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Conserved domains on  [gi|1955885167|ref|NP_001376655|]
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glyoxalase domain-containing protein 4 isoform 6 [Homo sapiens]

Protein Classification

VOC family protein( domain architecture ID 11675439)

vicinal oxygen chelate (VOC) family protein uses a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms; similar to Homo sapiens glyoxalase domain-containing protein 4

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 177-292 2.19e-74

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: 224.74  E-value: 2.19e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167 177 KVTLAVSDLQKSLNYWCNLLGMKIYEKDEekQRALLGYADNQCKLELQGVKGGVDHAAAFGRIAFSCPQKELPDLEDLMK 256
Cdd:cd16357     1 KVSLAVSDLEKSIDYWSDLLGMKVFEKSE--KSALLGYGEDQAKLELVDIPEPVDHGTAFGRIAFSCPADELPPIEEKVK 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1955885167 257 RENQKILTPLVSLDTPGKATVQVVILADPDGHEICF 292
Cdd:cd16357    79 AAGQTILTPLVSLDTPGKATVQVVILADPDGHEICF 114
VOC super family cl14632
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 4-167 1.15e-72

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.


The actual alignment was detected with superfamily member cd08358:

Pssm-ID: 472697  Cd Length: 127  Bit Score: 220.70  E-value: 1.15e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167   4 RRALHFVFKVGNRFQTARFYRDVLGMKV-------ESCSVArleCSGaisahcklslpgshhspasasrvagttgsdytr 76
Cdd:cd08358     1 RRALHFVFKVGDRNKTIKFYREILGMKVlrheefeEGCKAA---CNG--------------------------------- 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167  77 itedsfskPYDGKWSKTMVGFGPEDDHFVAELTYNYGVGDYKLGNDFMGITLASSQAVSNARKLEWPLTEVAEGVFETEA 156
Cdd:cd08358    45 --------PYDGKWSKTMVGYGPEDDHFVVELTYNYGIGDYELGNDFLGITIHSKQAVSRAKKHNWPVTQVGDGVYEVKA 116

                         170
                  ....*....|.
gi 1955885167 157 PGGYKFYLQNR 167
Cdd:cd08358   117 PGGYKFYLIDK 127
 
Name Accession Description Interval E-value
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 177-292 2.19e-74

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: 224.74  E-value: 2.19e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167 177 KVTLAVSDLQKSLNYWCNLLGMKIYEKDEekQRALLGYADNQCKLELQGVKGGVDHAAAFGRIAFSCPQKELPDLEDLMK 256
Cdd:cd16357     1 KVSLAVSDLEKSIDYWSDLLGMKVFEKSE--KSALLGYGEDQAKLELVDIPEPVDHGTAFGRIAFSCPADELPPIEEKVK 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1955885167 257 RENQKILTPLVSLDTPGKATVQVVILADPDGHEICF 292
Cdd:cd16357    79 AAGQTILTPLVSLDTPGKATVQVVILADPDGHEICF 114
GLOD4_N cd08358
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 4-167 1.15e-72

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: 220.70  E-value: 1.15e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167   4 RRALHFVFKVGNRFQTARFYRDVLGMKV-------ESCSVArleCSGaisahcklslpgshhspasasrvagttgsdytr 76
Cdd:cd08358     1 RRALHFVFKVGDRNKTIKFYREILGMKVlrheefeEGCKAA---CNG--------------------------------- 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167  77 itedsfskPYDGKWSKTMVGFGPEDDHFVAELTYNYGVGDYKLGNDFMGITLASSQAVSNARKLEWPLTEVAEGVFETEA 156
Cdd:cd08358    45 --------PYDGKWSKTMVGYGPEDDHFVVELTYNYGIGDYELGNDFLGITIHSKQAVSRAKKHNWPVTQVGDGVYEVKA 116

                         170
                  ....*....|.
gi 1955885167 157 PGGYKFYLQNR 167
Cdd:cd08358   117 PGGYKFYLIDK 127
PLN02300 PLN02300
lactoylglutathione lyase
 4-301 1.46e-24

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 101.01  E-value: 1.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167   4 RRALHFVFKVGNRFQTARFYRDVLGMKVEScsvarlecsgaisahcKLSLPgshhspasasrvagttgsdytritEDsfs 83
Cdd:PLN02300   23 RRMLHVVYRVGDLDRTIKFYTECLGMKLLR----------------KRDIP------------------------EE--- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167  84 kpydgKWSKTMVGFGPEDDHFVAELTYNYGVGDYKLGNDF--MGItlassqAVSNARKLewpLTEV-AEGVFETEAPG-- 158
Cdd:PLN02300   60 -----KYTNAFLGYGPEDSNFVVELTYNYGVDKYDIGTGFghFGI------AVEDVAKT---VELVkAKGGKVTREPGpv 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167 159 --------------GYKFYLQNRSlPQSDPVLKVTLAVSDLQKSLNYWCNLLGMKIYEKDEEKQR----ALLGYA--DNQ 218
Cdd:PLN02300  126 kggksviafvkdpdGYKFELIQRG-PTPEPLCQVMLRVGDLDRSIKFYEKAFGMKLLRKRDNPEYkytiAMMGYGpeDKT 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167 219 CKLELQ---GVKgGVDHAAAFGRIAFScpQKELPDLEDLMKRENQKILTPLVSLdtPGKATvQVVILADPDGHEICFVGD 295
Cdd:PLN02300  205 TVLELTynyGVT-EYTKGNAYAQIAIG--TDDVYKTAEAIKLVGGKITREPGPL--PGINT-KITACLDPDGWKTVFVDN 278


                  ....*..
gi 1955885167 296 EAF-REL 301
Cdd:PLN02300  279 IDFlKEL 285
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 4-172 1.50e-11

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: 61.75  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167   4 RRALHFVFKVGNRFQTARFYRDVLGMKVEScsvarlecsgaisahcKLSLPgshhspasasrvagttgsdytritedsfs 83
Cdd:TIGR00068  16 RRLLHTMLRVGDLDKSLDFYTEVLGMKLLR----------------KRDFP----------------------------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167  84 kpyDGKWSKTMVGFGPEDDHFVAELTYNYGVGDYKLGNDFMGITLASSQAVSNARKLE----------WPLTEVAEGVFE 153
Cdd:TIGR00068  51 ---EMKFSLAFLGYGDETSAAVIELTHNWGTEKYDLGNGFGHIAIGVDDVYKACERVRalggnvvrepGPVKGGTTVIAF 127

                         170       180
                  ....*....|....*....|
gi 1955885167 154 TEAPGGYKF-YLQNRSLPQS 172
Cdd:TIGR00068 128 VEDPDGYKIeLIQRKSTKDG 147
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 178-293 2.10e-08

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: 51.92  E-value: 2.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167 178 VTLAVSDLQKSLNYWCNLLGMKIYEK----DEEKQRALLGYADNQcKLELQGVKGG--VDHAAAFGRIAFSCpqkelPDL 251
Cdd:COG0346     6 VTLRVSDLEASLAFYTDVLGLELVKRtdfgDGGFGHAFLRLGDGT-ELELFEAPGAapAPGGGGLHHLAFRV-----DDL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1955885167 252 EDLMKR-ENQKIltPLVSLDTPGKATVQVVILADPDGHEICFV 293
Cdd:COG0346    80 DAAYARlRAAGV--EIEGEPRDRAYGYRSAYFRDPDGNLIELV 120
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
178-292 1.06e-07

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 49.75  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167 178 VTLAVSDLQKSLNYWCNLLGMKI---YEKDEEKQRALLGYADNQCKLEL---QGVKGGVDHAAAFGrIAFSCPQKElpDL 251
Cdd:pfam00903   5 VALRVGDLEKSLDFYTDVLGFKLveeTDAGEEGGLRSAFFLAGGRVLELllnETPPPAAAGFGGHH-IAFIAFSVD--DV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1955885167 252 E---DLMKRENQKILTPLvsldTPGKATVQVVILADPDGHEICF 292
Cdd:pfam00903  82 DaayDRLKAAGVEIVREP----GRHGWGGRYSYFRDPDGNLIEL 121
PRK10291 PRK10291
glyoxalase I; Provisional
 89-164 2.58e-06

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 46.17  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167  89 KWSKTMVGFGPEDDHFVAELTYNYGVGDYKLGNDFMGITLASSQAVS----------NARKLEWPLTEVAEGVFETEAPG 158
Cdd:PRK10291   32 KYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEacekirqnggNVTREAGPVKGGTTVIAFVEDPD 111


                  ....*.
gi 1955885167 159 GYKFYL 164
Cdd:PRK10291  112 GYKIEL 117
 
Name Accession Description Interval E-value
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 177-292 2.19e-74

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: 224.74  E-value: 2.19e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167 177 KVTLAVSDLQKSLNYWCNLLGMKIYEKDEekQRALLGYADNQCKLELQGVKGGVDHAAAFGRIAFSCPQKELPDLEDLMK 256
Cdd:cd16357     1 KVSLAVSDLEKSIDYWSDLLGMKVFEKSE--KSALLGYGEDQAKLELVDIPEPVDHGTAFGRIAFSCPADELPPIEEKVK 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1955885167 257 RENQKILTPLVSLDTPGKATVQVVILADPDGHEICF 292
Cdd:cd16357    79 AAGQTILTPLVSLDTPGKATVQVVILADPDGHEICF 114
GLOD4_N cd08358
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 4-167 1.15e-72

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: 220.70  E-value: 1.15e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167   4 RRALHFVFKVGNRFQTARFYRDVLGMKV-------ESCSVArleCSGaisahcklslpgshhspasasrvagttgsdytr 76
Cdd:cd08358     1 RRALHFVFKVGDRNKTIKFYREILGMKVlrheefeEGCKAA---CNG--------------------------------- 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167  77 itedsfskPYDGKWSKTMVGFGPEDDHFVAELTYNYGVGDYKLGNDFMGITLASSQAVSNARKLEWPLTEVAEGVFETEA 156
Cdd:cd08358    45 --------PYDGKWSKTMVGYGPEDDHFVVELTYNYGIGDYELGNDFLGITIHSKQAVSRAKKHNWPVTQVGDGVYEVKA 116

                         170
                  ....*....|.
gi 1955885167 157 PGGYKFYLQNR 167
Cdd:cd08358   117 PGGYKFYLIDK 127
PLN02300 PLN02300
lactoylglutathione lyase
 4-301 1.46e-24

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 101.01  E-value: 1.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167   4 RRALHFVFKVGNRFQTARFYRDVLGMKVEScsvarlecsgaisahcKLSLPgshhspasasrvagttgsdytritEDsfs 83
Cdd:PLN02300   23 RRMLHVVYRVGDLDRTIKFYTECLGMKLLR----------------KRDIP------------------------EE--- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167  84 kpydgKWSKTMVGFGPEDDHFVAELTYNYGVGDYKLGNDF--MGItlassqAVSNARKLewpLTEV-AEGVFETEAPG-- 158
Cdd:PLN02300   60 -----KYTNAFLGYGPEDSNFVVELTYNYGVDKYDIGTGFghFGI------AVEDVAKT---VELVkAKGGKVTREPGpv 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167 159 --------------GYKFYLQNRSlPQSDPVLKVTLAVSDLQKSLNYWCNLLGMKIYEKDEEKQR----ALLGYA--DNQ 218
Cdd:PLN02300  126 kggksviafvkdpdGYKFELIQRG-PTPEPLCQVMLRVGDLDRSIKFYEKAFGMKLLRKRDNPEYkytiAMMGYGpeDKT 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167 219 CKLELQ---GVKgGVDHAAAFGRIAFScpQKELPDLEDLMKRENQKILTPLVSLdtPGKATvQVVILADPDGHEICFVGD 295
Cdd:PLN02300  205 TVLELTynyGVT-EYTKGNAYAQIAIG--TDDVYKTAEAIKLVGGKITREPGPL--PGINT-KITACLDPDGWKTVFVDN 278


                  ....*..
gi 1955885167 296 EAF-REL 301
Cdd:PLN02300  279 IDFlKEL 285
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 178-292 9.06e-13

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: 64.08  E-value: 9.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167 178 VTLAVSDLQKSLNYWCNLLGMKIYEKDEEKQRALLGYADNQCkLELQGVKGGVD-HAAAFGRIAFSCPQKElpdlEDLMK 256
Cdd:cd06587     2 VALRVPDLDASVAFYEEVLGFEVVSRNEGGGFAFLRLGPGLR-LALLEGPEPERpGGGGLFHLAFEVDDVD----EVDER 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1955885167 257 RENQKILTPLVSLDTPGKATVQVVILADPDGHEICF 292
Cdd:cd06587    77 LREAGAEGELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 7-164 2.60e-12

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: 62.80  E-value: 2.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167   7 LHFVFKVGNRFQTARFYRDVLGMKVescsvarlecsgaisahcklslpgshhspasasrvagTTGSDYTritedsfskpy 86
Cdd:cd16358     2 LHTMLRVGDLDRSIKFYTEVLGMKL-------------------------------------LRKRDYP----------- 33

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167  87 DGKWSKTMVGFGPEDDHFVAELTYNYGVGDYKLGNDFMGITLASS---QAVSNARKLEWPLTEVAEGVFE-------TEA 156
Cdd:cd16358    34 EGKYTLAFVGYGDEDENTVLELTYNWGVDKYDLGTAYGHIAIGVEdvyETCERIRKKGGKVTREPGPMKGgttviafVED 113


                  ....*...
gi 1955885167 157 PGGYKFYL 164
Cdd:cd16358   114 PDGYKIEL 121
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 4-172 1.50e-11

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: 61.75  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167   4 RRALHFVFKVGNRFQTARFYRDVLGMKVEScsvarlecsgaisahcKLSLPgshhspasasrvagttgsdytritedsfs 83
Cdd:TIGR00068  16 RRLLHTMLRVGDLDKSLDFYTEVLGMKLLR----------------KRDFP----------------------------- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167  84 kpyDGKWSKTMVGFGPEDDHFVAELTYNYGVGDYKLGNDFMGITLASSQAVSNARKLE----------WPLTEVAEGVFE 153
Cdd:TIGR00068  51 ---EMKFSLAFLGYGDETSAAVIELTHNWGTEKYDLGNGFGHIAIGVDDVYKACERVRalggnvvrepGPVKGGTTVIAF 127

                         170       180
                  ....*....|....*....|
gi 1955885167 154 TEAPGGYKF-YLQNRSLPQS 172
Cdd:TIGR00068 128 VEDPDGYKIeLIQRKSTKDG 147
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 178-293 2.10e-08

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: 51.92  E-value: 2.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167 178 VTLAVSDLQKSLNYWCNLLGMKIYEK----DEEKQRALLGYADNQcKLELQGVKGG--VDHAAAFGRIAFSCpqkelPDL 251
Cdd:COG0346     6 VTLRVSDLEASLAFYTDVLGLELVKRtdfgDGGFGHAFLRLGDGT-ELELFEAPGAapAPGGGGLHHLAFRV-----DDL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1955885167 252 EDLMKR-ENQKIltPLVSLDTPGKATVQVVILADPDGHEICFV 293
Cdd:COG0346    80 DAAYARlRAAGV--EIEGEPRDRAYGYRSAYFRDPDGNLIELV 120
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
178-292 1.06e-07

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 49.75  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167 178 VTLAVSDLQKSLNYWCNLLGMKI---YEKDEEKQRALLGYADNQCKLEL---QGVKGGVDHAAAFGrIAFSCPQKElpDL 251
Cdd:pfam00903   5 VALRVGDLEKSLDFYTDVLGFKLveeTDAGEEGGLRSAFFLAGGRVLELllnETPPPAAAGFGGHH-IAFIAFSVD--DV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1955885167 252 E---DLMKRENQKILTPLvsldTPGKATVQVVILADPDGHEICF 292
Cdd:pfam00903  82 DaayDRLKAAGVEIVREP----GRHGWGGRYSYFRDPDGNLIEL 121
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
178-296 2.90e-07

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 49.19  E-value: 2.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167 178 VTLAVSDLQKSLNYWCNLLGMKiyEKDEEKQRALLGYADNQCKLELQGVKGGVDHAAAFG--RIAFSCPQKElpDLEDLM 255
Cdd:COG2514     7 VTLRVRDLERSAAFYTDVLGLE--VVEREGGRVYLRADGGEHLLVLEEAPGAPPRPGAAGldHVAFRVPSRA--DLDAAL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1955885167 256 KR-ENQKILTPLVSLDTPGKAtvqvVILADPDGHEICFVGDE 296
Cdd:COG2514    83 ARlAAAGVPVEGAVDHGVGES----LYFRDPDGNLIELYTDR 120
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 175-293 9.69e-07

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: 47.01  E-value: 9.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167 175 VLKVTLAVSDLQKSLNYWCNLLGMKIYEK----DEEKQRALLGYAD--NQCKLELQ---GVKgGVDHAAAFGRIAFSCPq 245
Cdd:cd16358     1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKrdypEGKYTLAFVGYGDedENTVLELTynwGVD-KYDLGTAYGHIAIGVE- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1955885167 246 kELPDLEDLMKRENQKILTPLVSLdtPGKATVqVVILADPDGHEICFV 293
Cdd:cd16358    79 -DVYETCERIRKKGGKVTREPGPM--KGGTTV-IAFVEDPDGYKIELI 122
PRK10291 PRK10291
glyoxalase I; Provisional
 89-164 2.58e-06

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 46.17  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167  89 KWSKTMVGFGPEDDHFVAELTYNYGVGDYKLGNDFMGITLASSQAVS----------NARKLEWPLTEVAEGVFETEAPG 158
Cdd:PRK10291   32 KYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEacekirqnggNVTREAGPVKGGTTVIAFVEDPD 111


                  ....*.
gi 1955885167 159 GYKFYL 164
Cdd:PRK10291  112 GYKIEL 117
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 178-292 2.29e-04

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


Pssm-ID: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 40.39  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167 178 VTLAVSDLQKSLNYWCNLLGMKIYEKDEEKQRALLGyaDNQCKLELQGVK-----GGVDHAAAFGRIAFscpqkELPDLE 252
Cdd:cd07264     4 IVLYVDDFAASLRFYRDVLGLPPRFLHEEGEYAEFD--TGETKLALFSRKemarsGGPDRRGSAFELGF-----EVDDVE 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1955885167 253 DLMK--RENQKILTPLVSLDTPGKatvQVVILADPDGHEICF 292
Cdd:cd07264    77 ATVEelVERGAEFVREPANKPWGQ---TVAYVRDPDGNLIEI 115
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 178-199 5.92e-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: 5.92e-04
                          10        20
                  ....*....|....*....|..
gi 1955885167 178 VTLAVSDLQKSLNYWCNLLGMK 199
Cdd:cd07244     5 ITLAVSDLERSLAFYVDLLGFK 26
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 178-293 9.60e-04

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 38.46  E-value: 9.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955885167 178 VTLAVSDLQKSLNYWCNLLGMKIYEKDEEKQRALLGYADNQCKLELqgVKGGVDHAAAFGRIAFSCPqkelpDLEDLMKR 257
Cdd:COG3324     8 VELPVDDLERAKAFYEEVFGWTFEDDAGPGGDYAEFDTDGGQVGGL--MPGAEEPGGPGWLLYFAVD-----DLDAAVAR 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1955885167 258 ---ENQKILTPLVSLDTPGKatvqVVILADPDGHEICFV 293
Cdd:COG3324    81 veaAGGTVLRPPTDIPPWGR----FAVFRDPEGNRFGLW 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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