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Conserved domains on  [gi|227351247|gb|EEJ41538|]
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glyoxalase family protein [Limosilactobacillus vaginalis DSM 5837 = ATCC 49540]

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 ...
 14-132 8.16e-17

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: 71.18  E-value: 8.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351247  14 LAHVGIPTDDLKKTIAFWEK-LGFKKQGQFDTDDQGHQVVFMKVG-HLMLEIWDSDGA--VHKTGAINHISLNVEDADNA 89
Cdd:COG0346    3 LHHVTLRVSDLEASLAFYTDvLGLELVKRTDFGDGGFGHAFLRLGdGTELELFEAPGAapAPGGGGLHHLAFRVDDLDAA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 227351247  90 FKAAKEEGFDVKEDEVQHldfwKHGIKFFNIVGPNDETIEFCE 132
Cdd:COG0346   83 YARLRAAGVEIEGEPRDR----AYGYRSAYFRDPDGNLIELVE 121
 
Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 14-132 8.16e-17

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: 71.18  E-value: 8.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351247  14 LAHVGIPTDDLKKTIAFWEK-LGFKKQGQFDTDDQGHQVVFMKVG-HLMLEIWDSDGA--VHKTGAINHISLNVEDADNA 89
Cdd:COG0346    3 LHHVTLRVSDLEASLAFYTDvLGLELVKRTDFGDGGFGHAFLRLGdGTELELFEAPGAapAPGGGGLHHLAFRVDDLDAA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 227351247  90 FKAAKEEGFDVKEDEVQHldfwKHGIKFFNIVGPNDETIEFCE 132
Cdd:COG0346   83 YARLRAAGVEIEGEPRDR----AYGYRSAYFRDPDGNLIELVE 121
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 16-132 1.74e-12

Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) interconverts (2R)-methylmalonyl-CoA and (2S)-methylmalonyl-CoA. MMCE has been found in bacteria, archaea, and in animals. In eukaryotes, MMCE is an essential enzyme in a pathway that converts propionyl-CoA to succinyl-CoA, and is important in the breakdown of odd-chain length fatty acids, branched-chain amino acids, and other metabolites. In bacteria, MMCE participates in the reverse pathway for propionate fermentation, glyoxylate regeneration, and the biosynthesis of polyketide antibiotics. MMCE is closely related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319912 [Multi-domain]  Cd Length: 127  Bit Score: 59.90  E-value: 1.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351247  16 HVGIPTDDLKKTIAFWEK-LGFKKQGQFDTDDQGHQVVFMKVGHLMLEI---WDSDGAVHKT-----GAINHISLNVEDA 86
Cdd:cd07249    3 HIGIAVPDLDEALKFYEDvLGVKVSEPEELEEQGVRVAFLELGNTQIELlepLGEDSPIAKFldkkgGGLHHIAFEVDDI 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 227351247  87 DNAFKAAKEEGFDVKEDEVQHLDFwKHGIKFFNivgPNDET---IEFCE 132
Cdd:cd07249   83 DAAVEELKAQGVRLLSEGPRIGAH-GKRVAFLH---PKDTGgvlIELVE 127
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
16-100 3.55e-08

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 48.04  E-value: 3.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351247   16 HVGIPTDDLKKTIAFWEK-LGFKKQGQFDTDDQGHQVVFMKVGHLMLEI-----WDSDG--AVHKTGaINHISLNVEDAD 87
Cdd:pfam13669   2 HVGIAVPDLDRALALWGAlLGLGPEGDYRSEPQNVDLAFALLGDGPVEVeliqpLDGDSplARHGPG-LHHLAYWVDDLD 80

                          90
                  ....*....|...
gi 227351247   88 NAFKAAKEEGFDV 100
Cdd:pfam13669  81 AAVARLLDQGYRV 93
 
Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 14-132 8.16e-17

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: 71.18  E-value: 8.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351247  14 LAHVGIPTDDLKKTIAFWEK-LGFKKQGQFDTDDQGHQVVFMKVG-HLMLEIWDSDGA--VHKTGAINHISLNVEDADNA 89
Cdd:COG0346    3 LHHVTLRVSDLEASLAFYTDvLGLELVKRTDFGDGGFGHAFLRLGdGTELELFEAPGAapAPGGGGLHHLAFRVDDLDAA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 227351247  90 FKAAKEEGFDVKEDEVQHldfwKHGIKFFNIVGPNDETIEFCE 132
Cdd:COG0346   83 YARLRAAGVEIEGEPRDR----AYGYRSAYFRDPDGNLIELVE 121
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 16-132 1.74e-12

Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) interconverts (2R)-methylmalonyl-CoA and (2S)-methylmalonyl-CoA. MMCE has been found in bacteria, archaea, and in animals. In eukaryotes, MMCE is an essential enzyme in a pathway that converts propionyl-CoA to succinyl-CoA, and is important in the breakdown of odd-chain length fatty acids, branched-chain amino acids, and other metabolites. In bacteria, MMCE participates in the reverse pathway for propionate fermentation, glyoxylate regeneration, and the biosynthesis of polyketide antibiotics. MMCE is closely related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319912 [Multi-domain]  Cd Length: 127  Bit Score: 59.90  E-value: 1.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351247  16 HVGIPTDDLKKTIAFWEK-LGFKKQGQFDTDDQGHQVVFMKVGHLMLEI---WDSDGAVHKT-----GAINHISLNVEDA 86
Cdd:cd07249    3 HIGIAVPDLDEALKFYEDvLGVKVSEPEELEEQGVRVAFLELGNTQIELlepLGEDSPIAKFldkkgGGLHHIAFEVDDI 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 227351247  87 DNAFKAAKEEGFDVKEDEVQHLDFwKHGIKFFNivgPNDET---IEFCE 132
Cdd:cd07249   83 DAAVEELKAQGVRLLSEGPRIGAH-GKRVAFLH---PKDTGgvlIELVE 127
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 16-130 4.33e-09

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: 50.60  E-value: 4.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351247  16 HVGIPTDDLKKTIAFWEK-LGFKKQGQFDTDDqghqVVFMKVG-HLMLEIWDSDGAVHKTGA-INHISLNVEDADNAFKA 92
Cdd:cd06587    1 HVALRVPDLDASVAFYEEvLGFEVVSRNEGGG----FAFLRLGpGLRLALLEGPEPERPGGGgLFHLAFEVDDVDEVDER 76

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 227351247  93 AKEEGFDVKEDEVQHLDFWkhGIKFFNIVGPNDETIEF 130
Cdd:cd06587   77 LREAGAEGELVAPPVDDPW--GGRSFYFRDPDGNLIEF 112
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 17-97 1.59e-08

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 49.44  E-value: 1.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351247  17 VGIPTDDLKKTIAFWEKLGFKKQGQFdTDDqghQVVFMKVGH---LML------------EIWDSDGAvhkTGAInhISL 81
Cdd:COG3607    7 VNLPVADLERSRAFYEALGFTFNPQF-SDE---GAACFVLGEgivLMLlprekfatftgkPIADATGF---TEVL--LAL 77

                         90
                 ....*....|....*....
gi 227351247  82 NV---EDADNAFKAAKEEG 97
Cdd:COG3607   78 NVesrEEVDALVAKALAAG 96
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
16-100 3.55e-08

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 48.04  E-value: 3.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351247   16 HVGIPTDDLKKTIAFWEK-LGFKKQGQFDTDDQGHQVVFMKVGHLMLEI-----WDSDG--AVHKTGaINHISLNVEDAD 87
Cdd:pfam13669   2 HVGIAVPDLDRALALWGAlLGLGPEGDYRSEPQNVDLAFALLGDGPVEVeliqpLDGDSplARHGPG-LHHLAYWVDDLD 80

                          90
                  ....*....|...
gi 227351247   88 NAFKAAKEEGFDV 100
Cdd:pfam13669  81 AAVARLLDQGYRV 93
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
14-130 1.17e-07

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 47.06  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351247   14 LAHVGIPTDDLKKTIAFWEK-LGFKKQGQFDTD-DQGHQVVFMKVGHLMLEI---WDSDGAVHKTGA--INHISLNVEDA 86
Cdd:pfam00903   2 IDHVALRVGDLEKSLDFYTDvLGFKLVEETDAGeEGGLRSAFFLAGGRVLELllnETPPPAAAGFGGhhIAFIAFSVDDV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 227351247   87 DNAFKAAKEEGFDVKEDEVQHldFWKHGIKFFNivGPNDETIEF 130
Cdd:pfam00903  82 DAAYDRLKAAGVEIVREPGRH--GWGGRYSYFR--DPDGNLIEL 121
VOC_like cd08353
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 16-112 3.88e-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: 319941  Cd Length: 142  Bit Score: 46.03  E-value: 3.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351247  16 HVGIPTDDLKKTIAFWEKLGFKKQGQ-------FDT----DDQGHQVVFMKV--GHLMLE----IWDSDGAVHKTGAIN- 77
Cdd:cd08353    6 HVGIVVEDLDAAIAFFTELGLELEGRmtvegewADRvvglDGVRVEIAMLRTpdGHGRLElskfLTPAAIPGHRPAPANa 85

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 227351247  78 ----HISLNVEDADNAFKAAKEEGFDVKEDEVQHLDFWK 112
Cdd:cd08353   86 lglrHVAFAVDDIDAVVARLRKHGAELVGEVVQYEDSYR 124
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
14-111 2.12e-06

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 44.18  E-value: 2.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351247  14 LAHVGIPTDDLKKTIAFWEK-LGFKKqgqfdTDDQGHQVVF-MKVGHLMLEIWDSDGAVHKTGA--INHISLNVEDA--- 86
Cdd:COG2514    4 LGHVTLRVRDLERSAAFYTDvLGLEV-----VEREGGRVYLrADGGEHLLVLEEAPGAPPRPGAagLDHVAFRVPSRadl 78

                         90       100
                 ....*....|....*....|....*
gi 227351247  87 DNAFKAAKEEGFDVkEDEVQHLDFW 111
Cdd:COG2514   79 DAALARLAAAGVPV-EGAVDHGVGE 102
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 14-100 3.29e-06

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 43.09  E-value: 3.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351247  14 LAHVGIPTDDLKKTIAFWEK-LGFKKqgQFDTDDQGHQVVFMKVGHLMLEIWDSDGAVHKTGAinHISLNVEDADNAFKA 92
Cdd:COG3324    5 IVWVELPVDDLERAKAFYEEvFGWTF--EDDAGPGGDYAEFDTDGGQVGGLMPGAEEPGGPGW--LLYFAVDDLDAAVAR 80


                 ....*...
gi 227351247  93 AKEEGFDV 100
Cdd:COG3324   81 VEAAGGTV 88
VOC_BsYqjT cd07242
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; The vicinal ...
 14-85 2.71e-05

vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; 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: 319906  Cd Length: 126  Bit Score: 40.93  E-value: 2.71e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227351247  14 LAHVGIPTDDLKKTIAFWEKLGFKKQGQFDTDDQGHQvvFMKVGHLMLEIWDSDGAV----HKTG-AINHISLNVED 85
Cdd:cd07242    2 VSHVELAVSDLHRSFKWFEWILGLGWKEYDTWSFGPS--WKLSGGSLLVVQQTDEFAtpefDRARvGLNHLAFHAES 76
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 16-100 5.22e-05

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: 41.41  E-value: 5.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351247  16 HVGI--PTDDLKKTIAFWEK-LGFKKQGQFD--TDDQGHQVVFMKV--GHLMLEI---WDSDGAVHK-----TGA-INHI 79
Cdd:COG3185  149 HIGIavPRGDLDEWVLFYEDvLGFEEIREEDieDPYQGVRSAVLQSpdGKVRIPLnepTSPDSQIAEflekyRGEgIQHI 228

                         90       100
                 ....*....|....*....|.
gi 227351247  80 SLNVEDADNAFKAAKEEGFDV 100
Cdd:COG3185  229 AFATDDIEATVAALRARGVRF 249
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 14-97 3.96e-04

N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth disturbances caused by high osmolarity and a high concentration of A-factor, a microbial hormone, during the early growth phase in Streptomyces griseus. A-factor (2-isocapryloyl-3R-hydroxymethyl-gamma-butyrolactone) controls morphological differentiation and secondary metabolism in Streptomyces griseus. It is a chemical signaling molecule that at a very low concentration acts as a switch for yellow pigment production, aerial mycelium formation, streptomycin production, and streptomycin resistance. The structure and amino acid sequence of SgaA are closely related to a group of antibiotics resistance proteins, including bleomycin resistance protein, mitomycin resistance protein, and fosfomycin resistance proteins. SgaA might also function as a streptomycin resistance protein.


Pssm-ID: 319911 [Multi-domain]  Cd Length: 114  Bit Score: 37.63  E-value: 3.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351247  14 LAHVGIPTDDLKKTIAFWEKLgFKKQGQFDTDDQGHQVVFMKVGHLMLEIWDSDGAVHKTGAINHISLNVEDADNAFKAA 93
Cdd:cd07247    1 PVWFELPTTDLERAKAFYGAV-FGWTFEDEGDGGGDYALFTAGGGAVGGLMRAPEEVAGAPPGWLIYFAVDDLDAALARV 79


                 ....
gi 227351247  94 KEEG 97
Cdd:cd07247   80 EAAG 83
VOC_like cd09012
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 17-61 5.70e-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: 319954  Cd Length: 127  Bit Score: 37.36  E-value: 5.70e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 227351247  17 VGIPTDDLKKTIAFWEKLGFKKQGQFdTDDQGHQVVFMKVGHLML 61
Cdd:cd09012    4 INLPVTDLEASTAFYEALGFKKNPQF-SDEHASCMVVSDNIFVML 47
 
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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