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Conserved domains on  [gi|504270825|ref|WP_014457927|]
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MULTISPECIES: VOC family protein [Priestia]

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 ...
 5-127 1.38e-29

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: 103.53  E-value: 1.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   5 KFEHVGVQVKDIEKSIEFYTQKVGLELIETLPHTDPSLKLAFLGLEGNVIVELIQGYN-SSLPNEGKVHHFALAVDGIEE 83
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTELELFEAPGaAPAPGGGGLHHLAFRVDDLDA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 504270825  84 EFERLKSAGVSFVEEnIVTLPNGARYLFFYGPDKEWIEYYEVKR 127
Cdd:COG0346   82 AYARLRAAGVEIEGE-PRDRAYGYRSAYFRDPDGNLIELVEPPP 124
 
Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 5-127 1.38e-29

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: 103.53  E-value: 1.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   5 KFEHVGVQVKDIEKSIEFYTQKVGLELIETLPHTDPSLKLAFLGLEGNVIVELIQGYN-SSLPNEGKVHHFALAVDGIEE 83
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTELELFEAPGaAPAPGGGGLHHLAFRVDDLDA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 504270825  84 EFERLKSAGVSFVEEnIVTLPNGARYLFFYGPDKEWIEYYEVKR 127
Cdd:COG0346   82 AYARLRAAGVEIEGE-PRDRAYGYRSAYFRDPDGNLIELVEPPP 124
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 8-122 1.14e-20

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


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 80.26  E-value: 1.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   8 HVGVQVKDIEKSIEFYTQKVGLELIetlpHTDPSLKLAFLGLEGNVIVELIQGYNSSLPNEGKVHHFALAVDGIEEEFER 87
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVV----SRNEGGGFAFLRLGPGLRLALLEGPEPERPGGGGLFHLAFEVDDVDEVDER 76

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 504270825  88 LKSAGVSF-VEENIVTLPNGARYLFFYGPDKEWIEY 122
Cdd:cd06587   77 LREAGAEGeLVAPPVDDPWGGRSFYFRDPDGNLIEF 112
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
5-122 1.71e-19

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 77.49  E-value: 1.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825    5 KFEHVGVQVKDIEKSIEFYTQKVGLELIETLPHTDPSLKLAFLGLEGNVIVELIQGYNSS----LPNEGKVHHFALAVDG 80
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLNETPPpaaaGFGGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 504270825   81 IEEEFERLKSAGVSFVEEnIVTLPNGARYLFFYGPDKEWIEY 122
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVRE-PGRHGWGGRYSYFRDPDGNLIEL 121
PLN02367 PLN02367
lactoylglutathione lyase
 12-127 1.64e-07

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 48.07  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825  12 QVKDIEKSIEFYTQKVGLELIETLPHTDPSLKLAFLGLEGNV------------------IVELIQGYNS-SLPNEGKVH 72
Cdd:PLN02367  82 RIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFMGYEDTAsaptdptertvwtfgqkaTIELTHNWGTeSDPDFKGYH 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504270825  73 ----------HFALAVDGIEEEFERLKSAGVSFVEEnivtlPNGARY---LFFYGPDKEWIEYYEVKR 127
Cdd:PLN02367 162 ngnseprgfgHIGITVDDVYKACERFEELGVEFVKK-----PNDGKMkgiAFIKDPDGYWIEIFDLKT 224
 
Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 5-127 1.38e-29

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: 103.53  E-value: 1.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   5 KFEHVGVQVKDIEKSIEFYTQKVGLELIETLPHTDPSLKLAFLGLEGNVIVELIQGYN-SSLPNEGKVHHFALAVDGIEE 83
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTELELFEAPGaAPAPGGGGLHHLAFRVDDLDA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 504270825  84 EFERLKSAGVSFVEEnIVTLPNGARYLFFYGPDKEWIEYYEVKR 127
Cdd:COG0346   82 AYARLRAAGVEIEGE-PRDRAYGYRSAYFRDPDGNLIELVEPPP 124
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 8-122 1.14e-20

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


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 80.26  E-value: 1.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   8 HVGVQVKDIEKSIEFYTQKVGLELIetlpHTDPSLKLAFLGLEGNVIVELIQGYNSSLPNEGKVHHFALAVDGIEEEFER 87
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVV----SRNEGGGFAFLRLGPGLRLALLEGPEPERPGGGGLFHLAFEVDDVDEVDER 76

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 504270825  88 LKSAGVSF-VEENIVTLPNGARYLFFYGPDKEWIEY 122
Cdd:cd06587   77 LREAGAEGeLVAPPVDDPWGGRSFYFRDPDGNLIEF 112
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
5-122 1.71e-19

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 77.49  E-value: 1.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825    5 KFEHVGVQVKDIEKSIEFYTQKVGLELIETLPHTDPSLKLAFLGLEGNVIVELIQGYNSS----LPNEGKVHHFALAVDG 80
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLNETPPpaaaGFGGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 504270825   81 IEEEFERLKSAGVSFVEEnIVTLPNGARYLFFYGPDKEWIEY 122
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVRE-PGRHGWGGRYSYFRDPDGNLIEL 121
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 8-112 4.06e-17

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: 71.45  E-value: 4.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   8 HVGVQVKDIEKSIEFYTQKVGLELIETLPHTDPSLKLAFLGLeGNVIVELIQ--GYNSSL------PNEGkVHHFALAVD 79
Cdd:cd07249    3 HIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLEL-GNTQIELLEplGEDSPIakfldkKGGG-LHHIAFEVD 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 504270825  80 GIEEEFERLKSAGVSFVEENIVTLPNGARYLFF 112
Cdd:cd07249   81 DIDAAVEELKAQGVRLLSEGPRIGAHGKRVAFL 113
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
8-111 1.26e-14

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 64.61  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825    8 HVGVQVKDIEKSIEFYTQKVGLELIETLPHTDPSLKLAFLGL-EGNVIVELIQ--GYNSSL-PNEGKVHHFALAVDGIEE 83
Cdd:pfam13669   2 HVGIAVPDLDRALALWGALLGLGPEGDYRSEPQNVDLAFALLgDGPVEVELIQplDGDSPLaRHGPGLHHLAYWVDDLDA 81

                          90       100
                  ....*....|....*....|....*...
gi 504270825   84 EFERLKSAGVSFVEENIVTLPNGARYLF 111
Cdd:pfam13669  82 AVARLLDQGYRVAPKGPRAGAAGRRVAF 109
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 6-121 1.27e-13

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: 63.11  E-value: 1.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   6 FEHVGVQVKDIEKSIEFYTQKVGLELIETLPHTDPSLKLAFLGLEGNVIVELIQGYNSSLPNEG---------------- 69
Cdd:cd07233    1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDPKDIPKDPRTAWVFSREGtlelthnwgtendedp 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504270825  70 KVH----------HFALAVDGIEEEFERLKSAGVSFVEEnivtlPNGARY---LFFYGPDKEWIE 121
Cdd:cd07233   81 VYHngnsdprgfgHIGIAVDDVYAACERFEELGVKFKKK-----PDDGKMkgiAFIKDPDGYWIE 140
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-116 1.89e-13

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: 61.95  E-value: 1.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   8 HVGVQVKDIEKSIEFYTQKVGLELIETLPHTDpsLKLAFLGLEGNVIVELIQGYNSSLPNE----GKVHHFALAVDGIEE 83
Cdd:cd07245    3 HVALACPDLERARRFYTDVLGLEEVPRPPFLK--FGGAWLYLGGGQQIHLVVEQNPSELPRpehpGRDRHPSFSVPDLDA 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 504270825  84 EFERLKSAGVSFVEEniVTLPNGARYLFFYGPD 116
Cdd:cd07245   81 LKQRLKEAGIPYTES--TSPGGGVTQLFFRDPD 111
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
3-123 3.64e-12

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 59.20  E-value: 3.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   3 ILKFEHVGVQVKDIEKSIEFYTQKVGLELIEtlpHTDPSLKLAFLGleGNVIVELIQGYN-SSLPNEGKVHHFALAVDGI 81
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVE---REGGRVYLRADG--GEHLLVLEEAPGaPPRPGAAGLDHVAFRVPSR 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 504270825  82 EEE---FERLKSAGVSFVEEnivTLPNGARYLFFYGPDKEWIEYY 123
Cdd:COG2514   76 ADLdaaLARLAAAGVPVEGA---VDHGVGESLYFRDPDGNLIELY 117
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 4-124 4.13e-11

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: 56.01  E-value: 4.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   4 LKFEHVGVQVKDIEKSIEFYTQKVGLELI-ETLPHTDPSLKLAfLGLeGNVIVELIQGYNS----SLPNEGKVHHFALAV 78
Cdd:cd08352    1 KKIHHIAIICSDYEKSKDFYVDKLGFEIIrEHYRPERNDIKLD-LAL-GGYQLELFIKPDAparpSYPEALGLRHLAFKV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 504270825  79 DGIEEEFERLKSAGVSfVEENIVTLPNGARYLFFYGPDKEWIEYYE 124
Cdd:cd08352   79 EDVEATVAELKSLGIE-TEPIRVDDFTGKKFTFFFDPDGLPLELYE 123
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 5-116 1.42e-10

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 54.64  E-value: 1.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   5 KFEHVGVQVKDIEKSIEFYTQKVGLELIEtlpHTDPSLKLAFLGLEGNVIVELIQGynSSLPNEGKVHhFALAVDGIEEE 84
Cdd:COG3324    4 TIVWVELPVDDLERAKAFYEEVFGWTFED---DAGPGGDYAEFDTDGGQVGGLMPG--AEEPGGPGWL-LYFAVDDLDAA 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 504270825  85 FERLKSAGVSFVEEnIVTLPNGARYLFFYGPD 116
Cdd:COG3324   78 VARVEAAGGTVLRP-PTDIPPWGRFAVFRDPE 108
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 5-92 1.10e-09

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: 52.72  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   5 KFEHVGVQVKDIEKSIEFYTQKVGLELI---ETLPHTDP---------------SLKLAFLGLEGNVIVELIQGYNSSLP 66
Cdd:cd16361    1 GVNHVGITVPDLDAAVEFYTDVLGAEVVyrsTPLAEGDRgggemraagfvpgfaRARIAMLRLGPGPGIELFEYKGPEQR 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 504270825  67 NEGK------VHHFALAVDGIEEEFERLKSAG 92
Cdd:cd16361   81 APVPrnsdvgIFHFALQVDDVEAAAERLAAAG 112
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 1-98 3.27e-09

4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and metabolism, General function prediction only];


Pssm-ID: 442418 [Multi-domain]  Cd Length: 333  Bit Score: 52.97  E-value: 3.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   1 MAILKFEHVGVQVK--DIEKSIEFYTQKVGLELI--ETLPHTDPSLKLAFLGL-EGNVIVEL---------IQGYNSSLP 66
Cdd:COG3185  142 AGLTRIDHIGIAVPrgDLDEWVLFYEDVLGFEEIreEDIEDPYQGVRSAVLQSpDGKVRIPLneptspdsqIAEFLEKYR 221

                         90       100       110
                 ....*....|....*....|....*....|..
gi 504270825  67 NEGkVHHFALAVDGIEEEFERLKSAGVSFVEE 98
Cdd:COG3185  222 GEG-IQHIAFATDDIEATVAALRARGVRFLDI 252
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 8-98 6.36e-09

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: 50.09  E-value: 6.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   8 HVGVQVKDIEKSIEFYTQKVGLELIETLPHTDPSLKLAFLGL---EGNVIVELIQGYNSSLPNEGKVH-HFALAVDGIEE 83
Cdd:cd16358    3 HTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYgdeDENTVLELTYNWGVDKYDLGTAYgHIAIGVEDVYE 82

                         90
                 ....*....|....*
gi 504270825  84 EFERLKSAGVSFVEE 98
Cdd:cd16358   83 TCERIRKKGGKVTRE 97
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-116 3.33e-08

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: 48.45  E-value: 3.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   8 HVGVQVKDIEKSIEFYTQKVGLEL-----------IETLPHTDPSLKLAflgLEGNVIVEliQGYNSSLPNEGKVHhFAL 76
Cdd:cd07263    1 QVMLYVDDQDKALDFYVEKLGFEVvedvpmggmrwVTVAPPGSPGTSLL---LEPKAHPA--QMPQSPEAAGGTPG-ILL 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 504270825  77 AVDGIEEEFERLKSAGVSFVEEniVTLPNGARYLFFYGPD 116
Cdd:cd07263   75 ATDDIDATYERLTAAGVTFVQE--PTQMGGGRVANFRDPD 112
PLN02367 PLN02367
lactoylglutathione lyase
 12-127 1.64e-07

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 48.07  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825  12 QVKDIEKSIEFYTQKVGLELIETLPHTDPSLKLAFLGLEGNV------------------IVELIQGYNS-SLPNEGKVH 72
Cdd:PLN02367  82 RIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFMGYEDTAsaptdptertvwtfgqkaTIELTHNWGTeSDPDFKGYH 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504270825  73 ----------HFALAVDGIEEEFERLKSAGVSFVEEnivtlPNGARY---LFFYGPDKEWIEYYEVKR 127
Cdd:PLN02367 162 ngnseprgfgHIGITVDDVYKACERFEELGVEFVKK-----PNDGKMkgiAFIKDPDGYWIEIFDLKT 224
PRK10291 PRK10291
glyoxalase I; Provisional
 11-126 8.62e-07

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 44.63  E-value: 8.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825  11 VQVKDIEKSIEFYTQKVGLELIETLPHTDPSLKLAFLGL---EGNVIVELIQGYNSSLPNEGKVH-HFALAVDGIEEEFE 86
Cdd:PRK10291   2 LRVGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYgpeTEEAVIELTYNWGVDKYELGTAYgHIALSVDNAAEACE 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 504270825  87 RLKSAGVSFVEENIVTLPNGARYLFFYGPDKEWIEYYEVK 126
Cdd:PRK10291  82 KIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIEEK 121
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 8-123 1.29e-06

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: 44.23  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   8 HVGVQVKDIEKSIEFYTQKVGLELIETLPHTDpSLKLAFLGLEGNVIVELI--QGYNSslpneGKVHHFALAVDGIEEE- 84
Cdd:cd08343    2 HVVLCSPDVEASRDFYTDVLGFRVSDRIVDPG-VDGGAFLHCDRGTDHHTValAGGPH-----PGLHHVAFEVHDLDDVg 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 504270825  85 --FERLKSAGVsfveeNIVT-----LPNGARYLFFYGPDKEWIEYY 123
Cdd:cd08343   76 rgHDRLREKGY-----KIEWgpgrhGLGSQVFDYWFDPSGNRVEYY 116
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 12-127 3.55e-06

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 44.04  E-value: 3.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825  12 QVKDIEKSIEFYTQKVGLELIETLPHTDPSLKLAFLGLEG------------------NVIVELIQGYNS-SLPNEGKVH 72
Cdd:PLN03042  34 RIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLGYEDsetaptdppertvwtfgrKATIELTHNWGTeSDPEFKGYH 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504270825  73 ----------HFALAVDGIEEEFERLKSAGVSFVEEnivtlPNGARY---LFFYGPDKEWIEYYEVKR 127
Cdd:PLN03042 114 ngnsdprgfgHIGITVDDVYKACERFEKLGVEFVKK-----PDDGKMkglAFIKDPDGYWIEIFDLKR 176
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 8-98 6.43e-06

N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from Rhodococcus rhodochrous K37, and similar proteins; 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). The enzyme contains a N-terminal and a C-terminal domain of similar structure fold, resulting from an ancient gene duplication. BphC belongs to the type I extradiol dioxygenase family, which requires a metal in the active site for its catalytic activity. Polychlorinated biphenyl degrading bacteria demonstrate multiplicity of BphCs. Bacterium Rhodococcus rhodochrous K37 has eight genes encoding BphC enzymes. This family includes the N-terminal domain of BphC5-RrK37. The crystal structure of the protein from Novosphingobium aromaticivorans has a Mn(II)in the active site, although most proteins of type I extradiol dioxygenases are activated by Fe(II).


Pssm-ID: 319950 [Multi-domain]  Cd Length: 120  Bit Score: 42.24  E-value: 6.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   8 HVGVQVKDIEKSIEFYTQKVGLELIetlpHTDPSlkLAFLGLEG--NVIVELIQGynsslpNEGKVHHFALAVDG---IE 82
Cdd:cd08362    6 YVALGVPDLAAEREFYTEVWGLEEV----AEDDD--VVYLRAEGseHHVLRLRQS------DENRLDLIAFAAATradVD 73

                         90
                 ....*....|....*.
gi 504270825  83 EEFERLKSAGVSFVEE 98
Cdd:cd08362   74 ALAARLAAAGVRILSE 89
PRK11478 PRK11478
VOC family protein;
8-124 6.43e-06

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 42.57  E-value: 6.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   8 HVGVQVKDIEKSIEFYTQKVGLELIETLPHTDPSLKLAFLGLEGNVIVELIQ----GYNSSLPNEGKVHHFALAVDGIEE 83
Cdd:PRK11478   9 HIAIIATDYAVSKAFYCDILGFTLQSEVYREARDSWKGDLALNGQYVIELFSfpfpPERPSRPEACGLRHLAFSVDDIDA 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 504270825  84 EFERLKSAGVSFveENIVTLP-NGARYLFFYGPDKEWIEYYE 124
Cdd:PRK11478  89 AVAHLESHNVKC--EAIRVDPyTQKRFTFFNDPDGLPLELYE 128
PLN02300 PLN02300
lactoylglutathione lyase
 5-92 1.13e-05

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 42.85  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   5 KFEHVGVQVKDIEKSIEFYTQKVGLELIETLPHTDPSLKLAFLGL---EGNVIVELIQGYNSSLPNEGK-VHHFALAVDG 80
Cdd:PLN02300  24 RMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYgpeDSNFVVELTYNYGVDKYDIGTgFGHFGIAVED 103

                         90
                 ....*....|..
gi 504270825  81 IEEEFERLKSAG 92
Cdd:PLN02300 104 VAKTVELVKAKG 115
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-102 1.67e-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: 319917 [Multi-domain]  Cd Length: 120  Bit Score: 41.29  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   8 HVGVQVKDIEKSIEFYTQKVGLE-----------LIEtlphtDPSLKLAFLGLEGnviveliqgynsslPNEGKVHHFAL 76
Cdd:cd07254    4 HLSLNVTDLERSIRFYSDLFGAEpakrkadyakfMLE-----DPPLNLALLVNDR--------------KEPYGLNHLGI 64

                         90       100
                 ....*....|....*....|....*....
gi 504270825  77 AVDGIEE---EFERLKSAGVSFVEENIVT 102
Cdd:cd07254   65 QVDSKEEvaaLKARAEAAGLPVRKEPRTT 93
VOC_like cd08353
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-115 2.56e-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: 319941  Cd Length: 142  Bit Score: 41.02  E-value: 2.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   3 ILKFEHVGVQVKDIEKSIEFYTqKVGLELI-------ETLPH----TDPSLKLAFLGL-EGNVIVELIQ--------GYN 62
Cdd:cd08353    1 IKRMDHVGIVVEDLDAAIAFFT-ELGLELEgrmtvegEWADRvvglDGVRVEIAMLRTpDGHGRLELSKfltpaaipGHR 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504270825  63 SSLPNEGKVHHFALAVDGIEEEFERLKSAGVSFVEEnIVTLPNGARYLFFYGP 115
Cdd:cd08353   80 PAPANALGLRHVAFAVDDIDAVVARLRKHGAELVGE-VVQYEDSYRLCYVRGP 131
VOC_like cd09011
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 4-124 6.16e-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: 319953  Cd Length: 122  Bit Score: 39.76  E-value: 6.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   4 LKFEHVGVQVKDIEKSIEFYTQKVGLELIETLpHTDPSLKLAFLGLEGNVIVELIQGYNSSLPNEGKVHHFALAVDGIEE 83
Cdd:cd09011    1 MKFVNPLLVVKDIEKSKKFYEDVLGQKILLDF-GENVVFEGGFALQEKKSWLETIIISDLSIKQQSNNFELYFEVDDFDA 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 504270825  84 EFERLKSAGVSFVEENIVTLPNGARYLFFYGPDKEWIEYYE 124
Cdd:cd09011   80 FFEKLNPHKDIEFIHPILEHPWGQRVFRFYDPDGHIIEIGE 120
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 8-99 6.18e-05

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: 39.57  E-value: 6.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   8 HVGVQVKDIEKSIEFYTQKVGLELIETLPhtdpslKLAFLgLEGNVIVELiqgynSSLPNEGKVH---HFALAVDgiEEE 84
Cdd:cd07244    4 HITLAVSDLERSLAFYVDLLGFKPHVRWD------KGAYL-TAGDLWLCL-----SLDPAAEPSPdytHIAFTVS--EED 69

                         90
                 ....*....|....*....
gi 504270825  85 F----ERLKSAGVSFVEEN 99
Cdd:cd07244   70 FeelsERLRAAGVKIWQEN 88
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 8-123 1.88e-04

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


Pssm-ID: 319933  Cd Length: 118  Bit Score: 38.31  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   8 HVGVQVKDIEKSIEFYTQKVGLELIETLPHTDPSL-KLAFLGLeGNVIVELIQGYNsslPNEGKVHHFALAVDgiEEEF- 85
Cdd:cd08345    1 HITLIVRDLEKSTAFLQDIFGAREVYSSGDKTFSLsKEKFFLL-GGLWIALMEGES---LQERSYTHIAFQIQ--SEDFd 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 504270825  86 ---ERLKSAGVSFVEENIVTLPNGaRYLFFYGPDKEWIEYY 123
Cdd:cd08345   75 ryaERLGALGVEMRPPRPRVEGEG-RSIYFYDPDNHLFELH 114
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 13-124 2.91e-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: 37.70  E-value: 2.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825  13 VKDIEKSIEFYTQKVGLeliETLPHTDPSLKLAFLGleGNVIVELIQGYNS--SLPNEGKVHHFALA--VDGIEEEFERL 88
Cdd:cd07264    8 VDDFAASLRFYRDVLGL---PPRFLHEEGEYAEFDT--GETKLALFSRKEMarSGGPDRRGSAFELGfeVDDVEATVEEL 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 504270825  89 KSAGVSFVEENIVTlPNGARYLFFYGPDKEWIEYYE 124
Cdd:cd07264   83 VERGAEFVREPANK-PWGQTVAYVRDPDGNLIEICE 117
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 3-121 3.79e-04

Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily of VOC family contains human glyoxalase domain-containing protein 5 and similar proteins. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319916 [Multi-domain]  Cd Length: 123  Bit Score: 37.59  E-value: 3.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   3 ILKFEHVGVQVKDIEKSIEFYTQKVGLELIETlphTDPSLKLAFlgleGNVIVELIQ-GYN----SSLPNEGkVHHFALA 77
Cdd:cd07253    1 IKRLDHLVLTVKDIERTIDFYTKVLGMTVVTF---KEGRKALRF----GNQKINLHQkGKEfepkASAPTPG-SADLCFI 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 504270825  78 VD-GIEEEFERLKSAGVSfVEENIV--TLPNGARY-LFFYGPDKEWIE 121
Cdd:cd07253   73 TEtPIDEVLEHLEACGVT-IEEGPVkrTGALGPILsIYFRDPDGNLIE 119
VOC_like cd07246
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 13-109 9.57e-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: 319910 [Multi-domain]  Cd Length: 124  Bit Score: 36.51  E-value: 9.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825  13 VKDIEKSIEFYTQKVGLELIETLPHTDPSLKLAFLGLEGNVIVEL----IQGYNSSLPNEGKVHHFALAVDGIEEEFERL 88
Cdd:cd07246    9 VEDAAAAIAFYKKAFGAEELGRTTQEDGRVGHAELRIGGTVVMVAdenpERGALSPTKLGGTPVIFHLYVEDVDATFARA 88

                         90       100
                 ....*....|....*....|.
gi 504270825  89 KSAGVSFVEEnIVTLPNGARY 109
Cdd:cd07246   89 VAAGAVVVEP-VEDQFWGDRV 108
THT_oxygenase_C cd07257
The C-terminal domain of 2,4,5-trihydroxytoluene (THT) oxygenase; This subfamily contains the ...
 5-82 1.01e-03

The C-terminal domain of 2,4,5-trihydroxytoluene (THT) oxygenase; This subfamily contains the C-terminal, catalytic, domain of THT oxygenase. THT oxygenase is an extradiol dioxygenase in the 2,4-dinitrotoluene (DNT) degradation pathway. It catalyzes the conversion of 2,4,5-trihydroxytoluene to an unstable ring fission product, 2,4-dihydroxy-5-methyl-6-oxo-2,4-hexadienoic acid. The native protein was determined to be a dimer by gel filtration. The enzyme belongs to the type I family of extradiol dioxygenases which contains two structurally homologous barrel-shaped domains at the N- and C-terminus of each monomer. The active-site metal is located in the C-terminal barrel. Fe(II) is required for its catalytic activity.


Pssm-ID: 319920  Cd Length: 152  Bit Score: 36.93  E-value: 1.01e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504270825   5 KFEHVGVQVKDIEKSIEFYTQKVGLELIETLPHTDPSLKLAFLGLE-GNVIVELIQGYNSSLPNeGKVHHFALAVDGIE 82
Cdd:cd07257    1 KLGHVGLEVNDFEATFDWYTKTFGLKPSDVIYLPDGKTVGSFLHLDrGSEYVDHHSFFFAQGPR-PKVHHAAFEVHDFD 78
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 7-79 1.11e-03

N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC superfamily contains Bacillus subtilis CatE and similar proteins. CatE is proposed to function as Catechol-2,3-dioxygenase. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319918  Cd Length: 124  Bit Score: 36.14  E-value: 1.11e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504270825   7 EHVGVQVKDIEKSIEFYTQKVGLELIETLPHTdpslklAFLGLEGN---VIVELIQGYNSSLPNEGKVHHFALAVD 79
Cdd:cd07255    4 GRVTLKVADLERQSAFYQNVIGLSVLKQNASR------AYLGVDGKqvlLVLEAIPDAVLAPRSTTGLYHFAILLP 73
Glyoxalase_3 pfam13468
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 6-97 4.36e-03

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


Pssm-ID: 433233  Cd Length: 175  Bit Score: 35.00  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825    6 FEHVGVQVKDIEKSIEFYTQKVG-------------------------LELIETLPHTDPSLKLAFLGLEgnvIVELIQG 60
Cdd:pfam13468   1 LDHVVLAVPDLDEAAARFARALGftvtpggrhpgmgtanalimfgdgyLELLAVDPEAPAPPRGRWFGLD---RLADGEG 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 504270825   61 ynsslpnegkVHHFALAVDGIEEEFERLKSAGVSFVE 97
Cdd:pfam13468  78 ----------LLGWALRTDDIDAVAARLRAAGVEPGR 104
BphC1-RGP6_C_like cd07237
C-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase; This subfamily contains the ...
 8-93 9.19e-03

C-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase; This subfamily contains the C-terminal, catalytic, domain of BphC1-RGP6 and similar proteins. BphC catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). This subfamily of BphCs belongs to the type I extradiol dioxygenase family, which require a metal in the active site in its catalytic mechanism. Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. For example, three types of BphC enzymes have been found in Rhodococcus globerulus (BphC1-RGP6 - BphC3-RGP6), all three enzymes are type I extradiol dioxygenases. BphC1-RGP6 has an internal duplication, it is a two-domain dioxygenase which forms octamers, and has Fe(II) at the catalytic site. Its C-terminal repeat is represented in this subfamily. BphC2-RGP6 and BphC3-RGP6 are one-domain dioxygenases, they belong to a different subfamily of the ED_TypeI_classII_C (C-terminal domain of type I, class II extradiol dioxygenases) family.


Pssm-ID: 319902  Cd Length: 153  Bit Score: 34.17  E-value: 9.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504270825   8 HVGVQVKDIEKSIEFYTQKVGLEL---IETLPHTDPSLKLAFLGlegnvivelIQGYNSSL-----PNEGKVHHFALAVD 79
Cdd:cd07237   12 HVVLIVPDVDEALAFYTDVLGFRLsdeIRIPLPPGVTARLHFLH---------CNGRHHSLafgagPGPKRLHHLMLEVT 82

                         90
                 ....*....|....*..
gi 504270825  80 GIE---EEFERLKSAGV 93
Cdd:cd07237   83 SLDdvgRAYDRVRKRGI 99
 
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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