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Conserved domains on  [gi|800613176|emb|CFH60815|]
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glyoxalase/bleomycin resistance protein/dioxygenase [Mycobacterium tuberculosis]

Protein Classification

VOC family protein( domain architecture ID 10001243)

vicinal oxygen chelate (VOC) family protein uses a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms

CATH:  3.10.180.10
Gene Ontology:  GO:0046872|GO:0003824
PubMed:  21820381|11076500

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 15-165 6.35e-29

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: 103.92  E-value: 6.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  15 GINHVALVCSDMARTVDFYSNILGMPLIKALDLPGGQGQHFFFDAGNGDCVAFFWFADAPDRVPGLSspvaipgigdits 94
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTELELFEAPGAAPAPGGGG------------- 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 800613176  95 avstMNHLAFHVPAerFDAYRQRLKDKGVRVgpvlnhddsetqVSAVVHPGVYVRSFYFQDPDGITLEFAC 165
Cdd:COG0346   69 ----LHHLAFRVDD--LDAAYARLRAAGVEI------------EGEPRDRAYGYRSAYFRDPDGNLIELVE 121
 
Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 15-165 6.35e-29

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: 103.92  E-value: 6.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  15 GINHVALVCSDMARTVDFYSNILGMPLIKALDLPGGQGQHFFFDAGNGDCVAFFWFADAPDRVPGLSspvaipgigdits 94
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTELELFEAPGAAPAPGGGG------------- 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 800613176  95 avstMNHLAFHVPAerFDAYRQRLKDKGVRVgpvlnhddsetqVSAVVHPGVYVRSFYFQDPDGITLEFAC 165
Cdd:COG0346   69 ----LHHLAFRVDD--LDAAYARLRAAGVEI------------EGEPRDRAYGYRSAYFRDPDGNLIELVE 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
15-163 8.64e-21

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 82.88  E-value: 8.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176   15 GINHVALVCSDMARTVDFYSNILGMPLIKALDLPGGQGQHFFFDAGNGDCVAFFWFADAPDRVPGLsspvaipgigdits 94
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGF-------------- 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176   95 avsTMNHLAFHVPAER-FDAYRQRLKDKGVRVGPVLNHDDSETqvsavvhpgvyvRSFYFQDPDGITLEF 163
Cdd:pfam00903  67 ---GGHHIAFIAFSVDdVDAAYDRLKAAGVEIVREPGRHGWGG------------RYSYFRDPDGNLIEL 121
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 15-163 2.46e-17

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


Pssm-ID: 319940 [Multi-domain]  Cd Length: 123  Bit Score: 74.12  E-value: 2.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  15 GINHVALVCSDMARTVDFYSNILGMPLIKALDLPggQGQHFFFDAGNGDCVA-FFWFADAPDRvpgLSSPVAiPGigdit 93
Cdd:cd08352    2 KIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRP--ERNDIKLDLALGGYQLeLFIKPDAPAR---PSYPEA-LG----- 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  94 savstMNHLAFHVpaERFDAYRQRLKDKGVRVGPVLNhdDSETQvsavvhpgvyVRSFYFQDPDGITLEF 163
Cdd:cd08352   71 -----LRHLAFKV--EDVEATVAELKSLGIETEPIRV--DDFTG----------KKFTFFFDPDGLPLEL 121
PRK04101 PRK04101
metallothiol transferase FosB;
12-167 1.75e-10

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 56.49  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  12 ELGGINHVALVCSDMARTVDFYSNILGM-PLIKaldlpggqgqhfffdagnGDCVAFF-----WFAdapdrvpgLSSPVA 85
Cdd:PRK04101   1 MLKGINHICFSVSNLEKSIEFYEKVLGAkLLVK------------------GRKTAYFdlnglWIA--------LNEEKD 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  86 IPGiGDITSavsTMNHLAFHVPAERFDAYRQRLKDKGVRVGPVLNHDDSETQvsavvhpgvyvrSFYFQDPDGITLEFAC 165
Cdd:PRK04101  55 IPR-NEIHQ---SYTHIAFSIEEEDFDHWYQRLKENDVNILPGRERDERDKK------------SIYFTDPDGHKFEFHT 118


                 ..
gi 800613176 166 WT 167
Cdd:PRK04101 119 GT 120
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 18-163 3.16e-06

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: 45.18  E-value: 3.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176   18 HVALVCSDMARTVDFYSNILGMPLIKALDLPGGQGQHFFFDAGNGDCVAFF-----WFADAPDrvpglsspvaipgIGdi 92
Cdd:TIGR00068  20 HTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSAAVIelthnWGTEKYD-------------LG-- 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 800613176   93 tsavSTMNHLAFHVPaerfDAYR--QRLKDKGVRV----GPVlnhdDSETQVSAVVhpgvyvrsfyfQDPDGITLEF 163
Cdd:TIGR00068  85 ----NGFGHIAIGVD----DVYKacERVRALGGNVvrepGPV----KGGTTVIAFV-----------EDPDGYKIEL 138
 
Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 15-165 6.35e-29

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: 103.92  E-value: 6.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  15 GINHVALVCSDMARTVDFYSNILGMPLIKALDLPGGQGQHFFFDAGNGDCVAFFWFADAPDRVPGLSspvaipgigdits 94
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTELELFEAPGAAPAPGGGG------------- 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 800613176  95 avstMNHLAFHVPAerFDAYRQRLKDKGVRVgpvlnhddsetqVSAVVHPGVYVRSFYFQDPDGITLEFAC 165
Cdd:COG0346   69 ----LHHLAFRVDD--LDAAYARLRAAGVEI------------EGEPRDRAYGYRSAYFRDPDGNLIELVE 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
15-163 8.64e-21

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 82.88  E-value: 8.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176   15 GINHVALVCSDMARTVDFYSNILGMPLIKALDLPGGQGQHFFFDAGNGDCVAFFWFADAPDRVPGLsspvaipgigdits 94
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGF-------------- 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176   95 avsTMNHLAFHVPAER-FDAYRQRLKDKGVRVGPVLNHDDSETqvsavvhpgvyvRSFYFQDPDGITLEF 163
Cdd:pfam00903  67 ---GGHHIAFIAFSVDdVDAAYDRLKAAGVEIVREPGRHGWGG------------RYSYFRDPDGNLIEL 121
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
15-174 9.05e-20

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 80.77  E-value: 9.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  15 GINHVALVCSDMARTVDFYSNILGMPLIKAldlpggQGQHFFFDAGNGDcvAFFWFADAPDRVPGLSSPvaipgigdits 94
Cdd:COG2514    3 RLGHVTLRVRDLERSAAFYTDVLGLEVVER------EGGRVYLRADGGE--HLLVLEEAPGAPPRPGAA----------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  95 avsTMNHLAFHVP-AERFDAYRQRLKDKGVRVGPVLNHDDSEtqvsavvhpgvyvrSFYFQDPDGITLEFACWTKEFTTS 173
Cdd:COG2514   64 ---GLDHVAFRVPsRADLDAALARLAAAGVPVEGAVDHGVGE--------------SLYFRDPDGNLIELYTDRPRFEHV 126


                 .
gi 800613176 174 D 174
Cdd:COG2514  127 G 127
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 15-163 2.46e-17

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


Pssm-ID: 319940 [Multi-domain]  Cd Length: 123  Bit Score: 74.12  E-value: 2.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  15 GINHVALVCSDMARTVDFYSNILGMPLIKALDLPggQGQHFFFDAGNGDCVA-FFWFADAPDRvpgLSSPVAiPGigdit 93
Cdd:cd08352    2 KIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRP--ERNDIKLDLALGGYQLeLFIKPDAPAR---PSYPEA-LG----- 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  94 savstMNHLAFHVpaERFDAYRQRLKDKGVRVGPVLNhdDSETQvsavvhpgvyVRSFYFQDPDGITLEF 163
Cdd:cd08352   71 -----LRHLAFKV--EDVEATVAELKSLGIETEPIRV--DDFTG----------KKFTFFFDPDGLPLEL 121
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 18-163 4.90e-17

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: 72.94  E-value: 4.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  18 HVALVCSDMARTVDFYSNILGMPLIKALDLPGgqgqHFFFDAGNGDCVAFFWFADAPDRVPGlsspvaipgigditsavs 97
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGG----FAFLRLGPGLRLALLEGPEPERPGGG------------------ 58

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 800613176  98 TMNHLAFHVP-AERFDAYRQRLKDKGVRVGPvlnhddsetqvsaVVHPGVYVRSFYFQDPDGITLEF 163
Cdd:cd06587   59 GLFHLAFEVDdVDEVDERLREAGAEGELVAP-------------PVDDPWGGRSFYFRDPDGNLIEF 112
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 15-162 6.95e-14

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: 65.00  E-value: 6.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  15 GINHVALVCSDMARTVDFYSNILGMPLIKALDlpggQGQHffFDAGNgdcvafFWFAdapdrvpgLSspvaipgIGDITS 94
Cdd:cd07244    1 GINHITLAVSDLERSLAFYVDLLGFKPHVRWD----KGAY--LTAGD------LWLC--------LS-------LDPAAE 53

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 800613176  95 AVSTMNHLAFHVPAERFDAYRQRLKDKGVrvgPVLNHDDSETqvsavvhpgvyvRSFYFQDPDGITLE 162
Cdd:cd07244   54 PSPDYTHIAFTVSEEDFEELSERLRAAGV---KIWQENSSEG------------DSLYFLDPDGHKLE 106
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 16-163 1.38e-11

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


Pssm-ID: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 58.87  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  16 INHVALVCSDMARTVDFYSNILGMPLIKA----------LDLPGGQGQHFFFDAgngdcvaffWFADAPDRVPGLSSPva 85
Cdd:cd07245    1 LDHVALACPDLERARRFYTDVLGLEEVPRppflkfggawLYLGGGQQIHLVVEQ---------NPSELPRPEHPGRDR-- 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 800613176  86 ipgigditsavstmnHLAFHVPAerFDAYRQRLKDKGVrvgpvlnhddsetQVSAVVHPGVYVRSFYFQDPDGITLEF 163
Cdd:cd07245   70 ---------------HPSFSVPD--LDALKQRLKEAGI-------------PYTESTSPGGGVTQLFFRDPDGNRLEF 117
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 18-163 1.36e-10

Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. The three types of fosfomycin resistance proteins, employ different mechanisms to render fosfomycin [(1R,2S)-epoxypropylphosphonic acid] inactive. FosB catalyzes the addition of L-cysteine to the epoxide ring of fosfomycin. FosX catalyzes the addition of a water molecule to the C1 position of the antibiotic with inversion of configuration at C1. FosA catalyzes the addition of glutathione to the antibiotic fosfomycin, making it inactive. Catalytic activities of both FosX and FosA are Mn(II)-dependent, but FosB is activated by Mg(II). Fosfomycin resistant proteins are evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319933  Cd Length: 118  Bit Score: 56.41  E-value: 1.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  18 HVALVCSDMARTVDFYSNILGMPLIKA-LDLPGGQGQHFFFDAGNgdcvafFWFAdapdrvpgLSSPVAIPGigditsav 96
Cdd:cd08345    1 HITLIVRDLEKSTAFLQDIFGAREVYSsGDKTFSLSKEKFFLLGG------LWIA--------LMEGESLQE-------- 58

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 800613176  97 STMNHLAFHVPAERFDAYRQRLKDKGVRVGPVLNHDDSETqvsavvhpgvyvRSFYFQDPDGITLEF 163
Cdd:cd08345   59 RSYTHIAFQIQSEDFDRYAERLGALGVEMRPPRPRVEGEG------------RSIYFYDPDNHLFEL 113
PRK04101 PRK04101
metallothiol transferase FosB;
12-167 1.75e-10

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 56.49  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  12 ELGGINHVALVCSDMARTVDFYSNILGM-PLIKaldlpggqgqhfffdagnGDCVAFF-----WFAdapdrvpgLSSPVA 85
Cdd:PRK04101   1 MLKGINHICFSVSNLEKSIEFYEKVLGAkLLVK------------------GRKTAYFdlnglWIA--------LNEEKD 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  86 IPGiGDITSavsTMNHLAFHVPAERFDAYRQRLKDKGVRVGPVLNHDDSETQvsavvhpgvyvrSFYFQDPDGITLEFAC 165
Cdd:PRK04101  55 IPR-NEIHQ---SYTHIAFSIEEEDFDHWYQRLKENDVNILPGRERDERDKK------------SIYFTDPDGHKFEFHT 118


                 ..
gi 800613176 166 WT 167
Cdd:PRK04101 119 GT 120
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 20-164 6.92e-10

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: 54.29  E-value: 6.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  20 ALVCSDMARTVDFYSNILGMPLIKAldlpggQGQHFFFDAGNGDCVAFFwfadapdrvPGLSSP----VAIPGIGDitsa 95
Cdd:cd08354    5 CLYADDLDAAEAFYEDVLGLKPMLR------SGRHAFFRLGPQVLLVFD---------PGATSKdvrtGEVPGHGA---- 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 800613176  96 vSTMNHLAFHVPAERFDAYRQRLKDKGVRVgpvlnhddsetqVSAVVHPGvYVRSFYFQDPDGITLEFA 164
Cdd:cd08354   66 -SGHGHFAFAVPTEELAAWEARLEAKGVPI------------ESYTQWPE-GGKSLYFRDPAGNLVELA 120
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 14-163 7.25e-10

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 54.26  E-value: 7.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  14 GGINHVALVCSDMARTVDFYSNILGMPLIKALDLPGGqgqHFFFDAGNGDCVAFFWFADAPdrvpglsspvAIPGIgdit 93
Cdd:COG3324    3 GTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPGGD---YAEFDTDGGQVGGLMPGAEEP----------GGPGW---- 65

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  94 savstmnHLAFHVpaERFDAYRQRLKDKGVRVgpvlnhddsetqVSAVVHPGVYVRSFYFQDPDGITLEF 163
Cdd:COG3324   66 -------LLYFAV--DDLDAAVARVEAAGGTV------------LRPPTDIPPWGRFAVFRDPEGNRFGL 114
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 16-163 2.10e-09

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


Pssm-ID: 319951 [Multi-domain]  Cd Length: 131  Bit Score: 53.51  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  16 INHVALVCSDMARTVDFYSNIL-GMPLIKALDLPggqgqhfFFDAgNGDCVAFFWFADAPDRvpglsspvaipgigDITS 94
Cdd:cd08363    1 INHITFSVSNLNKSIAFYKDVLdAKLLVLGEKTA-------YFDL-NGLWLALNVQEDIPRN--------------EISH 58

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 800613176  95 avsTMNHLAFHVPAERFDAYRQRLKDKGVRVGPVLNHDDSETQvsavvhpgvyvrSFYFQDPDGITLEF 163
Cdd:cd08363   59 ---SYTHIAFSIDEEDLDAFKERLKDNGVNILEGRKRDILEGQ------------SIYFTDPDGHLFEL 112
PcpA_N_like cd08346
N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 15-162 1.11e-07

N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins; The N-terminal domain of Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) 2,6-dichloro-p-hydroquinone1,2-dioxygenase (PcpA), and similar proteins. PcpA is a key enzyme in the pentachlorophenol (PCP) degradation pathway, catalyzing the conversion of 2,6-dichloro-p-hydroquinone to 2-chloromaleylacetate. This domain belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases.


Pssm-ID: 319934  Cd Length: 124  Bit Score: 48.44  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  15 GINHVALVCSDMARTVDFYSNILGMPLIKALDLPGGQGQ-HFFF--DAGN-GDCVAFFWFADAPDRVPGLSSPVAIpgig 90
Cdd:cd08346    1 GIHHITAITGDAQENVDFYVKVLGLRLVKKTVNQDDPPMyHLYYgdELGSpGTLLTFFPWPLGGPGRRGTGQISRI---- 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 800613176  91 ditsavstmnhlAFHVPAERFDAYRQRLKDKGVRVGPVlnhddsetqVSAVVHPgvYVRsfyFQDPDGITLE 162
Cdd:cd08346   77 ------------GLRVPKGSLSFWAERLEKFGVPHSEV---------VTRFGEK--YLR---FEDPDGTRLF 122
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 15-158 7.50e-07

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: 46.07  E-value: 7.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  15 GINHVALVCSDMARTVDFYSNILGMPLI------KALDLpgGQGQHFFFDAGNgdcvaffWFADAPdrvpglSSPVaiPG 88
Cdd:cd07253    3 RLDHLVLTVKDIERTIDFYTKVLGMTVVtfkegrKALRF--GNQKINLHQKGK-------EFEPKA------SAPT--PG 65

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 800613176  89 IGDITSAVSTmnhlaFHvpaerfDAYRQRLKDKGVRV--GPVlnhddsetQVSAVVHPGVyvrSFYFQDPDG 158
Cdd:cd07253   66 SADLCFITET-----PI------DEVLEHLEACGVTIeeGPV--------KRTGALGPIL---SIYFRDPDG 115
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 18-163 3.16e-06

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: 45.18  E-value: 3.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176   18 HVALVCSDMARTVDFYSNILGMPLIKALDLPGGQGQHFFFDAGNGDCVAFF-----WFADAPDrvpglsspvaipgIGdi 92
Cdd:TIGR00068  20 HTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSAAVIelthnWGTEKYD-------------LG-- 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 800613176   93 tsavSTMNHLAFHVPaerfDAYR--QRLKDKGVRV----GPVlnhdDSETQVSAVVhpgvyvrsfyfQDPDGITLEF 163
Cdd:TIGR00068  85 ----NGFGHIAIGVD----DVYKacERVRALGGNVvrepGPV----KGGTTVIAFV-----------EDPDGYKIEL 138
FosX cd08364
fosfomycin resistant protein subfamily FosX; This subfamily family contains FosX, a fosfomycin ...
 15-157 7.04e-06

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: 43.80  E-value: 7.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  15 GINHVALVCSDMARTVDFYSNILGmplikALDLPGGQGQHF------FFDAGNgdcvafFWFADAPDRVPglsspvaipg 88
Cdd:cd08364    3 GISHITFIVKDLDRTAAFLTEIFG-----AEEVYDSGAETFslspekFFLIGG------LWIAIMEGEPL---------- 61

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 800613176  89 igditsAVSTMNHLAFHVPAERFDAYRQRLKDKGVRVGPVLNHDDSETqvsavvhpgvyvRSFYFQDPD 157
Cdd:cd08364   62 ------LERSYNHIAFKVSEGDLDEYRARIKKLGLEIRPPRSRVQGEG------------RSLYFYDFD 112
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
17-153 7.25e-06

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 43.04  E-value: 7.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176   17 NHVALVCSDMARTVDFYSNILGM-PLIKALDLPGGQGQHFFFdAGNGDCVAFFwfaDAPDRVPglsSPVAIPGIGditsa 95
Cdd:pfam13669   1 HHVGIAVPDLDRALALWGALLGLgPEGDYRSEPQNVDLAFAL-LGDGPVEVEL---IQPLDGD---SPLARHGPG----- 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 800613176   96 vstMNHLAFHVpaERFDAYRQRLKDKGVRVgpvlnhddsetqVSAVVHPGVYVRSFYF 153
Cdd:pfam13669  69 ---LHHLAYWV--DDLDAAVARLLDQGYRV------------APKGPRAGAAGRRVAF 109
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 15-165 7.53e-05

N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC superfamily contains Bacillus subtilis CatE and similar proteins. CatE is proposed to function as Catechol-2,3-dioxygenase. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319918  Cd Length: 124  Bit Score: 40.76  E-value: 7.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  15 GINHVALVCSDMARTVDFYSNILGMPLIKaldlPGGQGQHFffdAGNGDCVAFFWFAD-----APDRVPGLsspvaipgi 89
Cdd:cd07255    2 RIGRVTLKVADLERQSAFYQNVIGLSVLK----QNASRAYL---GVDGKQVLLVLEAIpdavlAPRSTTGL--------- 65

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 800613176  90 gditsavstmNHLAFHVPAerfdayRQRLkdkgvrvGPVLNHDDSE-TQVSAVVHpgVYVRSFYFQDPDGITLEFAC 165
Cdd:cd07255   66 ----------YHFAILLPD------RKAL-------GRALAHLAEHgPLIGAADH--GVSEAIYLSDPEGNGIEIYA 117
ChaP_like cd08351
ChaP, an enzyme involved in the biosynthesis of the antitumor agent chartreusin (cha), and ...
 17-163 1.02e-04

ChaP, an enzyme involved in the biosynthesis of the antitumor agent chartreusin (cha), and similar proteins; ChaP is an enzyme involved in the biosynthesis of the potent antitumor agent chartreusin (cha). Cha is an aromatic polyketide glycoside produced by Streptomyces chartreusis. ChaP may play a role as a meta-cleavage dioxygenase in the oxidative rearrangement of the anthracyclic polyketide. ChaP belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases.


Pssm-ID: 319939  Cd Length: 118  Bit Score: 40.18  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  17 NHVALVCSDMARTVDFYSNILGMPlikaldlPGGQGQHFF-FDAGNGdcvAFFWFADAPDRVPGlsspvaipgigditsa 95
Cdd:cd08351    4 NHTIVPARDKEASARFLAEILGLP-------APPPWGPFApVRLNNG---LTLDFADPRGEIAP---------------- 57

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 800613176  96 vstmNHLAFHVPAERFDAYRQRLKDKGV--------RVGPVLNHDDSetqvsavvhpGvyvRSFYFQDPDGITLEF 163
Cdd:cd08351   58 ----QHYAFLVSDDEFDAILARIRARGLeywadpqhREPGEINHNDG----------G---RGVYFRDPDGHLLEI 116
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 18-43 1.38e-04

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: 39.85  E-value: 1.38e-04
                         10        20
                 ....*....|....*....|....*.
gi 800613176  18 HVALVCSDMARTVDFYSNILGMPLIK 43
Cdd:cd16357    1 KVSLAVSDLEKSIDYWSDLLGMKVFE 26
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 15-163 4.80e-04

vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; This subfamily of vicinal oxygen chelate (VOC) family protein includes Streptomyces hygroscopicus ValD protein and similar proteins. ValD protein functions in validamycin biosynthetic pathway. 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: 319968  Cd Length: 150  Bit Score: 38.85  E-value: 4.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  15 GINHVALVCSDMARTVDFYSNILG----MPLIKALDLPGGQGQ---HFFFDA-----------GNGDCVAFFWFADAPDR 76
Cdd:cd16361    1 GVNHVGITVPDLDAAVEFYTDVLGaevvYRSTPLAEGDRGGGEmraAGFVPGfarariamlrlGPGPGIELFEYKGPEQR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  77 VPglsspvaIPGIGDItsavsTMNHLAFHVPaeRFDAYRQRLKDKG--VRVGPVLNHDDSetqvsavvhPGVYVRSFYFQ 154
Cdd:cd16361   81 AP-------VPRNSDV-----GIFHFALQVD--DVEAAAERLAAAGgkVLMGPREIPDGG---------PGKGNRMVYLR 137


                 ....*....
gi 800613176 155 DPDGITLEF 163
Cdd:cd16361  138 DPWGTLIEL 146
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 17-50 3.65e-03

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: 36.15  E-value: 3.65e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 800613176  17 NHVALVCSDMARTVDFYSNILGMPLIKALDLPGG 50
Cdd:cd07233    2 NHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEM 35
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 18-158 3.88e-03

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: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 35.74  E-value: 3.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800613176  18 HVALVCSDMARTVDFYSNILGmpLIKALDLPGGQGQhfffdagngdcvaffWFADAPDRVPG----LSSPVAIPGIGDIT 93
Cdd:cd07263    1 QVMLYVDDQDKALDFYVEKLG--FEVVEDVPMGGMR---------------WVTVAPPGSPGtsllLEPKAHPAQMPQSP 63

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 800613176  94 SAVSTMNHLAFHVpaERFDAYRQRLKDKGVRVGPvlnhddsetqvsAVVHPGvYVRSFYFQDPDG 158
Cdd:cd07263   64 EAAGGTPGILLAT--DDIDATYERLTAAGVTFVQ------------EPTQMG-GGRVANFRDPDG 113
 
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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