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Conserved domains on  [gi|1958807075|ref|XP_006256768|]
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glyoxalase domain-containing protein 5 isoform X2 [Rattus norvegicus]

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 ...
 38-127 1.33e-52

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: 161.63  E-value: 1.33e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807075  38 GDRKALCFGDQKFNLHEVGKEFDPKAAHPIPGSLDVCLITETPLEEVMKRLKAFDVPIEEGPVSRTGAKGPILSIYFRDP 117
Cdd:cd07253    34 EGRKALRFGNQKINLHQKGKEFEPKASAPTPGSADLCFITETPIDEVLEHLEACGVTIEEGPVKRTGALGPILSIYFRDP 113

                          90
                  ....*....|
gi 1958807075 118 DRNLIEVSNY 127
Cdd:cd07253   114 DGNLIELSNY 123
 
Name Accession Description Interval E-value
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 38-127 1.33e-52

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: 161.63  E-value: 1.33e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807075  38 GDRKALCFGDQKFNLHEVGKEFDPKAAHPIPGSLDVCLITETPLEEVMKRLKAFDVPIEEGPVSRTGAKGPILSIYFRDP 117
Cdd:cd07253    34 EGRKALRFGNQKINLHQKGKEFEPKASAPTPGSADLCFITETPIDEVLEHLEACGVTIEEGPVKRTGALGPILSIYFRDP 113

                          90
                  ....*....|
gi 1958807075 118 DRNLIEVSNY 127
Cdd:cd07253   114 DGNLIELSNY 123
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 16-127 3.49e-09

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: 51.15  E-value: 3.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807075  16 LDFestYCSI--MKIGWSSDPSTQGDRKA-LCFGD-QKFNLHEvgkeFDPKAAHPIPGSLD-VCLITETpLEEVMKRLKA 90
Cdd:COG0346    17 LAF---YTDVlgLELVKRTDFGDGGFGHAfLRLGDgTELELFE----APGAAPAPGGGGLHhLAFRVDD-LDAAYARLRA 88

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958807075  91 FDVPIEEGPvsRTGAKGPIlSIYFRDPDRNLIEVSNY 127
Cdd:COG0346    89 AGVEIEGEP--RDRAYGYR-SAYFRDPDGNLIELVEP 122
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
53-124 5.30e-03

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 34.35  E-value: 5.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807075  53 HEVGKEFDPKAAHPIPGSLDVCLITETP--LEEVMKRLKAFDVPIEEGPvSRTGAKGpiLSIYFRDPDRNLIEV 124
Cdd:pfam00903  51 LELLLNETPPPAAAGFGGHHIAFIAFSVddVDAAYDRLKAAGVEIVREP-GRHGWGG--RYSYFRDPDGNLIEL 121
PRK04101 PRK04101
metallothiol transferase FosB;
76-124 5.84e-03

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 34.54  E-value: 5.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958807075  76 ITETPLEEVMKRLKAFDVPIEEGpvsRTGAKGPILSIYFRDPDRNLIEV 124
Cdd:PRK04101   71 IEEEDFDHWYQRLKENDVNILPG---RERDERDKKSIYFTDPDGHKFEF 116
 
Name Accession Description Interval E-value
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 38-127 1.33e-52

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: 161.63  E-value: 1.33e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807075  38 GDRKALCFGDQKFNLHEVGKEFDPKAAHPIPGSLDVCLITETPLEEVMKRLKAFDVPIEEGPVSRTGAKGPILSIYFRDP 117
Cdd:cd07253    34 EGRKALRFGNQKINLHQKGKEFEPKASAPTPGSADLCFITETPIDEVLEHLEACGVTIEEGPVKRTGALGPILSIYFRDP 113

                          90
                  ....*....|
gi 1958807075 118 DRNLIEVSNY 127
Cdd:cd07253   114 DGNLIELSNY 123
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 16-127 3.49e-09

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: 51.15  E-value: 3.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807075  16 LDFestYCSI--MKIGWSSDPSTQGDRKA-LCFGD-QKFNLHEvgkeFDPKAAHPIPGSLD-VCLITETpLEEVMKRLKA 90
Cdd:COG0346    17 LAF---YTDVlgLELVKRTDFGDGGFGHAfLRLGDgTELELFE----APGAAPAPGGGGLHhLAFRVDD-LDAAYARLRA 88

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958807075  91 FDVPIEEGPvsRTGAKGPIlSIYFRDPDRNLIEVSNY 127
Cdd:COG0346    89 AGVEIEGEP--RDRAYGYR-SAYFRDPDGNLIELVEP 122
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
81-124 6.84e-07

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 45.33  E-value: 6.84e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1958807075  81 LEEVMKRLKAFDVPIEeGPVSRTGAKgpilSIYFRDPDRNLIEV 124
Cdd:COG2514    78 LDAALARLAAAGVPVE-GAVDHGVGE----SLYFRDPDGNLIEL 116
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 76-124 1.25e-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: 41.57  E-value: 1.25e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958807075  76 ITETPLEEVMKRLKAFDVPIEEGpvsRTGAKGPILSIYFRDPDRNLIEV 124
Cdd:cd08363    67 IDEEDLDAFKERLKDNGVNILEG---RKRDILEGQSIYFTDPDGHLFEL 112
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 33-124 1.99e-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: 319942  Cd Length: 122  Bit Score: 41.20  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807075  33 DPSTQGDRKAlCF--GDQKFNLHEVGKEFDPKAAHPIP-----GSLDVCL-ITETPLEEVMKRLKAFDVPIEEgpVSRTG 104
Cdd:cd08354    25 KPMLRSGRHA-FFrlGPQVLLVFDPGATSKDVRTGEVPghgasGHGHFAFaVPTEELAAWEARLEAKGVPIES--YTQWP 101

                          90       100
                  ....*....|....*....|
gi 1958807075 105 AKGPilSIYFRDPDRNLIEV 124
Cdd:cd08354   102 EGGK--SLYFRDPAGNLVEL 119
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 44-124 3.23e-03

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: 34.81  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807075  44 CFGDQKFNLHEVGKEFDPKAahpiPGSLDVCLITETPLEEVMK--RLKAFDVPIEEGPVSRTGAKgpilSIYFRDPDRNL 121
Cdd:cd06587    38 LGPGLRLALLEGPEPERPGG----GGLFHLAFEVDDVDEVDERlrEAGAEGELVAPPVDDPWGGR----SFYFRDPDGNL 109


                  ...
gi 1958807075 122 IEV 124
Cdd:cd06587   110 IEF 112
FosX cd08364
fosfomycin resistant protein subfamily FosX; This subfamily family contains FosX, a fosfomycin ...
 76-123 4.39e-03

fosfomycin resistant protein subfamily FosX; This subfamily family contains FosX, a fosfomycin resistant protein. FosX is a Mn(II)-dependent fosfomycin-specific epoxide hydrolase. Fosfomycin inhibits the enzyme UDP-Nacetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosX catalyzes the addition of a water molecule to the C1 position of the antibiotic with inversion of the configuration at C1 in the presence of Mn(II). The hydrated fosfomycin loses the inhibition activity. FosX is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319952  Cd Length: 130  Bit Score: 34.94  E-value: 4.39e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958807075  76 ITETPLEEVMKRLKAFDVPIEEgPVSRTGAKGpiLSIYFRDPDRNLIE 123
Cdd:cd08364    73 VSEGDLDEYRARIKKLGLEIRP-PRSRVQGEG--RSLYFYDFDNHLFE 117
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
53-124 5.30e-03

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 34.35  E-value: 5.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807075  53 HEVGKEFDPKAAHPIPGSLDVCLITETP--LEEVMKRLKAFDVPIEEGPvSRTGAKGpiLSIYFRDPDRNLIEV 124
Cdd:pfam00903  51 LELLLNETPPPAAAGFGGHHIAFIAFSVddVDAAYDRLKAAGVEIVREP-GRHGWGG--RYSYFRDPDGNLIEL 121
PRK04101 PRK04101
metallothiol transferase FosB;
76-124 5.84e-03

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 34.54  E-value: 5.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958807075  76 ITETPLEEVMKRLKAFDVPIEEGpvsRTGAKGPILSIYFRDPDRNLIEV 124
Cdd:PRK04101   71 IEEEDFDHWYQRLKENDVNILPG---RERDERDKKSIYFTDPDGHKFEF 116
 
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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