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Conserved domains on  [gi|157819477|ref|NP_001100427|]
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glyoxalase domain-containing protein 5 [Rattus norvegicus]

Protein Classification

VOC family protein( domain architecture ID 10163535)

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

CATH:  3.10.180.10
PubMed:  21820381

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 23-145 2.09e-75

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: 220.18  E-value: 2.09e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477  23 ICRLDHIVMTVKNIEDTTMFYSKILGMEVTTFKGDRKALCFGDQKFNLHEVGKEFDPKAAHPIPGSLDVCLITETPLEEV 102
Cdd:cd07253    1 IKRLDHLVLTVKDIERTIDFYTKVLGMTVVTFKEGRKALRFGNQKINLHQKGKEFEPKASAPTPGSADLCFITETPIDEV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 157819477 103 MKRLKAFDVPIEEGPVSRTGAKGPILSIYFRDPDRNLIEVSNY 145
Cdd:cd07253   81 LEHLEACGVTIEEGPVKRTGALGPILSIYFRDPDGNLIELSNY 123
 
Name Accession Description Interval E-value
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 23-145 2.09e-75

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: 220.18  E-value: 2.09e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477  23 ICRLDHIVMTVKNIEDTTMFYSKILGMEVTTFKGDRKALCFGDQKFNLHEVGKEFDPKAAHPIPGSLDVCLITETPLEEV 102
Cdd:cd07253    1 IKRLDHLVLTVKDIERTIDFYTKVLGMTVVTFKEGRKALRFGNQKINLHQKGKEFEPKASAPTPGSADLCFITETPIDEV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 157819477 103 MKRLKAFDVPIEEGPVSRTGAKGPILSIYFRDPDRNLIEVSNY 145
Cdd:cd07253   81 LEHLEACGVTIEEGPVKRTGALGPILSIYFRDPDGNLIELSNY 123
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 25-145 9.05e-20

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: 78.88  E-value: 9.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477  25 RLDHIVMTVKNIEDTTMFYSKILGMEV---TTFKGDRKALCF----GDQKFNLHevgkEFDPKAAHPIPGSLD-VCLITE 96
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELvkrTDFGDGGFGHAFlrlgDGTELELF----EAPGAAPAPGGGGLHhLAFRVD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 157819477  97 TpLEEVMKRLKAFDVPIEEGPvsRTGAKGPIlSIYFRDPDRNLIEVSNY 145
Cdd:COG0346   78 D-LDAAYARLRAAGVEIEGEP--RDRAYGYR-SAYFRDPDGNLIELVEP 122
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
25-142 4.79e-11

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 56.30  E-value: 4.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477   25 RLDHIVMTVKNIEDTTMFYSKILGMEVtTFKGDRKALCFGDQKF-----NLHEVGKEFDPKAAHPIPGSLDVCLITETP- 98
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKL-VEETDAGEEGGLRSAFflaggRVLELLLNETPPPAAAGFGGHHIAFIAFSVd 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 157819477   99 -LEEVMKRLKAFDVPIEEGPvSRTGAKGpiLSIYFRDPDRNLIEV 142
Cdd:pfam00903  80 dVDAAYDRLKAAGVEIVREP-GRHGWGG--RYSYFRDPDGNLIEL 121
PRK04101 PRK04101
metallothiol transferase FosB;
26-142 2.73e-04

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 38.77  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477  26 LDHIVMTVKNIEDTTMFYSKILGMEVTTfKGDRKALcfgdqkFNLHEV----GKEFDpkaahpIPGSlDVCL-------- 93
Cdd:PRK04101   5 INHICFSVSNLEKSIEFYEKVLGAKLLV-KGRKTAY------FDLNGLwialNEEKD------IPRN-EIHQsythiafs 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 157819477  94 ITETPLEEVMKRLKAFDVPIEEGpvsRTGAKGPILSIYFRDPDRNLIEV 142
Cdd:PRK04101  71 IEEEDFDHWYQRLKENDVNILPG---RERDERDKKSIYFTDPDGHKFEF 116
 
Name Accession Description Interval E-value
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 23-145 2.09e-75

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: 220.18  E-value: 2.09e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477  23 ICRLDHIVMTVKNIEDTTMFYSKILGMEVTTFKGDRKALCFGDQKFNLHEVGKEFDPKAAHPIPGSLDVCLITETPLEEV 102
Cdd:cd07253    1 IKRLDHLVLTVKDIERTIDFYTKVLGMTVVTFKEGRKALRFGNQKINLHQKGKEFEPKASAPTPGSADLCFITETPIDEV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 157819477 103 MKRLKAFDVPIEEGPVSRTGAKGPILSIYFRDPDRNLIEVSNY 145
Cdd:cd07253   81 LEHLEACGVTIEEGPVKRTGALGPILSIYFRDPDGNLIELSNY 123
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 25-145 9.05e-20

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: 78.88  E-value: 9.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477  25 RLDHIVMTVKNIEDTTMFYSKILGMEV---TTFKGDRKALCF----GDQKFNLHevgkEFDPKAAHPIPGSLD-VCLITE 96
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELvkrTDFGDGGFGHAFlrlgDGTELELF----EAPGAAPAPGGGGLHhLAFRVD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 157819477  97 TpLEEVMKRLKAFDVPIEEGPvsRTGAKGPIlSIYFRDPDRNLIEVSNY 145
Cdd:COG0346   78 D-LDAAYARLRAAGVEIEGEP--RDRAYGYR-SAYFRDPDGNLIELVEP 122
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
25-142 6.61e-18

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 74.61  E-value: 6.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477  25 RLDHIVMTVKNIEDTTMFYSKILGMEVTTFKGDRKALCF--GDQKFNLHEVGkefDPKAAHPIPGSLDVCLITETP--LE 100
Cdd:COG2514    3 RLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRAdgGEHLLVLEEAP---GAPPRPGAAGLDHVAFRVPSRadLD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 157819477 101 EVMKRLKAFDVPIeEGPVSRTGAKgpilSIYFRDPDRNLIEV 142
Cdd:COG2514   80 AALARLAAAGVPV-EGAVDHGVGE----SLYFRDPDGNLIEL 116
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 28-142 1.93e-11

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: 57.15  E-value: 1.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477  28 HIVMTVKNIEDTTMFYSKILGMEVTTFKGDRKALCFGD---QKFNLHEVGKEFDPKAahpiPGSLDVCLITETPLEEVMK 104
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGFAFLRLgpgLRLALLEGPEPERPGG----GGLFHLAFEVDDVDEVDER 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 157819477 105 --RLKAFDVPIEEGPVSRTGAKgpilSIYFRDPDRNLIEV 142
Cdd:cd06587   77 lrEAGAEGELVAPPVDDPWGGR----SFYFRDPDGNLIEF 112
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
25-142 4.79e-11

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 56.30  E-value: 4.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477   25 RLDHIVMTVKNIEDTTMFYSKILGMEVtTFKGDRKALCFGDQKF-----NLHEVGKEFDPKAAHPIPGSLDVCLITETP- 98
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKL-VEETDAGEEGGLRSAFflaggRVLELLLNETPPPAAAGFGGHHIAFIAFSVd 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 157819477   99 -LEEVMKRLKAFDVPIEEGPvSRTGAKGpiLSIYFRDPDRNLIEV 142
Cdd:pfam00903  80 dVDAAYDRLKAAGVEIVREP-GRHGWGG--RYSYFRDPDGNLIEL 121
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 42-142 2.91e-08

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: 48.90  E-value: 2.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477  42 FYSKILGMEVTTFKGDRKALCFGDQKFNLHEVGKEFDPKAAHPIP-----GSLDVCL-ITETPLEEVMKRLKAFDVPIEE 115
Cdd:cd08354   17 FYEDVLGLKPMLRSGRHAFFRLGPQVLLVFDPGATSKDVRTGEVPghgasGHGHFAFaVPTEELAAWEARLEAKGVPIES 96

                         90       100
                 ....*....|....*....|....*..
gi 157819477 116 gpVSRTGAKGPilSIYFRDPDRNLIEV 142
Cdd:cd08354   97 --YTQWPEGGK--SLYFRDPAGNLVEL 119
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 26-142 1.15e-07

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: 47.31  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477  26 LDHIVMTVKNIEDTTMFYSKILGMEV----TTFKGDRKALCFGDqKFNLH-EVGKEFDPKAAHPIPGSLD-VCLITETpL 99
Cdd:cd07245    1 LDHVALACPDLERARRFYTDVLGLEEvprpPFLKFGGAWLYLGG-GQQIHlVVEQNPSELPRPEHPGRDRhPSFSVPD-L 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 157819477 100 EEVMKRLKAFDVPIeegpVSRTGAKGPILSIYFRDPDRNLIEV 142
Cdd:cd07245   79 DALKQRLKEAGIPY----TESTSPGGGVTQLFFRDPDGNRLEF 117
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 27-143 3.76e-07

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


Pssm-ID: 319931  Cd Length: 132  Bit Score: 46.16  E-value: 3.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477  27 DHIVMTVKNIEDTTMFYSKILGMEVT--TFKGDRKALCF--GDQKFNLHEVG--KEFDPKAAHpipGSLDVcliteTPLE 100
Cdd:cd08343    1 GHVVLCSPDVEASRDFYTDVLGFRVSdrIVDPGVDGGAFlhCDRGTDHHTVAlaGGPHPGLHH---VAFEV-----HDLD 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 157819477 101 EVMK---RLKAFDVPIEEGPVsRTGAKGPIlSIYFRDPDRNLIEVS 143
Cdd:cd08343   73 DVGRghdRLREKGYKIEWGPG-RHGLGSQV-FDYWFDPSGNRVEYY 116
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 26-142 4.53e-07

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: 46.19  E-value: 4.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477  26 LDHIVMTVKNIEDTTMFYSKILgMEVTTFKGDRKA--------LCFGDQKfNLHEvgKEFDPKAAHpIPGSldvclITET 97
Cdd:cd08363    1 INHITFSVSNLNKSIAFYKDVL-DAKLLVLGEKTAyfdlnglwLALNVQE-DIPR--NEISHSYTH-IAFS-----IDEE 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 157819477  98 PLEEVMKRLKAFDVPIEEGpvsRTGAKGPILSIYFRDPDRNLIEV 142
Cdd:cd08363   71 DLDAFKERLKDNGVNILEG---RKRDILEGQSIYFTDPDGHLFEL 112
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 25-142 4.35e-06

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: 43.45  E-value: 4.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477  25 RLDHIVMTVKNIEDTTMFYSKILGMEVTTFKGDRKALCFGDQKFNLHEVGKEFDPKAAHPIPGSLDVCLI--TETPLEEV 102
Cdd:cd07255    2 RIGRVTLKVADLERQSAFYQNVIGLSVLKQNASRAYLGVDGKQVLLVLEAIPDAVLAPRSTTGLYHFAILlpDRKALGRA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 157819477 103 MKRLkafdvpIEEGPVSRTGAKGPILSIYFRDPDRNLIEV 142
Cdd:cd07255   82 LAHL------AEHGPLIGAADHGVSEAIYLSDPEGNGIEI 115
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 25-142 2.23e-05

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 41.16  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477  25 RLDHIVMTVKNIEDTTMFYSKILGMEVTTFKGDRKALCFGDqkFNLHEVGkEFDPKAAHPIPGSLDVCLITEtPLEEVMK 104
Cdd:COG3324    4 TIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPGGDYAEFD--TDGGQVG-GLMPGAEEPGGPGWLLYFAVD-DLDAAVA 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 157819477 105 RLKAFDVPIEEGPVSRTGAkGPILsiYFRDPDRNLIEV 142
Cdd:COG3324   80 RVEAAGGTVLRPPTDIPPW-GRFA--VFRDPEGNRFGL 114
FosX cd08364
fosfomycin resistant protein subfamily FosX; This subfamily family contains FosX, a fosfomycin ...
 26-141 3.46e-05

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: 41.11  E-value: 3.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477  26 LDHIVMTVKNIEDTTMFYSKILGMEVTTFKGDR-------KALCFGDQKFNLHEvGKEFDPKAAHPIPGSldvclITETP 98
Cdd:cd08364    4 ISHITFIVKDLDRTAAFLTEIFGAEEVYDSGAEtfslspeKFFLIGGLWIAIME-GEPLLERSYNHIAFK-----VSEGD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 157819477  99 LEEVMKRLKAFDVPIEEgPVSRTGAKGpiLSIYFRDPDRNLIE 141
Cdd:cd08364   78 LDEYRARIKKLGLEIRP-PRSRVQGEG--RSLYFYDFDNHLFE 117
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 28-141 2.02e-04

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: 38.69  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477  28 HIVMTVKNIEDTTMFYSKILGMevttfkgdRKALCFGDQKFNLHEvGKEFDpkaahpiPGSLDVCL-------------- 93
Cdd:cd08345    1 HITLIVRDLEKSTAFLQDIFGA--------REVYSSGDKTFSLSK-EKFFL-------LGGLWIALmegeslqersythi 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157819477  94 ---ITETPLEEVMKRLKAFDVPIEEGpvsRTGAKGPILSIYFRDPDRNLIE 141
Cdd:cd08345   65 afqIQSEDFDRYAERLGALGVEMRPP---RPRVEGEGRSIYFYDPDNHLFE 112
PRK04101 PRK04101
metallothiol transferase FosB;
26-142 2.73e-04

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 38.77  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477  26 LDHIVMTVKNIEDTTMFYSKILGMEVTTfKGDRKALcfgdqkFNLHEV----GKEFDpkaahpIPGSlDVCL-------- 93
Cdd:PRK04101   5 INHICFSVSNLEKSIEFYEKVLGAKLLV-KGRKTAY------FDLNGLwialNEEKD------IPRN-EIHQsythiafs 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 157819477  94 ITETPLEEVMKRLKAFDVPIEEGpvsRTGAKGPILSIYFRDPDRNLIEV 142
Cdd:PRK04101  71 IEEEDFDHWYQRLKENDVNILPG---RERDERDKKSIYFTDPDGHKFEF 116
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 26-136 6.41e-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: 37.26  E-value: 6.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477  26 LDHIVMTVKNIEDTTMFYSKILGMEVTTfKGDRKA-LCFGDQKFNLhEVGKEFDPKA--AHPipgSLDVcliTETPLEEV 102
Cdd:cd07244    2 INHITLAVSDLERSLAFYVDLLGFKPHV-RWDKGAyLTAGDLWLCL-SLDPAAEPSPdyTHI---AFTV---SEEDFEEL 73

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 157819477 103 MKRLKAFDVPI-----EEGPvsrtgakgpilSIYFRDPD 136
Cdd:cd07244   74 SERLRAAGVKIwqensSEGD-----------SLYFLDPD 101
BphC-JF8_C_like cd09014
C-terminal, catalytic domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase); 2, ...
 25-144 6.42e-04

C-terminal, catalytic domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase); 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, a key step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). BphC belongs to the type I extradiol dioxygenase family, which requires a metal ion in the active site in its catalytic mechanism. Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. This subfamily of BphC is represented by the enzyme purified from the thermophilic biphenyl and naphthalene degrader, Bacillus sp. JF8. The members in this family of BphC enzymes may use either Mn(II) or Fe(II) as cofactors. The enzyme purified from Bacillus sp. JF8 is Mn(II)-dependent, however, the enzyme from Rhodococcus jostii RHAI has Fe(II) bound to it. BphC_JF8 is thermostable and its optimum activity is at 85 degrees C. The enzymes in this family have an internal duplication. This family represents the C-terminal repeat.


Pssm-ID: 319956  Cd Length: 167  Bit Score: 38.13  E-value: 6.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477  25 RLDHIVMTVKNIEDTTMFYSKILGMEVTTF---KGDRKALCFGDQKFNLHEVGKEFDPKAAhpiPGSL-DVCLITETPlE 100
Cdd:cd09014    6 RIDHLNLLASDVTANRQFMSDTLGFRLREQirdNNGGEAGAWMSVSSLVHDVAVMRDGKGE---PGRLhHLAYWYGTP-E 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157819477 101 EVMKRLKAF---DVPIEEGP----VSRTgakgpiLSIYFRDPDRNLIEVSN 144
Cdd:cd09014   82 DLLRAADIFrehGIQIEAGPgkhgISQA------FFLYVYEPGGNRVELFG 126
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 28-143 1.23e-03

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


Pssm-ID: 319967  Cd Length: 111  Bit Score: 36.53  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477  28 HIVMTVKNIEDTTMFYSKILGMEVTTFKGDRKAL-CFGDQKFNL--HEVgkefdpkaahPIPGSLDVCLITETP--LEEV 102
Cdd:cd16360    1 YAELGVPDLEKALEFYTDVLGLQVAKRDGNSVYLrGYEDEHHSLvlYEA----------PEAGLKHFAFEVASEedLERA 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 157819477 103 MKRLKAFDVPIEEGPVSRTGAKGpiLSIYFRDPDRNLIEVS 143
Cdd:cd16360   71 AASLTALGCDVTWGPDGEVPGGG--KGFRFQDPSGHLLELF 109
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 28-142 1.65e-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: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 36.16  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157819477  28 HIVMTVKNIEDTTMFYSKILGMEV--TTFKGDRKALCFGDQKFNLHEVGKEFDPKAAHPIPGSLDVCLITETpLEEVMKR 105
Cdd:cd07264    3 YIVLYVDDFAASLRFYRDVLGLPPrfLHEEGEYAEFDTGETKLALFSRKEMARSGGPDRRGSAFELGFEVDD-VEATVEE 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 157819477 106 LKAFDVPIEEGPVSRT-GAKgpilSIYFRDPDRNLIEV 142
Cdd:cd07264   82 LVERGAEFVREPANKPwGQT----VAYVRDPDGNLIEI 115
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 11-52 3.29e-03

4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and metabolism, General function prediction only];


Pssm-ID: 442418 [Multi-domain]  Cd Length: 333  Bit Score: 36.41  E-value: 3.29e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 157819477  11 WRTSSQTPSPCLICRLDHIVMTVK--NIEDTTMFYSKILGMEVT 52
Cdd:COG3185  132 PLPGDAAPAGAGLTRIDHIGIAVPrgDLDEWVLFYEDVLGFEEI 175
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 33-82 5.48e-03

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


Pssm-ID: 319964  Cd Length: 114  Bit Score: 34.45  E-value: 5.48e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 157819477  33 VKNIEDTTMFYSKILGMEVTTFKGDRKALCFGDQKFNL--HEVGKEFDPKAA 82
Cdd:cd16357    6 VSDLEKSIDYWSDLLGMKVFEKSEKSALLGYGEDQAKLelVDIPEPVDHGTA 57
 
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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