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Conserved domains on  [gi|1955885588|ref|NP_001376662|]
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glyoxalase domain-containing protein 4 isoform 10 [Homo sapiens]

Protein Classification

glyoxalase domain-containing protein 4( domain architecture ID 11579539)

glyoxalase domain-containing protein 4 is a vicinal oxygen chelate (VOC) family protein and may use a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms; contains tandem repeats

PubMed:  11076500|21820381

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GLOD4_N cd08358
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 4-130 1.65e-96

N-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: 319946  Cd Length: 127  Bit Score: 279.25  E-value: 1.65e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588   4 RRALHFVFKVGNRFQTARFYRDVLGMKVLRHEEFEEGCKAACNGPYDGKWSKTMVGFGPEDDHFVAELTYNYGVGDYKLG 83
Cdd:cd08358     1 RRALHFVFKVGDRNKTIKFYREILGMKVLRHEEFEEGCKAACNGPYDGKWSKTMVGYGPEDDHFVVELTYNYGIGDYELG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1955885588  84 NDFMGITLASSQAVSNARKLEWPLTEVAEGVFETEAPGGYKFYLQNR 130
Cdd:cd08358    81 NDFLGITIHSKQAVSRAKKHNWPVTQVGDGVYEVKAPGGYKFYLIDK 127
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 140-236 3.80e-51

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: 163.50  E-value: 3.80e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588 140 KVTLAVSDLQKSLNYWCNLLGMKIYEKDEekQRALLGYADNQCKLELQGVKGGVDHAAAFGRIAFSCPQKELPDLEDLMK 219
Cdd:cd16357     1 KVSLAVSDLEKSIDYWSDLLGMKVFEKSE--KSALLGYGEDQAKLELVDIPEPVDHGTAFGRIAFSCPADELPPIEEKVK 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1955885588 220 RENQKILTPL-------------------DGHEICF 236
Cdd:cd16357    79 AAGQTILTPLvsldtpgkatvqvviladpDGHEICF 114
 
Name Accession Description Interval E-value
GLOD4_N cd08358
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 4-130 1.65e-96

N-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: 319946  Cd Length: 127  Bit Score: 279.25  E-value: 1.65e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588   4 RRALHFVFKVGNRFQTARFYRDVLGMKVLRHEEFEEGCKAACNGPYDGKWSKTMVGFGPEDDHFVAELTYNYGVGDYKLG 83
Cdd:cd08358     1 RRALHFVFKVGDRNKTIKFYREILGMKVLRHEEFEEGCKAACNGPYDGKWSKTMVGYGPEDDHFVVELTYNYGIGDYELG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1955885588  84 NDFMGITLASSQAVSNARKLEWPLTEVAEGVFETEAPGGYKFYLQNR 130
Cdd:cd08358    81 NDFLGITIHSKQAVSRAKKHNWPVTQVGDGVYEVKAPGGYKFYLIDK 127
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 140-236 3.80e-51

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: 163.50  E-value: 3.80e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588 140 KVTLAVSDLQKSLNYWCNLLGMKIYEKDEekQRALLGYADNQCKLELQGVKGGVDHAAAFGRIAFSCPQKELPDLEDLMK 219
Cdd:cd16357     1 KVSLAVSDLEKSIDYWSDLLGMKVFEKSE--KSALLGYGEDQAKLELVDIPEPVDHGTAFGRIAFSCPADELPPIEEKVK 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1955885588 220 RENQKILTPL-------------------DGHEICF 236
Cdd:cd16357    79 AAGQTILTPLvsldtpgkatvqvviladpDGHEICF 114
PLN02300 PLN02300
lactoylglutathione lyase
 4-205 2.39e-30

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 114.88  E-value: 2.39e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588   4 RRALHFVFKVGNRFQTARFYRDVLGMKVLRHEEFEEGckaacngpydgKWSKTMVGFGPEDDHFVAELTYNYGVGDYKLG 83
Cdd:PLN02300   23 RRMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEE-----------KYTNAFLGYGPEDSNFVVELTYNYGVDKYDIG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588  84 NDF--MGITLASSQAVSNARKlewpltevAEGVFETEAPG----------------GYKFYLQNRSlPQSDPVLKVTLAV 145
Cdd:PLN02300   92 TGFghFGIAVEDVAKTVELVK--------AKGGKVTREPGpvkggksviafvkdpdGYKFELIQRG-PTPEPLCQVMLRV 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1955885588 146 SDLQKSLNYWCNLLGMKIYEKDEEKQR----ALLGYA--DNQCKLELQ---GVKgGVDHAAAFGRIAFS 205
Cdd:PLN02300  163 GDLDRSIKFYEKAFGMKLLRKRDNPEYkytiAMMGYGpeDKTTVLELTynyGVT-EYTKGNAYAQIAIG 230
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 4-135 3.13e-20

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: 84.47  E-value: 3.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588   4 RRALHFVFKVGNRFQTARFYRDVLGMKVLRHEEFEEGckaacngpydgKWSKTMVGFGPEDDHFVAELTYNYGVGDYKLG 83
Cdd:TIGR00068  16 RRLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEM-----------KFSLAFLGYGDETSAAVIELTHNWGTEKYDLG 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955885588  84 NDFMGITLASSQAVSNARKLE----------WPLTEVAEGVFETEAPGGYKF-YLQNRSLPQS 135
Cdd:TIGR00068  85 NGFGHIAIGVDDVYKACERVRalggnvvrepGPVKGGTTVIAFVEDPDGYKIeLIQRKSTKDG 147
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
141-252 1.95e-05

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 43.41  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588 141 VTLAVSDLQKSLNYWCNLLGMKiyEKDEEKQRALLGYADNQCKLELQGVKGGVDHAAAFG--RIAFSCPQKElpDLEDLM 218
Cdd:COG2514     7 VTLRVRDLERSAAFYTDVLGLE--VVEREGGRVYLRADGGEHLLVLEEAPGAPPRPGAAGldHVAFRVPSRA--DLDAAL 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1955885588 219 KR-ENQKIltPLDGHEICFVGdEA--FRelskmDPEG 252
Cdd:COG2514    83 ARlAAAGV--PVEGAVDHGVG-ESlyFR-----DPDG 111
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 4-92 5.91e-04

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: 38.82  E-value: 5.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588   4 RRALHFVFKVGNRFQTARFYRDVLGMKVLRHEEFEEGckaacngpydgkwSKTMVGFGPEDDHFVaELTYNYGVGDYKLG 83
Cdd:COG0346     1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDG-------------GFGHAFLRLGDGTEL-ELFEAPGAAPAPGG 66


                  ....*....
gi 1955885588  84 NDFMGITLA 92
Cdd:COG0346    67 GGLHHLAFR 75
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
141-236 1.53e-03

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 37.81  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588 141 VTLAVSDLQKSLNYWCNLLGMKI---YEKDEEKQRALLGYADNQCKLEL---QGVKGGVDHAAAFGrIAFSCPQKElpDL 214
Cdd:pfam00903   5 VALRVGDLEKSLDFYTDVLGFKLveeTDAGEEGGLRSAFFLAGGRVLELllnETPPPAAAGFGGHH-IAFIAFSVD--DV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1955885588 215 E---DLMKRENQKILTPL---------------DGHEICF 236
Cdd:pfam00903  82 DaayDRLKAAGVEIVREPgrhgwggrysyfrdpDGNLIEL 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
8-89 1.67e-03

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 37.43  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588   8 HFVFKVGNRFQTARFYRDVLGMKVLRHEEFEEGckaacngpydgkwsKTMVGFGPEDDHFVAELTYNYGVGDYKLGNDFM 87
Cdd:pfam00903   4 HVALRVGDLEKSLDFYTDVLGFKLVEETDAGEE--------------GGLRSAFFLAGGRVLELLLNETPPPAAAGFGGH 69


                  ..
gi 1955885588  88 GI 89
Cdd:pfam00903  70 HI 71
 
Name Accession Description Interval E-value
GLOD4_N cd08358
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 4-130 1.65e-96

N-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: 319946  Cd Length: 127  Bit Score: 279.25  E-value: 1.65e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588   4 RRALHFVFKVGNRFQTARFYRDVLGMKVLRHEEFEEGCKAACNGPYDGKWSKTMVGFGPEDDHFVAELTYNYGVGDYKLG 83
Cdd:cd08358     1 RRALHFVFKVGDRNKTIKFYREILGMKVLRHEEFEEGCKAACNGPYDGKWSKTMVGYGPEDDHFVVELTYNYGIGDYELG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1955885588  84 NDFMGITLASSQAVSNARKLEWPLTEVAEGVFETEAPGGYKFYLQNR 130
Cdd:cd08358    81 NDFLGITIHSKQAVSRAKKHNWPVTQVGDGVYEVKAPGGYKFYLIDK 127
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 140-236 3.80e-51

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: 163.50  E-value: 3.80e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588 140 KVTLAVSDLQKSLNYWCNLLGMKIYEKDEekQRALLGYADNQCKLELQGVKGGVDHAAAFGRIAFSCPQKELPDLEDLMK 219
Cdd:cd16357     1 KVSLAVSDLEKSIDYWSDLLGMKVFEKSE--KSALLGYGEDQAKLELVDIPEPVDHGTAFGRIAFSCPADELPPIEEKVK 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1955885588 220 RENQKILTPL-------------------DGHEICF 236
Cdd:cd16357    79 AAGQTILTPLvsldtpgkatvqvviladpDGHEICF 114
PLN02300 PLN02300
lactoylglutathione lyase
 4-205 2.39e-30

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 114.88  E-value: 2.39e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588   4 RRALHFVFKVGNRFQTARFYRDVLGMKVLRHEEFEEGckaacngpydgKWSKTMVGFGPEDDHFVAELTYNYGVGDYKLG 83
Cdd:PLN02300   23 RRMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEE-----------KYTNAFLGYGPEDSNFVVELTYNYGVDKYDIG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588  84 NDF--MGITLASSQAVSNARKlewpltevAEGVFETEAPG----------------GYKFYLQNRSlPQSDPVLKVTLAV 145
Cdd:PLN02300   92 TGFghFGIAVEDVAKTVELVK--------AKGGKVTREPGpvkggksviafvkdpdGYKFELIQRG-PTPEPLCQVMLRV 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1955885588 146 SDLQKSLNYWCNLLGMKIYEKDEEKQR----ALLGYA--DNQCKLELQ---GVKgGVDHAAAFGRIAFS 205
Cdd:PLN02300  163 GDLDRSIKFYEKAFGMKLLRKRDNPEYkytiAMMGYGpeDKTTVLELTynyGVT-EYTKGNAYAQIAIG 230
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 4-135 3.13e-20

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: 84.47  E-value: 3.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588   4 RRALHFVFKVGNRFQTARFYRDVLGMKVLRHEEFEEGckaacngpydgKWSKTMVGFGPEDDHFVAELTYNYGVGDYKLG 83
Cdd:TIGR00068  16 RRLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEM-----------KFSLAFLGYGDETSAAVIELTHNWGTEKYDLG 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955885588  84 NDFMGITLASSQAVSNARKLE----------WPLTEVAEGVFETEAPGGYKF-YLQNRSLPQS 135
Cdd:TIGR00068  85 NGFGHIAIGVDDVYKACERVRalggnvvrepGPVKGGTTVIAFVEDPDGYKIeLIQRKSTKDG 147
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 7-127 6.73e-20

Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other prokaryotic glyoxalase I that uses nickel as cofactor. Glyoxalase I (also known as lactoylglutathione lyase; EC 4.4.1.5) is part of the glyoxalase system, a two-step system for detoxifying methylglyoxal, a side product of glycolysis. This system is responsible for the conversion of reactive, acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids and involves 2 enzymes, glyoxalase I and II. Glyoxalase I catalyses an intramolecular redox reaction of the hemithioacetal (formed from methylglyoxal and glutathione) to form the thioester, S-D-lactoylglutathione. This reaction involves the transfer of two hydrogen atoms from C1 to C2 of the methylglyoxal, and proceeds via an ene-diol intermediate. Glyoxalase I has a requirement for bound metal ions for catalysis. Eukaryotic glyoxalase I prefers the divalent cation zinc as cofactor, whereas Escherichia coil and other prokaryotic glyoxalase I uses nickel. However, eukaryotic Trypanosomatid parasites also use nickel as a cofactor, which could possibly be explained by acquiring their GLOI gene by horizontal gene transfer. Human glyoxalase I is a two-domain enzyme and it has the structure of a domain-swapped dimer with two active sites located at the dimer interface. In yeast, in various plants, insects and Plasmodia, glyoxalase I is four-domain, possibly the result of a further gene duplication and an additional gene fusing event.


Pssm-ID: 319965 [Multi-domain]  Cd Length: 122  Bit Score: 82.83  E-value: 6.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588   7 LHFVFKVGNRFQTARFYRDVLGMKVLRHEEFEEGckaacngpydgKWSKTMVGFGPEDDHFVAELTYNYGVGDYKLGNDF 86
Cdd:cd16358     2 LHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEG-----------KYTLAFVGYGDEDENTVLELTYNWGVDKYDLGTAY 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1955885588  87 MGITLASS---QAVSNARKLEWPLTEVAEGVFE-------TEAPGGYKFYL 127
Cdd:cd16358    71 GHIAIGVEdvyETCERIRKKGGKVTREPGPMKGgttviafVEDPDGYKIEL 121
PRK10291 PRK10291
glyoxalase I; Provisional
 10-127 1.88e-11

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 60.42  E-value: 1.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588  10 VFKVGNRFQTARFYRDVLGMKVLRHEEfeegckaacNGPYdgKWSKTMVGFGPEDDHFVAELTYNYGVGDYKLGNDFMGI 89
Cdd:PRK10291    1 MLRVGDLQRSIDFYTNVLGMKLLRTSE---------NPEY--KYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1955885588  90 TLASSQAVS----------NARKLEWPLTEVAEGVFETEAPGGYKFYL 127
Cdd:PRK10291   70 ALSVDNAAEacekirqnggNVTREAGPVKGGTTVIAFVEDPDGYKIEL 117
PLN02300 PLN02300
lactoylglutathione lyase
 11-93 6.95e-10

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 58.25  E-value: 6.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588  11 FKVGNRFQTARFYRDVLGMKVLRHEEFEEGckaacngpydgKWSKTMVGFGPEDDHFVAELTYNYGVGDYKLGNDFMGIT 90
Cdd:PLN02300  160 LRVGDLDRSIKFYEKAFGMKLLRKRDNPEY-----------KYTIAMMGYGPEDKTTVLELTYNYGVTEYTKGNAYAQIA 228


                  ...
gi 1955885588  91 LAS 93
Cdd:PLN02300  229 IGT 231
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 141-236 3.46e-07

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: 47.90  E-value: 3.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588 141 VTLAVSDLQKSLNYWCNLLGMKIYEKDEEKQRALLGYADNQCkLELQGVKGGVD-HAAAFGRIAFSCPQK-ELPDLEDLM 218
Cdd:cd06587     2 VALRVPDLDASVAFYEEVLGFEVVSRNEGGGFAFLRLGPGLR-LALLEGPEPERpGGGGLFHLAFEVDDVdEVDERLREA 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1955885588 219 KRENQKILTPL--------------DGHEICF 236
Cdd:cd06587    81 GAEGELVAPPVddpwggrsfyfrdpDGNLIEF 112
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
141-252 1.95e-05

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 43.41  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588 141 VTLAVSDLQKSLNYWCNLLGMKiyEKDEEKQRALLGYADNQCKLELQGVKGGVDHAAAFG--RIAFSCPQKElpDLEDLM 218
Cdd:COG2514     7 VTLRVRDLERSAAFYTDVLGLE--VVEREGGRVYLRADGGEHLLVLEEAPGAPPRPGAAGldHVAFRVPSRA--DLDAAL 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1955885588 219 KR-ENQKIltPLDGHEICFVGdEA--FRelskmDPEG 252
Cdd:COG2514    83 ARlAAAGV--PVEGAVDHGVG-ESlyFR-----DPDG 111
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 141-220 2.20e-05

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: 43.06  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588 141 VTLAVSDLQKSLNYWCNLLGMKIYEK----DEEKQRALLGYADNQcKLELQGVKGG--VDHAAAFGRIAFSCpqkelPDL 214
Cdd:COG0346     6 VTLRVSDLEASLAFYTDVLGLELVKRtdfgDGGFGHAFLRLGDGT-ELELFEAPGAapAPGGGGLHHLAFRV-----DDL 79


                  ....*.
gi 1955885588 215 EDLMKR 220
Cdd:COG0346    80 DAAYAR 85
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 138-203 8.20e-05

Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other prokaryotic glyoxalase I that uses nickel as cofactor. Glyoxalase I (also known as lactoylglutathione lyase; EC 4.4.1.5) is part of the glyoxalase system, a two-step system for detoxifying methylglyoxal, a side product of glycolysis. This system is responsible for the conversion of reactive, acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids and involves 2 enzymes, glyoxalase I and II. Glyoxalase I catalyses an intramolecular redox reaction of the hemithioacetal (formed from methylglyoxal and glutathione) to form the thioester, S-D-lactoylglutathione. This reaction involves the transfer of two hydrogen atoms from C1 to C2 of the methylglyoxal, and proceeds via an ene-diol intermediate. Glyoxalase I has a requirement for bound metal ions for catalysis. Eukaryotic glyoxalase I prefers the divalent cation zinc as cofactor, whereas Escherichia coil and other prokaryotic glyoxalase I uses nickel. However, eukaryotic Trypanosomatid parasites also use nickel as a cofactor, which could possibly be explained by acquiring their GLOI gene by horizontal gene transfer. Human glyoxalase I is a two-domain enzyme and it has the structure of a domain-swapped dimer with two active sites located at the dimer interface. In yeast, in various plants, insects and Plasmodia, glyoxalase I is four-domain, possibly the result of a further gene duplication and an additional gene fusing event.


Pssm-ID: 319965 [Multi-domain]  Cd Length: 122  Bit Score: 41.23  E-value: 8.20e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955885588 138 VLKVTLAVSDLQKSLNYWCNLLGMKIYEK----DEEKQRALLGYAD--NQCKLELQ---GVKgGVDHAAAFGRIA 203
Cdd:cd16358     1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKrdypEGKYTLAFVGYGDedENTVLELTynwGVD-KYDLGTAYGHIA 74
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 8-128 1.44e-04

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: 40.59  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588   8 HFVFKVGNRFQTARFYRDVLGMKVLRHEEFEEGCkaacngpydgkwsktMVGFGPeddHFVAELTYNYGVGDYKL-GNDF 86
Cdd:cd06587     1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGFA---------------FLRLGP---GLRLALLEGPEPERPGGgGLFH 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1955885588  87 MGITLASSQAVSnARKLEWPLTEVAEGVFETEAPGGYKFYLQ 128
Cdd:cd06587    63 LAFEVDDVDEVD-ERLREAGAEGELVAPPVDDPWGGRSFYFR 103
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 21-85 2.67e-04

Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that prefers the divalent cation zinc as cofactor. Glyoxalase I (also known as lactoylglutathione lyase; EC 4.4.1.5) is part of the glyoxalase system, a two-step system for detoxifying methylglyoxal, a side product of glycolysis. This system is responsible for the conversion of reactive, acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids and involves 2 enzymes, glyoxalase I and II. Glyoxalase I catalyses an intramolecular redox reaction of the hemithioacetal (formed from methylglyoxal and glutathione) to form the thioester, S-D-lactoylglutathione. This reaction involves the transfer of two hydrogen atoms from C1 to C2 of the methylglyoxal, and proceeds via an ene-diol intermediate. Glyoxalase I has a requirement for bound metal ions for catalysis. Eukaryotic glyoxalase I prefers the divalent cation zinc as cofactor, whereas Escherichia coil and other prokaryotic glyoxalase I uses nickel. However, eukaryotic Trypanosomatid parasites also use nickel as a cofactor, which could possibly be explained by acquiring their GLOI gene by horizontal gene transfer. Human glyoxalase I is a two-domain enzyme and it has the structure of a domain-swapped dimer with two active sites located at the dimer interface. In yeast, in various plants, insects and Plasmodia, glyoxalase I is four-domain, possibly the result of a further gene duplication and an additional gene fusing event.


Pssm-ID: 319900 [Multi-domain]  Cd Length: 142  Bit Score: 40.39  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588  21 RFYRDVLGMKVLRHEEFEEgckaacngpydGKWSKTMVGFGPEDD-------------HFVAELTYNYGVGD-----YKL 82
Cdd:cd07233    16 KFYTEVLGMKLLRKKDFPE-----------MKFSLYFLGYEDPKDipkdprtawvfsrEGTLELTHNWGTENdedpvYHN 84


                  ...
gi 1955885588  83 GND 85
Cdd:cd07233    85 GNS 87
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 141-162 5.08e-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: 39.19  E-value: 5.08e-04
                          10        20
                  ....*....|....*....|..
gi 1955885588 141 VTLAVSDLQKSLNYWCNLLGMK 162
Cdd:cd07244     5 ITLAVSDLERSLAFYVDLLGFK 26
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 4-92 5.91e-04

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: 38.82  E-value: 5.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588   4 RRALHFVFKVGNRFQTARFYRDVLGMKVLRHEEFEEGckaacngpydgkwSKTMVGFGPEDDHFVaELTYNYGVGDYKLG 83
Cdd:COG0346     1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDG-------------GFGHAFLRLGDGTEL-ELFEAPGAAPAPGG 66


                  ....*....
gi 1955885588  84 NDFMGITLA 92
Cdd:COG0346    67 GGLHHLAFR 75
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
141-236 1.53e-03

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 37.81  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588 141 VTLAVSDLQKSLNYWCNLLGMKI---YEKDEEKQRALLGYADNQCKLEL---QGVKGGVDHAAAFGrIAFSCPQKElpDL 214
Cdd:pfam00903   5 VALRVGDLEKSLDFYTDVLGFKLveeTDAGEEGGLRSAFFLAGGRVLELllnETPPPAAAGFGGHH-IAFIAFSVD--DV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1955885588 215 E---DLMKRENQKILTPL---------------DGHEICF 236
Cdd:pfam00903  82 DaayDRLKAAGVEIVREPgrhgwggrysyfrdpDGNLIEL 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
8-89 1.67e-03

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 37.43  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885588   8 HFVFKVGNRFQTARFYRDVLGMKVLRHEEFEEGckaacngpydgkwsKTMVGFGPEDDHFVAELTYNYGVGDYKLGNDFM 87
Cdd:pfam00903   4 HVALRVGDLEKSLDFYTDVLGFKLVEETDAGEE--------------GGLRSAFFLAGGRVLELLLNETPPPAAAGFGGH 69


                  ..
gi 1955885588  88 GI 89
Cdd:pfam00903  70 HI 71
 
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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