAFSVDDLDSE 83
Cdd:cd07263    3 MLYVDDQDKALDFYVEKLGFEVVEDVPMGGMRWVTVAPPGsPGTSLLLEPKAhpaQMPQSPEAAGGTPGILLATDDIDAT 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 493989954  84 HARFEAAGLNPRKLVDFAPGGdviaRFFFVADPDGYQIEVLQ 125
Cdd:cd07263   83 YERLTAAGVTFVQEPTQMGGG----RVANFRDPDGNLFALME 120
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 10-119 6.16e-07

Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance protein, confers Bm resistance by directly binding to Bm. Bm is a glycopeptide antibiotic produced naturally by actinomycetes. It is a potent anti-cancer drug, which acts as a strong DNA-cutting agent, thereby causing cell death. BLMA is produced by actinomycetes to protect themselves against their own lethal compound. BLMA has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMAs are dimers and each dimer binds to two Bm molecules at the Bm-binding pockets formed at the dimer interface; two Bm molecules are bound per dimer. BLMA belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. As for the larger superfamily, this family contains members with or without domain swapping.


Pssm-ID: 319937 [Multi-domain]  Cd Length: 114  Bit Score: 44.91  E-value: 6.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954  10 RVLDEHRSLSFYEKAFGLTVADRLDFPDFTLIYLSnsetGFELELTvnkgRTEPYDLGDGYGHLAFSVDDLDSEHARFEA 89
Cdd:cd08349    5 PVRDIDKTLAFYVDVLGFEVDYERPPPGYAILSRG----GVELHLF----EHPGLDPAGSGVAAYIRVEDIDALHAELKA 76

                         90       100       110
                 ....*....|....*....|....*....|..
gi 493989954  90 AGLNPRKLVDFAPGGDV--IARFFFVADPDGY 119
Cdd:cd08349   77 AGLPLFGIPRITPIEDKpwGMREFAVVDPDGN 108
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 6-123 1.33e-05

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: 41.38  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   6 HSMIRVLDEHRSLSFYEKAFGLTVADRLDFPDFTLIYLSNSETGFELELTVNKG--RTEPYDLGDGYGHLAFSVDDLDSE 83
Cdd:cd08352    5 HIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDIKLDLALGGYQLELFIKPDapARPSYPEALGLRHLAFKVEDVEAT 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 493989954  84 HARFEAAGL--NPRKLVDFAPggdviARFFFVADPDGYQIEV 123
Cdd:cd08352   85 VAELKSLGIetEPIRVDDFTG-----KKFTFFFDPDGLPLEL 121
VOC_like cd07238
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 9-124 4.37e-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: 319903  Cd Length: 112  Bit Score: 40.15  E-value: 4.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   9 IRVLDEHRSLSFYEKAFGLTVADRLDFpdfTLIYLSNSETGFELELtVNKGRTEPyDLGDgyghLAFSVDDLDSEHARFE 88
Cdd:cd07238    6 IATADPERAAAFYGDHLGLPLVMDHGW---IVTFASPGNAHAQISL-AREGGSGT-VVPD----LSIEVDDVDAVHARVV 76

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 493989954  89 AAGLN-PRKLVDFAPGgdviARFFFVADPDGYQIEVL 124
Cdd:cd07238   77 AAGLRiEYGPTTEAWG----VRRFFVRDPFGRLINIL 109
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 13-125 1.04e-04

N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth disturbances caused by high osmolarity and a high concentration of A-factor, a microbial hormone, during the early growth phase in Streptomyces griseus. A-factor (2-isocapryloyl-3R-hydroxymethyl-gamma-butyrolactone) controls morphological differentiation and secondary metabolism in Streptomyces griseus. It is a chemical signaling molecule that at a very low concentration acts as a switch for yellow pigment production, aerial mycelium formation, streptomycin production, and streptomycin resistance. The structure and amino acid sequence of SgaA are closely related to a group of antibiotics resistance proteins, including bleomycin resistance protein, mitomycin resistance protein, and fosfomycin resistance proteins. SgaA might also function as a streptomycin resistance protein.


Pssm-ID: 319911 [Multi-domain]  Cd Length: 114  Bit Score: 39.17  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954  13 DEHRSLSFYEKAFGLTVADR-LDFPDFTLIYLSNSETGfeleltvnkG---RTEPYDLGDGYGHLAFSVDDLDSEHARFE 88
Cdd:cd07247   10 DLERAKAFYGAVFGWTFEDEgDGGGDYALFTAGGGAVG---------GlmrAPEEVAGAPPGWLIYFAVDDLDAALARVE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 493989954  89 AAG---LNPRklVDFAPGGdviaRFFFVADPDGYQIEVLQ 125
Cdd:cd07247   81 AAGgkvVVPP--TDIPGGG----RFAVFADPEGNRFGLWS 114
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 6-124 1.09e-04

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


Pssm-ID: 319967  Cd Length: 111  Bit Score: 38.84  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   6 HSMIRVLDEHRSLSFYEKAFGLTVADRldfpDFTLIYLSNSEtgfeleltvnkgrTEPYDL------GDGYGHLAFSV-- 77
Cdd:cd16360    1 YAELGVPDLEKALEFYTDVLGLQVAKR----DGNSVYLRGYE-------------DEHHSLvlyeapEAGLKHFAFEVas 63

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 493989954  78 -DDLDSEHARFEAAGLNPRKLVD-FAPGGdviARFFFVADPDGYQIEVL 124
Cdd:cd16360   64 eEDLERAAASLTALGCDVTWGPDgEVPGG---GKGFRFQDPSGHLLELF 109
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 9-123 1.19e-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: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 38.85  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   9 IRVLDEHRSLSFYEKAFGLTVADRLDFPDFTLiyLSNSETGFELELTVNKGRTEPYDLGDGYGHLAFSVDDLDSEHARFE 88
Cdd:cd07264    6 LYVDDFAASLRFYRDVLGLPPRFLHEEGEYAE--FDTGETKLALFSRKEMARSGGPDRRGSAFELGFEVDDVEATVEELV 83

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 493989954  89 AAGLNPRKLVDFAPGGdviARFFFVADPDGYQIEV 123
Cdd:cd07264   84 ERGAEFVREPANKPWG---QTVAYVRDPDGNLIEI 115
PRK11478 PRK11478
VOC family protein;
69-126 1.32e-04

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 39.11  E-value: 1.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 493989954  69 GYGHLAFSVDDLDSEHARFEAAGLNPRKL-VDFAPGgdviARFFFVADPDGYQIEVLQR 126
Cdd:PRK11478  75 GLRHLAFSVDDIDAAVAHLESHNVKCEAIrVDPYTQ----KRFTFFNDPDGLPLELYEQ 129
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 8-121 1.79e-04

C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. 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: 319964  Cd Length: 114  Bit Score: 38.31  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   8 MIRVLDEHRSLSFYEKAFGLTVADRLDfpdfTLIYLSNSETGFELELtvnKGRTEPYDLGDGYGHLAFSV--DDLDSEHA 85
Cdd:cd16357    3 SLAVSDLEKSIDYWSDLLGMKVFEKSE----KSALLGYGEDQAKLEL---VDIPEPVDHGTAFGRIAFSCpaDELPPIEE 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 493989954  86 RFEAAG---LNPRKLVDfAPGGD----VIarfffVADPDGYQI 121
Cdd:cd16357   76 KVKAAGqtiLTPLVSLD-TPGKAtvqvVI-----LADPDGHEI 112
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
11-91 2.01e-04

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 38.03  E-value: 2.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   11 VLDEHRSLSFYEKAFGLTVADRLDFP--DFTLIYLSNSETGFELELTVNKGRTEPYDL-GDGYGHLAFSVDDLDSEHARF 87
Cdd:pfam13669   7 VPDLDRALALWGALLGLGPEGDYRSEpqNVDLAFALLGDGPVEVELIQPLDGDSPLARhGPGLHHLAYWVDDLDAAVARL 86


                  ....
gi 493989954   88 EAAG 91
Cdd:pfam13669  87 LDQG 90
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 9-125 3.82e-04

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: 37.56  E-value: 3.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   9 IRVLDEHRSLSFYEKAFGLTVADRLDFPDF--TLIYLSNSETgfELEL--------TVNKGRTEPydlGDGYGHLAFSVD 78
Cdd:cd07249    6 IAVPDLDEALKFYEDVLGVKVSEPEELEEQgvRVAFLELGNT--QIELleplgedsPIAKFLDKK---GGGLHHIAFEVD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493989954  79 DLDSEHARFEAAGLN-----PRKLVDfapGGDVIarFFFVADPDGYQIEVLQ 125
Cdd:cd07249   81 DIDAAVEELKAQGVRllsegPRIGAH---GKRVA--FLHPKDTGGVLIELVE 127
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 13-123 3.96e-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: 37.73  E-value: 3.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954  13 DEHRSLSFYEKAFGLTV---ADRLDF----PDFTLIylsnsetgFELELTVNKGRTE--PYDLGDGYGHLAFSV--DDLD 81
Cdd:cd08354   10 DLDAAEAFYEDVLGLKPmlrSGRHAFfrlgPQVLLV--------FDPGATSKDVRTGevPGHGASGHGHFAFAVptEELA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 493989954  82 SEHARFEAAGLNPRKLVDFAPGGDVIarffFVADPDGYQIEV 123
Cdd:cd08354   82 AWEARLEAKGVPIESYTQWPEGGKSL----YFRDPAGNLVEL 119
EhpR_like cd07261
phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter ...
 11-123 5.14e-04

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


Pssm-ID: 319922  Cd Length: 114  Bit Score: 36.99  E-value: 5.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954  11 VLDEHRSLSFYEKAFGLTVADRldFPDFTLIYLSNsetGFELELTVNKGRTEPYDLGDGYGHLAFSV---DDLDSEHARF 87
Cdd:cd07261    6 VDNPERSTEFYRFLLGKEPVES--SPTFASFVLSG---GAKLGLWSSEEVEPKVAVTGGGAELSFMVpsgEQVDEVYAEW 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 493989954  88 EAAGLNPRKlvdfAPGGDVIARFFFVADPDGYQIEV 123
Cdd:cd07261   81 KAMGIPIIQ----EPTTMDFGYTFVATDPDGHRLRV 112
Glyoxalase_3 pfam13468
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 6-117 5.48e-04

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


Pssm-ID: 433233  Cd Length: 175  Bit Score: 37.70  E-value: 5.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954    6 HSMIRVLDEHRSLSFYEKAFGLTVADRLDFPDF----TLIYLSNSEtgFELELTVNKGRTEP---------YDLGDGYGH 72
Cdd:pfam13468   3 HVVLAVPDLDEAAARFARALGFTVTPGGRHPGMgtanALIMFGDGY--LELLAVDPEAPAPPrgrwfgldrLADGEGLLG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 493989954   73 LAFSVDDLDSEHARFEAAGLNPRKLVDFaPGGDVIARFFFVADPD 117
Cdd:pfam13468  81 WALRTDDIDAVAARLRAAGVEPGRRVRP-DGGDLRWRLLFLADGA 124
VOC_like cd09011
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-123 1.00e-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: 319953  Cd Length: 122  Bit Score: 36.68  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   3 KAIHSMIRVLDEHRSLSFYEKAFGLTVadRLDFPDFTLIylsnsETGFELEL------TVNKGRTEPYDLGDGYgHLAFS 76
Cdd:cd09011    2 KFVNPLLVVKDIEKSKKFYEDVLGQKI--LLDFGENVVF-----EGGFALQEkkswleTIIISDLSIKQQSNNF-ELYFE 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493989954  77 VDDLDsehARFEAagLNPRKLVDFA------PGGDVIARFFfvaDPDGYQIEV 123
Cdd:cd09011   74 VDDFD---AFFEK--LNPHKDIEFIhpilehPWGQRVFRFY---DPDGHIIEI 118
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 69-125 1.15e-03

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


Pssm-ID: 319968  Cd Length: 150  Bit Score: 36.54  E-value: 1.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493989954  69 GYGHLAFSVDDLDSEHARFEAAG----LNPRKLVDFAPGGDviARFFFVADPDGYQIEVLQ 125
Cdd:cd16361   90 GIFHFALQVDDVEAAAERLAAAGgkvlMGPREIPDGGPGKG--NRMVYLRDPWGTLIELVS 148
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 6-122 1.25e-03

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


Pssm-ID: 319931  Cd Length: 132  Bit Score: 36.53  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954   6 HSMIRVLDEHRSLSFYEKAFGLTVADRLDFPDFTLI---YLSNSETGFELELTVNKGRtepydlgdGYGHLAFSVDDLDS 82
Cdd:cd08343    2 HVVLCSPDVEASRDFYTDVLGFRVSDRIVDPGVDGGaflHCDRGTDHHTVALAGGPHP--------GLHHVAFEVHDLDD 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 493989954  83 E---HARFEAAGLNprklVDFAPGGDVI--ARFFFVADPDGYQIE 122
Cdd:cd08343   74 VgrgHDRLREKGYK----IEWGPGRHGLgsQVFDYWFDPSGNRVE 114
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
 6-125 2.47e-03

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


Pssm-ID: 213772 [Multi-domain]  Cd Length: 128  Bit Score: 35.38  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954    6 HSMIRVLDEHRSLSFYEKAFGLTVADRLDFPD--FTLIYLSNSETGFE-LELTVNKGRTEPY--DLGDGYGHLAFSVDDL 80
Cdd:TIGR03081   4 HVGIAVPDLEEAAKFYEDVLGAQVSEIEELPEqgVKVVFIALGNTKVElLEPLGEDSPIAKFleKNGGGIHHIAIEVDDI 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 493989954   81 DSEHARFEAAGLnprKLVDFAP----GGDVIArFFFVADPDGYQIEVLQ 125
Cdd:TIGR03081  84 EAALETLKEKGV---RLIDEEPrigaHGKPVA-FLHPKSTGGVLIELEQ 128
Glyoxalase_6 pfam18029
Glyoxalase-like domain; This entry comprises a diverse set of domains related to the ...
 9-124 3.13e-03

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: 35.05  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954    9 IRVLDEHRSLSFYEKAFGLTVADR----LDFPDFTLIYLSNSETGFEleltvnkgRTEPYDLGDGYGHLAFSVDDLDSEH 84
Cdd:pfam18029   4 LDCADPAALAAFWSAALGWEVVPDdtalPDPDGGGPIGGGGPRLLFQ--------RVPEPKPGKNRVHLDLAVDDLEAAV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 493989954   85 ARFEAAGlnpRKLVDFAPGGDviARFFFVADPDGYQIEVL 124
Cdd:pfam18029  76 ARLVALG---ATVLDDGDDPD--GGRWVLADPEGNEFCLV 110
Glyoxalase_2 pfam12681
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 8-123 3.86e-03

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


Pssm-ID: 403776  Cd Length: 118  Bit Score: 34.69  E-value: 3.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493989954    8 MIRVLDEHRSLSFYEKAFGLTVadRLDFPDFTLIylsnsETGFELELTVNKGRTEPYDLGDGYGH--LAFSVDDLDSEHA 85
Cdd:pfam12681   5 LLVVKDINISRKFYEDVLDQKI--KLDFGENVSF-----EGGFAIQSDFKELIGIDLSIAEQSNNfeLYFEVADVDAFLQ 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 493989954   86 RFEAAG----LNPRKLvdfAPGGDVIARFffvADPDGYQIEV 123
Cdd:pfam12681  78 KIKEIGnieyLHELKE---QPWGQRVFRF---YDPDGHIIEI 113
 
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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