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Conserved domains on  [gi|18422918|ref|NP_568698|]
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Lactoylglutathione lyase / glyoxalase I family protein [Arabidopsis thaliana]

Protein Classification

VOC family protein( domain architecture ID 10163498)

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
VOC_like cd07246
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 24-155 4.25e-36

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: 319910 [Multi-domain]  Cd Length: 124  Bit Score: 121.25  E-value: 4.25e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422918  24 TEFKQMLLVEaqKVGDAVTFYKSAFGAIESGHSlypkrklDQELPHVLSSELNLAGSSFVVCDVSSLPG-FSTAKSEGSG 102
Cdd:cd07246   1 TTVSPYLVVE--DAAAAIAFYKKAFGAEELGRT-------TQEDGRVGHAELRIGGTVVMVADENPERGaLSPTKLGGTP 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 18422918 103 VTFLLGTKDAEAAVAKAVDAGAVKVEVTEAEVELGFKGKVTDPFGVTWIFAEK 155
Cdd:cd07246  72 VIFHLYVEDVDATFARAVAAGAVVVEPVEDQFWGDRVGKVKDPFGHVWWLATP 124
 
Name Accession Description Interval E-value
VOC_like cd07246
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 24-155 4.25e-36

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: 319910 [Multi-domain]  Cd Length: 124  Bit Score: 121.25  E-value: 4.25e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422918  24 TEFKQMLLVEaqKVGDAVTFYKSAFGAIESGHSlypkrklDQELPHVLSSELNLAGSSFVVCDVSSLPG-FSTAKSEGSG 102
Cdd:cd07246   1 TTVSPYLVVE--DAAAAIAFYKKAFGAEELGRT-------TQEDGRVGHAELRIGGTVVMVADENPERGaLSPTKLGGTP 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 18422918 103 VTFLLGTKDAEAAVAKAVDAGAVKVEVTEAEVELGFKGKVTDPFGVTWIFAEK 155
Cdd:cd07246  72 VIFHLYVEDVDATFARAVAAGAVVVEPVEDQFWGDRVGKVKDPFGHVWWLATP 124
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
37-154 1.67e-11

Zn-dependent glyoxalase, PhnB family [Energy production and conversion];


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 57.94  E-value: 1.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422918  37 VGDAVTFYKSAFGAIESGHSLYPKRKLDqelpHVlssELNLAGSSFVVCDVSSlpgfSTAKSEGSGVTFLLGTKDAEAAV 116
Cdd:COG2764  11 AEEALEFYEDVFGFEVVFRMTDPDGKIM----HA---ELRIGGSVLMLSDAPP----DSPAAEGNGVSLSLYVDDVDALF 79

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 18422918 117 AKAVDAGA-VKVEVTEAEVELGFkGKVTDPFGVTWIFAE 154
Cdd:COG2764  80 ARLVAAGAtVVMPLQDTFWGDRF-GMVRDPFGVLWMINT 117
 
Name Accession Description Interval E-value
VOC_like cd07246
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 24-155 4.25e-36

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: 319910 [Multi-domain]  Cd Length: 124  Bit Score: 121.25  E-value: 4.25e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422918  24 TEFKQMLLVEaqKVGDAVTFYKSAFGAIESGHSlypkrklDQELPHVLSSELNLAGSSFVVCDVSSLPG-FSTAKSEGSG 102
Cdd:cd07246   1 TTVSPYLVVE--DAAAAIAFYKKAFGAEELGRT-------TQEDGRVGHAELRIGGTVVMVADENPERGaLSPTKLGGTP 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 18422918 103 VTFLLGTKDAEAAVAKAVDAGAVKVEVTEAEVELGFKGKVTDPFGVTWIFAEK 155
Cdd:cd07246  72 VIFHLYVEDVDATFARAVAAGAVVVEPVEDQFWGDRVGKVKDPFGHVWWLATP 124
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
37-154 1.67e-11

Zn-dependent glyoxalase, PhnB family [Energy production and conversion];


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 57.94  E-value: 1.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422918  37 VGDAVTFYKSAFGAIESGHSLYPKRKLDqelpHVlssELNLAGSSFVVCDVSSlpgfSTAKSEGSGVTFLLGTKDAEAAV 116
Cdd:COG2764  11 AEEALEFYEDVFGFEVVFRMTDPDGKIM----HA---ELRIGGSVLMLSDAPP----DSPAAEGNGVSLSLYVDDVDALF 79

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 18422918 117 AKAVDAGA-VKVEVTEAEVELGFkGKVTDPFGVTWIFAE 154
Cdd:COG2764  80 ARLVAAGAtVVMPLQDTFWGDRF-GMVRDPFGVLWMINT 117
PhnB_like cd06588
Escherichia coli PhnB and similar proteins; The Escherichia coli phnB gene is found next to an ...
 39-150 1.12e-06

Escherichia coli PhnB and similar proteins; The Escherichia coli phnB gene is found next to an operon of fourteen genes (phnC-to-phnP) related to the cleavage of carbon-phosphorus (C-P) bonds in unactivated alkylphosphonates, supporting bacterial growth on alkylphosphonates as the sole phosphorus source. It was originally considered part of that operon. PhnB appears to play no direct catalytic role in the usage of alkylphosphonate. Although many of the proteins in this family have been annotated as 3-demethylubiquinone-9 3-methyltransferase enzymes by automatic annotation programs, the experimental evidence for this assignment is lacking. In Escherichia coli, the gene coding 3-demethylubiquinone-9 3-methyltransferase enzyme is ubiG, which belongs to the AdoMet-MTase protein family. PhnB-like proteins adopt a structural fold similar to bleomycin resistance proteins, glyoxalase I, and type I extradiol dioxygenases.


Pssm-ID: 319899  Cd Length: 129  Bit Score: 45.34  E-value: 1.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18422918  39 DAVTFYKSAFGA--IES--GHSLYPKRKLDQELPHVLSSELNLAGSSFVVCDvsSLPGFSTAKSEGsgVTFLLGTKD--- 111
Cdd:cd06588  13 EALEFYAEVFPGgeILSltRYGEGPPDFPEGDEGKVMHAEFTLGGQTLMASD--DGPGFPFTFGNA--ISLSVDCDSqee 88

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 18422918 112 AEAAVAKAVDAGAVKVEVTEAEVELGFkGKVTDPFGVTW 150
Cdd:cd06588  89 ADRLFEKLSEGGEVLMPLQETFWGARY-GWVKDKFGVSW 126
 
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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