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Conserved domains on  [gi|446512264|ref|WP_000589719|]
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MULTISPECIES: VOC family protein [Bacillus]

Protein Classification

VOC family protein( domain architecture ID 11457526)

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
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
2-136 8.81e-24

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


:

Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 90.02  E-value: 8.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264   2 IKGLYEAHLPVSNLEISISFYES-LGLKLYKRGDDIAFFWIKENESWLGLWEGTE-YKVNYHPSLRHIAFQV-SLHDLEN 78
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDvLGLEVVEREGGRVYLRADGGEHLLVLEEAPGaPPRPGAAGLDHVAFRVpSRADLDA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446512264  79 AIHWLNQKGIsarkdfgmePIEPIVfPELAHAAVYFNDPDGNSLELIAQLPVGLPTAE 136
Cdd:COG2514   81 ALARLAAAGV---------PVEGAV-DHGVGESLYFRDPDGNLIELYTDRPRFEHVGD 128
 
Name Accession Description Interval E-value
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
2-136 8.81e-24

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 90.02  E-value: 8.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264   2 IKGLYEAHLPVSNLEISISFYES-LGLKLYKRGDDIAFFWIKENESWLGLWEGTE-YKVNYHPSLRHIAFQV-SLHDLEN 78
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDvLGLEVVEREGGRVYLRADGGEHLLVLEEAPGaPPRPGAAGLDHVAFRVpSRADLDA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446512264  79 AIHWLNQKGIsarkdfgmePIEPIVfPELAHAAVYFNDPDGNSLELIAQLPVGLPTAE 136
Cdd:COG2514   81 ALARLAAAGV---------PVEGAV-DHGVGESLYFRDPDGNLIELYTDRPRFEHVGD 128
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 9-124 1.50e-12

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: 60.23  E-value: 1.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264   9 HLPVSNLEISISFYES-LGLKLYKRGDDIAFFWIK-ENESWLGLWEGTEYKVNYHPSLRHIAFQVSlhDLENAIHWLNQK 86
Cdd:cd06587    3 ALRVPDLDASVAFYEEvLGFEVVSRNEGGGFAFLRlGPGLRLALLEGPEPERPGGGGLFHLAFEVD--DVDEVDERLREA 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446512264  87 GIsarkdfGMEPIEPIVFPELAHAAVYFNDPDGNSLEL 124
Cdd:cd06587   81 GA------EGELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
PRK04101 PRK04101
metallothiol transferase FosB;
1-124 3.53e-12

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 59.96  E-value: 3.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264   1 MIKGLYEAHLPVSNLEISISFYES-LGLKLYKRGDDIAFFWIkeNESWLGLWEGTEYKVN-YHPSLRHIAFQVSLHDLEN 78
Cdd:PRK04101   1 MLKGINHICFSVSNLEKSIEFYEKvLGAKLLVKGRKTAYFDL--NGLWIALNEEKDIPRNeIHQSYTHIAFSIEEEDFDH 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446512264  79 AIHWLNQKGISARKDFGMEPIEpivfpelaHAAVYFNDPDGNSLEL 124
Cdd:PRK04101  79 WYQRLKENDVNILPGRERDERD--------KKSIYFTDPDGHKFEF 116
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
10-124 2.47e-07

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 46.67  E-value: 2.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264   10 LPVSNLEISISFYES-LGLKLYKRGDDIAF-----FWIKENESWLGL-WEGTEYKVNYHPSLRHIAFQV-SLHDLENAIH 81
Cdd:pfam00903   7 LRVGDLEKSLDFYTDvLGFKLVEETDAGEEgglrsAFFLAGGRVLELlLNETPPPAAAGFGGHHIAFIAfSVDDVDAAYD 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 446512264   82 WLnqkgisarKDFGMEPIEPIVFPELAHAAVYFNDPDGNSLEL 124
Cdd:pfam00903  87 RL--------KAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
2-136 8.81e-24

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 90.02  E-value: 8.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264   2 IKGLYEAHLPVSNLEISISFYES-LGLKLYKRGDDIAFFWIKENESWLGLWEGTE-YKVNYHPSLRHIAFQV-SLHDLEN 78
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDvLGLEVVEREGGRVYLRADGGEHLLVLEEAPGaPPRPGAAGLDHVAFRVpSRADLDA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446512264  79 AIHWLNQKGIsarkdfgmePIEPIVfPELAHAAVYFNDPDGNSLELIAQLPVGLPTAE 136
Cdd:COG2514   81 ALARLAAAGV---------PVEGAV-DHGVGESLYFRDPDGNLIELYTDRPRFEHVGD 128
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 10-125 7.16e-15

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: 66.55  E-value: 7.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264  10 LPVSNLEISISFYES-LGLKLYKRGD------DIAFFWIkENESWLGLWEGT-EYKVNYHPSLRHIAFQVSlhDLENAIH 81
Cdd:COG0346    8 LRVSDLEASLAFYTDvLGLELVKRTDfgdggfGHAFLRL-GDGTELELFEAPgAAPAPGGGGLHHLAFRVD--DLDAAYA 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446512264  82 WLNQKGIsarkdfgmEPIEPIVFPELAHAAVYFNDPDGNSLELI 125
Cdd:COG0346   85 RLRAAGV--------EIEGEPRDRAYGYRSAYFRDPDGNLIELV 120
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 9-124 1.50e-12

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: 60.23  E-value: 1.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264   9 HLPVSNLEISISFYES-LGLKLYKRGDDIAFFWIK-ENESWLGLWEGTEYKVNYHPSLRHIAFQVSlhDLENAIHWLNQK 86
Cdd:cd06587    3 ALRVPDLDASVAFYEEvLGFEVVSRNEGGGFAFLRlGPGLRLALLEGPEPERPGGGGLFHLAFEVD--DVDEVDERLREA 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446512264  87 GIsarkdfGMEPIEPIVFPELAHAAVYFNDPDGNSLEL 124
Cdd:cd06587   81 GA------EGELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
PRK04101 PRK04101
metallothiol transferase FosB;
1-124 3.53e-12

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 59.96  E-value: 3.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264   1 MIKGLYEAHLPVSNLEISISFYES-LGLKLYKRGDDIAFFWIkeNESWLGLWEGTEYKVN-YHPSLRHIAFQVSLHDLEN 78
Cdd:PRK04101   1 MLKGINHICFSVSNLEKSIEFYEKvLGAKLLVKGRKTAYFDL--NGLWIALNEEKDIPRNeIHQSYTHIAFSIEEEDFDH 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446512264  79 AIHWLNQKGISARKDFGMEPIEpivfpelaHAAVYFNDPDGNSLEL 124
Cdd:PRK04101  79 WYQRLKENDVNILPGRERDERD--------KKSIYFTDPDGHKFEF 116
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 12-124 4.18e-09

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


Pssm-ID: 319951 [Multi-domain]  Cd Length: 131  Bit Score: 51.58  E-value: 4.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264  12 VSNLEISISFYES-LGLKLYKRGDDIAFFWIkeNESWLGLWEGTEYKVN-YHPSLRHIAFQVSLHDLENAIHWLNQKGIS 89
Cdd:cd08363    8 VSNLNKSIAFYKDvLDAKLLVLGEKTAYFDL--NGLWLALNVQEDIPRNeISHSYTHIAFSIDEEDLDAFKERLKDNGVN 85

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446512264  90 ARKdfGMEPiepivfPELAHAAVYFNDPDGNSLEL 124
Cdd:cd08363   86 ILE--GRKR------DILEGQSIYFTDPDGHLFEL 112
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 12-124 2.69e-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: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 49.24  E-value: 2.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264  12 VSNLEISISFYES-LGLKLYKR----GDDIAFFWIkENESWLGLWEG---TEYKVNYHP-SLRHIAFQVSlhDLENAIHW 82
Cdd:cd07245    8 CPDLERARRFYTDvLGLEEVPRppflKFGGAWLYL-GGGQQIHLVVEqnpSELPRPEHPgRDRHPSFSVP--DLDALKQR 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446512264  83 LNQKGISARKDfgmepiepiVFPELAHAAVYFNDPDGNSLEL 124
Cdd:cd07245   85 LKEAGIPYTES---------TSPGGGVTQLFFRDPDGNRLEF 117
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 7-129 1.92e-07

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: 46.92  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264   7 EAHLPVSNLEISISFYES-LGLKLYKRGDDIAFFWIKENESWLGLWEGTEYKVNYHPS--LRHIAFQV-SLHDLENAIHW 82
Cdd:cd07255    5 RVTLKVADLERQSAFYQNvIGLSVLKQNASRAYLGVDGKQVLLVLEAIPDAVLAPRSTtgLYHFAILLpDRKALGRALAH 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446512264  83 L--NQKGISArKDFGMEpiepivfpelahAAVYFNDPDGNSLELIAQLP 129
Cdd:cd07255   85 LaeHGPLIGA-ADHGVS------------EAIYLSDPEGNGIEIYADRP 120
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
10-124 2.47e-07

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 46.67  E-value: 2.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264   10 LPVSNLEISISFYES-LGLKLYKRGDDIAF-----FWIKENESWLGL-WEGTEYKVNYHPSLRHIAFQV-SLHDLENAIH 81
Cdd:pfam00903   7 LRVGDLEKSLDFYTDvLGFKLVEETDAGEEgglrsAFFLAGGRVLELlLNETPPPAAAGFGGHHIAFIAfSVDDVDAAYD 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 446512264   82 WLnqkgisarKDFGMEPIEPIVFPELAHAAVYFNDPDGNSLEL 124
Cdd:pfam00903  87 RL--------KAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 10-124 8.15e-07

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: 45.24  E-value: 8.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264  10 LPVSNLEISISFYES-LGLKLYKRGDDIAFFWIKE-----NESWLGLWEGTEYKvnyHPSLRHIAFQVSLHDLENAIHWL 83
Cdd:cd08345    4 LIVRDLEKSTAFLQDiFGAREVYSSGDKTFSLSKEkffllGGLWIALMEGESLQ---ERSYTHIAFQIQSEDFDRYAERL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446512264  84 NQKGISarkdfgMEPIEPIVFPElaHAAVYFNDPDGNSLEL 124
Cdd:cd08345   81 GALGVE------MRPPRPRVEGE--GRSIYFYDPDNHLFEL 113
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 10-125 3.99e-06

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 43.47  E-value: 3.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264  10 LPVSNLEISISFYES-LGLKLYKRGDDIAFFWI--KENESWLGLWEGTEYKVNYHPslrHIAFQVSlhDLENAIHWLNQK 86
Cdd:COG3324   10 LPVDDLERAKAFYEEvFGWTFEDDAGPGGDYAEfdTDGGQVGGLMPGAEEPGGPGW---LLYFAVD--DLDAAVARVEAA 84

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446512264  87 GISARKdfgmepiEPIVFPELAHAAvYFNDPDGNSLELI 125
Cdd:COG3324   85 GGTVLR-------PPTDIPPWGRFA-VFRDPEGNRFGLW 115
PRK11478 PRK11478
VOC family protein;
4-127 1.13e-05

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 42.57  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264   4 GLYEAH---LPVSNLEISISFY-ESLGLKLykrgddIAFFWIKENESWLG-LWEGTEYKVNY--------HPS------L 64
Cdd:PRK11478   3 GLKQVHhiaIIATDYAVSKAFYcDILGFTL------QSEVYREARDSWKGdLALNGQYVIELfsfpfppeRPSrpeacgL 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446512264  65 RHIAFqvSLHDLENAIHWLNQKGISArkdfgmEPIEpiVFPELAHAAVYFNDPDGNSLELIAQ 127
Cdd:PRK11478  77 RHLAF--SVDDIDAAVAHLESHNVKC------EAIR--VDPYTQKRFTFFNDPDGLPLELYEQ 129
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 61-124 1.00e-04

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: 39.83  E-value: 1.00e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446512264  61 HPSLRHIAFQVSlhDLENAIHWLNQKGIsarkdfgmePIEPIVFPELAHAA-VYFNDPDGNSLEL 124
Cdd:cd08352   68 ALGLRHLAFKVE--DVEATVAELKSLGI---------ETEPIRVDDFTGKKfTFFFDPDGLPLEL 121
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 10-52 1.03e-04

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 39.81  E-value: 1.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446512264  10 LPVSNLEISISFYESLGLKLYKR--GDDIAFFWIKENeSWLGLWE 52
Cdd:COG3607    9 LPVADLERSRAFYEALGFTFNPQfsDEGAACFVLGEG-IVLMLLP 52
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 10-124 1.11e-04

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: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264  10 LPVSNLEISISFY-ESLGLKLYKRGDDIAFFwiKENESWLGLweGTEYKVNYHPSLRHIAFQVSLHDLENAIHWLNQKGI 88
Cdd:cd07244    7 LAVSDLERSLAFYvDLLGFKPHVRWDKGAYL--TAGDLWLCL--SLDPAAEPSPDYTHIAFTVSEEDFEELSERLRAAGV 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446512264  89 SARKDFGMEpiepivfpelaHAAVYFNDPDGNSLEL 124
Cdd:cd07244   83 KIWQENSSE-----------GDSLYFLDPDGHKLEL 107
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 10-124 1.15e-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: 39.62  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264  10 LPVSNLEISISFY-ESLGLKLYKRGDDIAFFWIKENESWLGL----WEGTEYKVNYHPSLRHIAFQVSlhDLENAIHWLN 84
Cdd:cd07264    6 LYVDDFAASLRFYrDVLGLPPRFLHEEGEYAEFDTGETKLALfsrkEMARSGGPDRRGSAFELGFEVD--DVEATVEELV 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446512264  85 QKGISARkdfgMEPIEPivfpELAHAAVYFNDPDGNSLEL 124
Cdd:cd07264   84 ERGAEFV----REPANK----PWGQTVAYVRDPDGNLIEI 115
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 8-126 2.79e-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: 38.45  E-value: 2.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264   8 AHLPVSNLEISISFYES-LGLKLYKRGDDIAFFWIKENESW-LGLWEGTEykvnyhPSLRHIAFQV-SLHDLENAIHWLN 84
Cdd:cd16360    2 AELGVPDLEKALEFYTDvLGLQVAKRDGNSVYLRGYEDEHHsLVLYEAPE------AGLKHFAFEVaSEEDLERAAASLT 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446512264  85 QKGISARKdfgmepiEPIVFPELAHAAVYFNDPDGNSLELIA 126
Cdd:cd16360   76 ALGCDVTW-------GPDGEVPGGGKGFRFQDPSGHLLELFV 110
VOC_BsYqjT cd07242
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; The vicinal ...
 4-126 7.57e-04

vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; 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: 319906  Cd Length: 126  Bit Score: 37.47  E-value: 7.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264   4 GLYEAHLPVSNLEISISFYESLGLKLYKRGDDIAFF--WIKENESWLGLWEGTEYKVNYH----PSLRHIAFQV-SLHDL 76
Cdd:cd07242    1 GVSHVELAVSDLHRSFKWFEWILGLGWKEYDTWSFGpsWKLSGGSLLVVQQTDEFATPEFdrarVGLNHLAFHAeSREAV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446512264  77 ENAIHWLNQKGisARKDFGmepiEPIVFPELA-HAAVYFNDPDGNSLELIA 126
Cdd:cd07242   81 DELTEKLAKIG--GVRTYG----DRHPFAGGPpHYAAFCEDPDGIKLELVA 125
MhqB_like_N cd08344
N-terminal domain of MhqB, a type I extradiol dioxygenase, and similar proteins; This ...
 10-124 1.36e-03

N-terminal domain of MhqB, a type I extradiol dioxygenase, and similar proteins; This subfamily contains the N-terminal, non-catalytic, domain of Burkholderia sp. NF100 MhqB and similar proteins. MhqB is a type I extradiol dioxygenase involved in the catabolism of methylhydroquinone, an intermediate in the degradation of fenitrothion. The purified enzyme has shown extradiol ring cleavage activity toward 3-methylcatechol. Fe2+ was suggested as a cofactor, the same as most other enzymes in the family. Burkholderia sp. NF100 MhqB is encoded on the plasmid pNF1. The type I family of extradiol dioxygenases contains two structurally homologous barrel-shaped domains at the N- and C-terminal. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism.


Pssm-ID: 319932  Cd Length: 112  Bit Score: 36.24  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264  10 LPVSNLEISISFYESLGLKLYKRGDDIAFFWIKENESWLGLWEGTEYKvnyhpsLRHIAFQVSLHDLENAIHWLNQKGIs 89
Cdd:cd08344    8 LEVPDLEVARRFYEAFGLDVRETGEDLELRAPGNDHVWARLIQGARKR------LAYLSFGIFGDDLARFAAHLDAAGV- 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446512264  90 ARKD--FGMEPiepivfpelahAAVYFNDPDGNSLEL 124
Cdd:cd08344   81 ALIAapPGADP-----------DGVWFEDPDGNLLQV 106
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 10-124 9.10e-03

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: 34.12  E-value: 9.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446512264  10 LPVSNLEISISFYES-LGLKL-YKRGDDIAffwikeneswlgLWEGTEyKVNYH--------------PSLRHIAFQVSl 73
Cdd:cd07253    9 LTVKDIERTIDFYTKvLGMTVvTFKEGRKA------------LRFGNQ-KINLHqkgkefepkasaptPGSADLCFITE- 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446512264  74 HDLENAIHWLNQKGISarkdfgmePIEPIVFPELAHAA---VYFNDPDGNSLEL 124
Cdd:cd07253   75 TPIDEVLEHLEACGVT--------IEEGPVKRTGALGPilsIYFRDPDGNLIEL 120
 
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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