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Conserved domains on  [gi|1879460250|ref|XP_035505977|]
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glyoxalase domain-containing protein 5 [Scophthalmus maximus]

Protein Classification

VOC family protein( domain architecture ID 10163535)

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
PubMed:  21820381

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 39-161 6.34e-76

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: 222.49  E-value: 6.34e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  39 LSHLDHLVLTVKSVPDTIHFYTSVLGMEVVTFKGNRKALSFGQQKFNLHQLGQEFEPKAKHPTSGSADLCLITNTPLATV 118
Cdd:cd07253     1 IKRLDHLVLTVKDIERTIDFYTKVLGMTVVTFKEGRKALRFGNQKINLHQKGKEFEPKASAPTPGSADLCFITETPIDEV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1879460250 119 AAHLKVCGVEIEEGPVERSGAVGPITSLYFRDPDHNLIEVSNY 161
Cdd:cd07253    81 LEHLEACGVTIEEGPVKRTGALGPILSIYFRDPDGNLIELSNY 123
 
Name Accession Description Interval E-value
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 39-161 6.34e-76

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: 222.49  E-value: 6.34e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  39 LSHLDHLVLTVKSVPDTIHFYTSVLGMEVVTFKGNRKALSFGQQKFNLHQLGQEFEPKAKHPTSGSADLCLITNTPLATV 118
Cdd:cd07253     1 IKRLDHLVLTVKDIERTIDFYTKVLGMTVVTFKEGRKALRFGNQKINLHQKGKEFEPKASAPTPGSADLCFITETPIDEV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1879460250 119 AAHLKVCGVEIEEGPVERSGAVGPITSLYFRDPDHNLIEVSNY 161
Cdd:cd07253    81 LEHLEACGVTIEEGPVKRTGALGPILSIYFRDPDGNLIELSNY 123
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 41-161 6.41e-18

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: 75.03  E-value: 6.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  41 HLDHLVLTVKSVPDTIHFYTSVLGMEVVT------FKGNRKALSFGQ-QKFNLHqlgqEFEPKAKHPTSGSAD-LCLITN 112
Cdd:COG0346     2 GLHHVTLRVSDLEASLAFYTDVLGLELVKrtdfgdGGFGHAFLRLGDgTELELF----EAPGAAPAPGGGGLHhLAFRVD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1879460250 113 TpLATVAAHLKVCGVEIEEGPVERsgAVGPiTSLYFRDPDHNLIEVSNY 161
Cdd:COG0346    78 D-LDAAYARLRAAGVEIEGEPRDR--AYGY-RSAYFRDPDGNLIELVEP 122
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
41-158 5.42e-09

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 51.68  E-value: 5.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  41 HLDHLVLTVKSVPDTIHFYTSVLGMEVVTFKGNRKALSFGQQKF----NLHQLGQEFEPKAKHPTSGSADLCLITNTP-- 114
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFlaggRVLELLLNETPPPAAAGFGGHHIAFIAFSVdd 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1879460250 115 LATVAAHLKVCGVEIEEGPveRSGAVGPITSlYFRDPDHNLIEV 158
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREP--GRHGWGGRYS-YFRDPDGNLIEL 121
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 42-101 4.54e-03

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


Pssm-ID: 272886  Cd Length: 150  Bit Score: 35.94  E-value: 4.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  42 LDHLVLTVKSVPDTIHFYTSVLGMEVVtfkgnrKALSFGQQKFNLHQLGqeFEPKAKHPT 101
Cdd:TIGR00068  18 LLHTMLRVGDLDKSLDFYTEVLGMKLL------RKRDFPEMKFSLAFLG--YGDETSAAV 69
 
Name Accession Description Interval E-value
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 39-161 6.34e-76

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: 222.49  E-value: 6.34e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  39 LSHLDHLVLTVKSVPDTIHFYTSVLGMEVVTFKGNRKALSFGQQKFNLHQLGQEFEPKAKHPTSGSADLCLITNTPLATV 118
Cdd:cd07253     1 IKRLDHLVLTVKDIERTIDFYTKVLGMTVVTFKEGRKALRFGNQKINLHQKGKEFEPKASAPTPGSADLCFITETPIDEV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1879460250 119 AAHLKVCGVEIEEGPVERSGAVGPITSLYFRDPDHNLIEVSNY 161
Cdd:cd07253    81 LEHLEACGVTIEEGPVKRTGALGPILSIYFRDPDGNLIELSNY 123
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 41-161 6.41e-18

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: 75.03  E-value: 6.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  41 HLDHLVLTVKSVPDTIHFYTSVLGMEVVT------FKGNRKALSFGQ-QKFNLHqlgqEFEPKAKHPTSGSAD-LCLITN 112
Cdd:COG0346     2 GLHHVTLRVSDLEASLAFYTDVLGLELVKrtdfgdGGFGHAFLRLGDgTELELF----EAPGAAPAPGGGGLHhLAFRVD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1879460250 113 TpLATVAAHLKVCGVEIEEGPVERsgAVGPiTSLYFRDPDHNLIEVSNY 161
Cdd:COG0346    78 D-LDAAYARLRAAGVEIEGEPRDR--AYGY-RSAYFRDPDGNLIELVEP 122
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
39-158 6.33e-17

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 72.68  E-value: 6.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  39 LSHLDHLVLTVKSVPDTIHFYTSVLGMEVVTFKGNRKALSFGQQKFNLHqLGQEFEPKAKHPTSGSADLCLITNTP--LA 116
Cdd:COG2514     1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEHLLV-LEEAPGAPPRPGAAGLDHVAFRVPSRadLD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1879460250 117 TVAAHLKVCGVEIeEGPVERSGAvgpiTSLYFRDPDHNLIEV 158
Cdd:COG2514    80 AALARLAAAGVPV-EGAVDHGVG----ESLYFRDPDGNLIEL 116
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 58-158 9.63e-12

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


Pssm-ID: 319942  Cd Length: 122  Bit Score: 58.92  E-value: 9.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  58 FYTSVLGMEVVTFKGNRKALSFGQQKFNLHQLGQEFEPKAK-----HPTSGSADLCL-ITNTPLATVAAHLKVCGVEIEE 131
Cdd:cd08354    17 FYEDVLGLKPMLRSGRHAFFRLGPQVLLVFDPGATSKDVRTgevpgHGASGHGHFAFaVPTEELAAWEARLEAKGVPIES 96

                          90       100
                  ....*....|....*....|....*..
gi 1879460250 132 gpVERSGAVGpiTSLYFRDPDHNLIEV 158
Cdd:cd08354    97 --YTQWPEGG--KSLYFRDPAGNLVEL 119
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 44-158 2.97e-10

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: 54.84  E-value: 2.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  44 HLVLTVKSVPDTIHFYTSVLGMEVVTFKGNRKALSFGQQKFnlHQLG-QEFEPKAKHPTSGSADLCLITNTPLATVAAH- 121
Cdd:cd06587     1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGFAFLRLGPG--LRLAlLEGPEPERPGGGGLFHLAFEVDDVDEVDERLr 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1879460250 122 -LKVCGVEIEEGPVERSGAvgpiTSLYFRDPDHNLIEV 158
Cdd:cd06587    79 eAGAEGELVAPPVDDPWGG----RSFYFRDPDGNLIEF 112
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 41-158 4.72e-09

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: 51.54  E-value: 4.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  41 HLDHLVLTVKSVPDTIHFYTSVLGMEVVTFKGNRKALSFGQQKFNLHQLGQEFEPKAKHPTSG---SADLcLITNTPLAT 117
Cdd:cd07255     2 RIGRVTLKVADLERQSAFYQNVIGLSVLKQNASRAYLGVDGKQVLLVLEAIPDAVLAPRSTTGlyhFAIL-LPDRKALGR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1879460250 118 VAAHLkvcgveIEEGPVERSGAVGPITSLYFRDPDHNLIEV 158
Cdd:cd07255    81 ALAHL------AEHGPLIGAADHGVSEAIYLSDPEGNGIEI 115
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
41-158 5.42e-09

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 51.68  E-value: 5.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  41 HLDHLVLTVKSVPDTIHFYTSVLGMEVVTFKGNRKALSFGQQKF----NLHQLGQEFEPKAKHPTSGSADLCLITNTP-- 114
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFlaggRVLELLLNETPPPAAAGFGGHHIAFIAFSVdd 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1879460250 115 LATVAAHLKVCGVEIEEGPveRSGAVGPITSlYFRDPDHNLIEV 158
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREP--GRHGWGGRYS-YFRDPDGNLIEL 121
BphC2-C3-RGP6_C_like cd08348
The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus ...
 42-170 1.93e-07

The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus globerulus P6 BphC2-RGP6 and BphC3-RGP6, and similar proteins. BphC catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, yielding 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid. This is 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. Most type I extradiol dioxygenases are activated by Fe(II). 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. BphC2-RGP6 and BphC3-RGP6 are one-domain dioxygenases, which form hexamers. BphC1-RGP6 has an internal duplication, it is a two-domain dioxygenase which forms octamers, its two domains do not belong to this subfamily.


Pssm-ID: 319936  Cd Length: 137  Bit Score: 47.90  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  42 LDHLVLTVK--SVPDTIHFYTSVLGMEVVTFKGNRKALSFGQQKFNLHQLGQE---FEPKAKHPTSGSADLCLITNT--P 114
Cdd:cd08348     2 LAHFVLRTNpeKFEAMVQWYLDILGARIVARNAKGCFLSFDEEHHRIAIFGAPggaQPPDKRPTRVGLAHIAFTYASldD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1879460250 115 LATVAAHLKVCGVEIEEgPVERsgavGPITSLYFRDPDHNLIEVSNYNQSSSEGSS 170
Cdd:cd08348    82 LARNYAQLKERGIKPVW-PVNH----GVTTSIYYRDPDGNMLEMQVDNFDTPDEAT 132
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 41-158 3.50e-06

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 43.86  E-value: 3.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  41 HLDHLVLTVKSVPDTIHFYTSVLGMEVVTFKGNrkALSFGQQKFNLHQLGqEFEPKAKHPTSGSADLCLITnTPLATVAA 120
Cdd:COG3324     4 TIVWVELPVDDLERAKAFYEEVFGWTFEDDAGP--GGDYAEFDTDGGQVG-GLMPGAEEPGGPGWLLYFAV-DDLDAAVA 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1879460250 121 HLKVCGVEIEEGPVERSGaVGpiTSLYFRDPDHNLIEV 158
Cdd:COG3324    80 RVEAAGGTVLRPPTDIPP-WG--RFAVFRDPEGNRFGL 114
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 42-158 3.61e-06

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: 43.85  E-value: 3.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  42 LDHLVLTVKSVPDTIHFYTSVLGMEVV---TFKGNRKA-----------LSFGQQKFNLHQLgqEFEPKAKHPTSGSADl 107
Cdd:cd07245     1 LDHVALACPDLERARRFYTDVLGLEEVprpPFLKFGGAwlylgggqqihLVVEQNPSELPRP--EHPGRDRHPSFSVPD- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1879460250 108 clitntpLATVAAHLKVCGVEIeegpVERSGAVGPITSLYFRDPDHNLIEV 158
Cdd:cd07245    78 -------LDALKQRLKEAGIPY----TESTSPGGGVTQLFFRDPDGNRLEF 117
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 44-158 2.59e-05

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


Pssm-ID: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 41.55  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  44 HLVLTVKSVPDTIHFYTSVLG---------MEVVTFKGNRKALSFGQqkfnlHQLGQEFEPKAKHPTSGSadLCLITNTP 114
Cdd:cd07264     3 YIVLYVDDFAASLRFYRDVLGlpprflheeGEYAEFDTGETKLALFS-----RKEMARSGGPDRRGSAFE--LGFEVDDV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1879460250 115 LATVAaHLKVCGVEIEEGPVERSgaVGPiTSLYFRDPDHNLIEV 158
Cdd:cd07264    76 EATVE-ELVERGAEFVREPANKP--WGQ-TVAYVRDPDGNLIEI 115
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 42-158 8.82e-05

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: 40.41  E-value: 8.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  42 LDHLVLTVKSVPDTIHFYTSVLGMEVVTfKGNRKA--------LSFGQQKfNLHQlgQEFEPKAKHPTSGsadlclITNT 113
Cdd:cd08363     1 INHITFSVSNLNKSIAFYKDVLDAKLLV-LGEKTAyfdlnglwLALNVQE-DIPR--NEISHSYTHIAFS------IDEE 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1879460250 114 PLATVAAHLKVCGVEIEEGpveRSGAVGPITSLYFRDPDHNLIEV 158
Cdd:cd08363    71 DLDAFKERLKDNGVNILEG---RKRDILEGQSIYFTDPDGHLFEL 112
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 43-159 1.16e-04

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: 39.99  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  43 DHLVLTVKSVPDTIHFYTSVLGMEV--VTFKGNRKALSF--GQQKFNLHQLG-QEFEPKAKHPTS---GSADLCLItntp 114
Cdd:cd08343     1 GHVVLCSPDVEASRDFYTDVLGFRVsdRIVDPGVDGGAFlhCDRGTDHHTVAlAGGPHPGLHHVAfevHDLDDVGR---- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1879460250 115 latVAAHLKVCGVEIEEGPVeRSGaVGPITSLYFRDPDHNLIEVS 159
Cdd:cd08343    77 ---GHDRLREKGYKIEWGPG-RHG-LGSQVFDYWFDPSGNRVEYY 116
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 44-159 2.42e-04

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


Pssm-ID: 319967  Cd Length: 111  Bit Score: 38.84  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  44 HLVLTVKSVPDTIHFYTSVLGMEVVTFKGNRKAL-SFGQQKFNLhQLGQEFEPKAKHptsgsADLCLITNTPLATVAAHL 122
Cdd:cd16360     1 YAELGVPDLEKALEFYTDVLGLQVAKRDGNSVYLrGYEDEHHSL-VLYEAPEAGLKH-----FAFEVASEEDLERAAASL 74

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1879460250 123 KVCGVEIEEGPVERSGAVGpiTSLYFRDPDHNLIEVS 159
Cdd:cd16360    75 TALGCDVTWGPDGEVPGGG--KGFRFQDPSGHLLELF 109
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 44-94 2.25e-03

C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319964  Cd Length: 114  Bit Score: 35.99  E-value: 2.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1879460250  44 HLVLTVKSVPDTIHFYTSVLGMEVVTFKGNRKALSFG--QQKFNLHQLGQEFE 94
Cdd:cd16357     1 KVSLAVSDLEKSIDYWSDLLGMKVFEKSEKSALLGYGedQAKLELVDIPEPVD 53
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
46-159 4.23e-03

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 35.22  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  46 VLTVKSVPDTIHFYTSVLGMEV---VTFKGNRKA---LSFGQQKFNLHqlgqEFEPKAKHPTSGSADLCLITNTPLATVA 119
Cdd:COG2764     5 YLVVDDAEEALEFYEDVFGFEVvfrMTDPDGKIMhaeLRIGGSVLMLS----DAPPDSPAAEGNGVSLSLYVDDVDALFA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1879460250 120 AhLKVCGVEIEEGPVE-----RSGAVgpitslyfRDPDHNLIEVS 159
Cdd:COG2764    81 R-LVAAGATVVMPLQDtfwgdRFGMV--------RDPFGVLWMIN 116
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 42-101 4.54e-03

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


Pssm-ID: 272886  Cd Length: 150  Bit Score: 35.94  E-value: 4.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  42 LDHLVLTVKSVPDTIHFYTSVLGMEVVtfkgnrKALSFGQQKFNLHQLGqeFEPKAKHPT 101
Cdd:TIGR00068  18 LLHTMLRVGDLDKSLDFYTEVLGMKLL------RKRDFPEMKFSLAFLG--YGDETSAAV 69
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 36-68 6.70e-03

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: 36.02  E-value: 6.70e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1879460250  36 PVGLSHLDHLVLTVK--SVPDTIHFYTSVLGMEVV 68
Cdd:COG3185   141 GAGLTRIDHIGIAVPrgDLDEWVLFYEDVLGFEEI 175
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 39-159 6.71e-03

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: 34.92  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879460250  39 LSHLDHLVLTVKSVPDTIHFYTSVLGMEVVTFKGNRKALSFGQQKFNLHQLGQEFEPKAKHPTSGSAdlcliTNTPLATV 118
Cdd:cd08362     1 VTHLRYVALGVPDLAAEREFYTEVWGLEEVAEDDDVVYLRAEGSEHHVLRLRQSDENRLDLIAFAAA-----TRADVDAL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1879460250 119 AAHLKVCGVEI--EEGPVERSGAvGpiTSLYFRDPDHNLIEVS 159
Cdd:cd08362    76 AARLAAAGVRIlsEPGPLDDPGG-G--YGFRFFDPDGRTIEVS 115
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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