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Conserved domains on  [gi|410516948|sp|A6NK44|]
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RecName: Full=Glyoxalase domain-containing protein 5

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 ...
 35-157 5.63e-77

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: 224.80  E-value: 5.63e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410516948  35 IRRLDHIVMTVKSIKDTTMFYSKILGMEVMTFKEDRKALCFGDQKFNLHEVGKEFEPKAAHPVPGSLDICLITEVPLEEM 114
Cdd:cd07253    1 IKRLDHLVLTVKDIERTIDFYTKVLGMTVVTFKEGRKALRFGNQKINLHQKGKEFEPKASAPTPGSADLCFITETPIDEV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 410516948 115 IQHLKACDVPIEEGPVPRTGAKGPIMSIYFRDPDRNLIEVSNY 157
Cdd:cd07253   81 LEHLEACGVTIEEGPVKRTGALGPILSIYFRDPDGNLIELSNY 123
 
Name Accession Description Interval E-value
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 35-157 5.63e-77

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: 224.80  E-value: 5.63e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410516948  35 IRRLDHIVMTVKSIKDTTMFYSKILGMEVMTFKEDRKALCFGDQKFNLHEVGKEFEPKAAHPVPGSLDICLITEVPLEEM 114
Cdd:cd07253    1 IKRLDHLVLTVKDIERTIDFYTKVLGMTVVTFKEGRKALRFGNQKINLHQKGKEFEPKASAPTPGSADLCFITETPIDEV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 410516948 115 IQHLKACDVPIEEGPVPRTGAKGPIMSIYFRDPDRNLIEVSNY 157
Cdd:cd07253   81 LEHLEACGVTIEEGPVKRTGALGPILSIYFRDPDGNLIELSNY 123
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 36-157 4.92e-19

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: 77.73  E-value: 4.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410516948  36 RRLDHIVMTVKSIKDTTMFYSKILGMEV---MTFKEDRKALCF----GDQKFNLHevgkEFEPKAAHPVPGSLD-ICLIT 107
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELvkrTDFGDGGFGHAFlrlgDGTELELF----EAPGAAPAPGGGGLHhLAFRV 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 410516948 108 EvPLEEMIQHLKACDVPIEEGpvPRTGAKGPImSIYFRDPDRNLIEVSNY 157
Cdd:COG0346   77 D-DLDAAYARLRAAGVEIEGE--PRDRAYGYR-SAYFRDPDGNLIELVEP 122
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
37-154 1.80e-09

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 52.45  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410516948   37 RLDHIVMTVKSIKDTTMFYSKILGMEVmTFKEDRKALCFGDQKF-----NLHEVGKEFEPKAAHPVPGSLDICLITEVP- 110
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKL-VEETDAGEEGGLRSAFflaggRVLELLLNETPPPAAAGFGGHHIAFIAFSVd 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 410516948  111 -LEEMIQHLKACDVPIEEGPvPRTGAKGpiMSIYFRDPDRNLIEV 154
Cdd:pfam00903  80 dVDAAYDRLKAAGVEIVREP-GRHGWGG--RYSYFRDPDGNLIEL 121
PRK04101 PRK04101
metallothiol transferase FosB;
106-154 1.16e-03

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 37.23  E-value: 1.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 410516948 106 ITEVPLEEMIQHLKACDVPIEEGpvpRTGAKGPIMSIYFRDPDRNLIEV 154
Cdd:PRK04101  71 IEEEDFDHWYQRLKENDVNILPG---RERDERDKKSIYFTDPDGHKFEF 116
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 26-97 1.46e-03

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: 37.09  E-value: 1.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 410516948   26 SSQTPPPCLIRRLDHIVMTVKSIKDTTMFYSKILGMEVMTFKEdrkalcFGDQKFNLHEVGkeFEPKAAHPV 97
Cdd:TIGR00068   6 DLVADPKTKKRRLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRD------FPEMKFSLAFLG--YGDETSAAV 69
 
Name Accession Description Interval E-value
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 35-157 5.63e-77

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: 224.80  E-value: 5.63e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410516948  35 IRRLDHIVMTVKSIKDTTMFYSKILGMEVMTFKEDRKALCFGDQKFNLHEVGKEFEPKAAHPVPGSLDICLITEVPLEEM 114
Cdd:cd07253    1 IKRLDHLVLTVKDIERTIDFYTKVLGMTVVTFKEGRKALRFGNQKINLHQKGKEFEPKASAPTPGSADLCFITETPIDEV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 410516948 115 IQHLKACDVPIEEGPVPRTGAKGPIMSIYFRDPDRNLIEVSNY 157
Cdd:cd07253   81 LEHLEACGVTIEEGPVKRTGALGPILSIYFRDPDGNLIELSNY 123
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 36-157 4.92e-19

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: 77.73  E-value: 4.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410516948  36 RRLDHIVMTVKSIKDTTMFYSKILGMEV---MTFKEDRKALCF----GDQKFNLHevgkEFEPKAAHPVPGSLD-ICLIT 107
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELvkrTDFGDGGFGHAFlrlgDGTELELF----EAPGAAPAPGGGGLHhLAFRV 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 410516948 108 EvPLEEMIQHLKACDVPIEEGpvPRTGAKGPImSIYFRDPDRNLIEVSNY 157
Cdd:COG0346   77 D-DLDAAYARLRAAGVEIEGE--PRDRAYGYR-SAYFRDPDGNLIELVEP 122
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
35-154 2.74e-16

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 70.76  E-value: 2.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410516948  35 IRRLDHIVMTVKSIKDTTMFYSKILGMEVMTFKEDRKALCF--GDQKFNLHEVGkefEPKAAHPVPGSLDICLitEVP-- 110
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRAdgGEHLLVLEEAP---GAPPRPGAAGLDHVAF--RVPsr 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 410516948 111 --LEEMIQHLKACDVPIeEGPVPRTGAKgpimSIYFRDPDRNLIEV 154
Cdd:COG2514   76 adLDAALARLAAAGVPV-EGAVDHGVGE----SLYFRDPDGNLIEL 116
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 54-154 4.26e-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: 4.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410516948  54 FYSKILGMEVMTfKEDRKAlCF--GDQKFNLHEVGKEFEPKAAHPVP-----GSLDICL-ITEVPLEEMIQHLKACDVPI 125
Cdd:cd08354   17 FYEDVLGLKPML-RSGRHA-FFrlGPQVLLVFDPGATSKDVRTGEVPghgasGHGHFAFaVPTEELAAWEARLEAKGVPI 94

                         90       100
                 ....*....|....*....|....*....
gi 410516948 126 EEgpVPRTGAKGpiMSIYFRDPDRNLIEV 154
Cdd:cd08354   95 ES--YTQWPEGG--KSLYFRDPAGNLVEL 119
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
37-154 1.80e-09

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 52.45  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410516948   37 RLDHIVMTVKSIKDTTMFYSKILGMEVmTFKEDRKALCFGDQKF-----NLHEVGKEFEPKAAHPVPGSLDICLITEVP- 110
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKL-VEETDAGEEGGLRSAFflaggRVLELLLNETPPPAAAGFGGHHIAFIAFSVd 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 410516948  111 -LEEMIQHLKACDVPIEEGPvPRTGAKGpiMSIYFRDPDRNLIEV 154
Cdd:pfam00903  80 dVDAAYDRLKAAGVEIVREP-GRHGWGG--RYSYFRDPDGNLIEL 121
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 40-154 7.89e-08

vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases.


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 47.90  E-value: 7.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410516948  40 HIVMTVKSIKDTTMFYSKILGMEVMTFKEDRKALCFGD---QKFNLHEVGKEFEPKAAHPVpgslDICLITEvPLEEMIQ 116
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGFAFLRLgpgLRLALLEGPEPERPGGGGLF----HLAFEVD-DVDEVDE 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 410516948 117 HL---KACDVPIEEGPVPRTGAKgpimSIYFRDPDRNLIEV 154
Cdd:cd06587   76 RLreaGAEGELVAPPVDDPWGGR----SFYFRDPDGNLIEF 112
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 38-154 8.96e-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: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 48.08  E-value: 8.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410516948  38 LDHIVMTVKSIKDTTMFYSKILGMEVMtfkEDRKALCFGDQKFNLHE-------VGKEFEPKAAHPVPGSLD-ICLitEV 109
Cdd:cd07245    1 LDHVALACPDLERARRFYTDVLGLEEV---PRPPFLKFGGAWLYLGGgqqihlvVEQNPSELPRPEHPGRDRhPSF--SV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 410516948 110 P-LEEMIQHLKACDVPIEEGPVPRTGakgpIMSIYFRDPDRNLIEV 154
Cdd:cd07245   76 PdLDALKQRLKEAGIPYTESTSPGGG----VTQLFFRDPDGNRLEF 117
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 37-154 4.12e-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: 4.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410516948  37 RLDHIVMTVKSIKDTTMFYSKILGMEVMTfKEDRKALCFGDQKFNLHEVGKEFE-PKAAHPVPGsLD---ICLITEVPLE 112
Cdd:cd07255    2 RIGRVTLKVADLERQSAFYQNVIGLSVLK-QNASRAYLGVDGKQVLLVLEAIPDaVLAPRSTTG-LYhfaILLPDRKALG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 410516948 113 EMIQHLkacdvpIEEGPVprTGAKGPIMS--IYFRDPDRNLIEV 154
Cdd:cd07255   80 RALAHL------AEHGPL--IGAADHGVSeaIYLSDPEGNGIEI 115
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 106-154 9.86e-05

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


Pssm-ID: 319951 [Multi-domain]  Cd Length: 131  Bit Score: 40.03  E-value: 9.86e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 410516948 106 ITEVPLEEMIQHLKACDVPIEEGpvpRTGAKGPIMSIYFRDPDRNLIEV 154
Cdd:cd08363   67 IDEEDLDAFKERLKDNGVNILEG---RKRDILEGQSIYFTDPDGHLFEL 112
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 40-154 4.44e-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: 38.08  E-value: 4.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410516948  40 HIVMTVKSIKDTTMFYSKILGMEVmTFKEDRKALC---FGDQKFNLHEVGKEFEPKAAHPVPGSLDICLITEvPLEEMIQ 116
Cdd:cd07264    3 YIVLYVDDFAASLRFYRDVLGLPP-RFLHEEGEYAefdTGETKLALFSRKEMARSGGPDRRGSAFELGFEVD-DVEATVE 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 410516948 117 HLKACDVPIEEGPVPRT-GAKgpimSIYFRDPDRNLIEV 154
Cdd:cd07264   81 ELVERGAEFVREPANKPwGQT----VAYVRDPDGNLIEI 115
PRK04101 PRK04101
metallothiol transferase FosB;
106-154 1.16e-03

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 37.23  E-value: 1.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 410516948 106 ITEVPLEEMIQHLKACDVPIEEGpvpRTGAKGPIMSIYFRDPDRNLIEV 154
Cdd:PRK04101  71 IEEEDFDHWYQRLKENDVNILPG---RERDERDKKSIYFTDPDGHKFEF 116
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 26-97 1.46e-03

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: 37.09  E-value: 1.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 410516948   26 SSQTPPPCLIRRLDHIVMTVKSIKDTTMFYSKILGMEVMTFKEdrkalcFGDQKFNLHEVGkeFEPKAAHPV 97
Cdd:TIGR00068   6 DLVADPKTKKRRLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRD------FPEMKFSLAFLG--YGDETSAAV 69
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 37-154 1.78e-03

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 36.15  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410516948  37 RLDHIVMTVKSIKDTTMFYSKILGMEV-MTFKEDRKALCFgdqKFNLHEVGkEFEPKAAHPVPGSLDICLITEvPLEEMI 115
Cdd:COG3324    4 TIVWVELPVDDLERAKAFYEEVFGWTFeDDAGPGGDYAEF---DTDGGQVG-GLMPGAEEPGGPGWLLYFAVD-DLDAAV 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 410516948 116 QHLKACDVPIEEGPVPRTGAkGPIMsiYFRDPDRNLIEV 154
Cdd:COG3324   79 ARVEAAGGTVLRPPTDIPPW-GRFA--VFRDPEGNRFGL 114
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 23-64 2.63e-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: 37.18  E-value: 2.63e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 410516948  23 WRDSSQTPPPCLIRRLDHIVMTVK--SIKDTTMFYSKILGMEVM 64
Cdd:COG3185  132 PLPGDAAPAGAGLTRIDHIGIAVPrgDLDEWVLFYEDVLGFEEI 175
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 40-155 3.94e-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: 35.37  E-value: 3.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410516948  40 HIVMTVKSIKDTTMFYSKILGMEVMtfKEDRKAL---CFGDQKFNL--HEVgkefepkaahPVPGSLDICLITEVP--LE 112
Cdd:cd16360    1 YAELGVPDLEKALEFYTDVLGLQVA--KRDGNSVylrGYEDEHHSLvlYEA----------PEAGLKHFAFEVASEedLE 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 410516948 113 EMIQHLKACDVPIEEGPVPRTGAKGpiMSIYFRDPDRNLIEVS 155
Cdd:cd16360   69 RAAASLTALGCDVTWGPDGEVPGGG--KGFRFQDPSGHLLELF 109
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 38-148 6.32e-03

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: 34.95  E-value: 6.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410516948  38 LDHIVMTVKSIKDTTMFYSKILGMEVMTfKEDRKA-LCFGDQKFNLhEVGKEFEPKA--AHPVPGsldiclITEVPLEEM 114
Cdd:cd07244    2 INHITLAVSDLERSLAFYVDLLGFKPHV-RWDKGAyLTAGDLWLCL-SLDPAAEPSPdyTHIAFT------VSEEDFEEL 73

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 410516948 115 IQHLKACDVPI-----EEGPvprtgakgpimSIYFRDPD 148
Cdd:cd07244   74 SERLRAAGVKIwqensSEGD-----------SLYFLDPD 101
 
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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