NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1005601728|ref|WP_061686599|]
View 

MULTISPECIES: VOC family protein [Bacillus]

Protein Classification

VOC family protein( domain architecture ID 11164827)

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

CATH:  3.10.180.10
PubMed:  21820381

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
3-dmu-9_3-mt pfam06983
3-demethylubiquinone-9 3-methyltransferase; This family represents a conserved region ...
 6-132 6.81e-60

3-demethylubiquinone-9 3-methyltransferase; This family represents a conserved region approximately 100 residues long within a number of bacterial and archaeal 3-demethylubiquinone-9 3-methyltransferases (EC:2.1.1.64). Note that some family members contain more than one copy of this region, and that many members are hypothetical proteins.


:

Pssm-ID: 399756  Cd Length: 116  Bit Score: 180.19  E-value: 6.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005601728   6 QKITTFLMFEGKAEAAMNFYTSLFDQSEIVNISRYDENGPGKEGTVIQATFTLHGQEFMCIDSyvNHNFTFTPAMSLYVT 85
Cdd:pfam06983   1 QKITPCLWFDGQAEEAAEFYVSLFPNSEIGSVNRYPEDGPGKPGSVLTVEFTLNGQPFIALNG--GPNFKFNEAVSFQVT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1005601728  86 CDTEEEIETAFNKLAEDGAvlmplgayPFSkKFGWLNDKYGVSWQLT 132
Cdd:pfam06983  79 CKDQEEVDRYWNALSENGG--------PES-QCGWLKDKFGVSWQIV 116
 
Name Accession Description Interval E-value
3-dmu-9_3-mt pfam06983
3-demethylubiquinone-9 3-methyltransferase; This family represents a conserved region ...
 6-132 6.81e-60

3-demethylubiquinone-9 3-methyltransferase; This family represents a conserved region approximately 100 residues long within a number of bacterial and archaeal 3-demethylubiquinone-9 3-methyltransferases (EC:2.1.1.64). Note that some family members contain more than one copy of this region, and that many members are hypothetical proteins.


Pssm-ID: 399756  Cd Length: 116  Bit Score: 180.19  E-value: 6.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005601728   6 QKITTFLMFEGKAEAAMNFYTSLFDQSEIVNISRYDENGPGKEGTVIQATFTLHGQEFMCIDSyvNHNFTFTPAMSLYVT 85
Cdd:pfam06983   1 QKITPCLWFDGQAEEAAEFYVSLFPNSEIGSVNRYPEDGPGKPGSVLTVEFTLNGQPFIALNG--GPNFKFNEAVSFQVT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1005601728  86 CDTEEEIETAFNKLAEDGAvlmplgayPFSkKFGWLNDKYGVSWQLT 132
Cdd:pfam06983  79 CKDQEEVDRYWNALSENGG--------PES-QCGWLKDKFGVSWQIV 116
PhnB_like cd06588
Escherichia coli PhnB and similar proteins; The Escherichia coli phnB gene is found next to an ...
 8-132 5.79e-56

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: 170.53  E-value: 5.79e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005601728   8 ITTFLMFEGKAEAAMNFYTSLFDQSEIVNISRYDENGP----GKEGTVIQATFTLHGQEFMCIDSYVNHNFTFTPAMSLY 83
Cdd:cd06588     1 ITPYLWFNGNAEEALEFYAEVFPGGEILSLTRYGEGPPdfpeGDEGKVMHAEFTLGGQTLMASDDGPGFPFTFGNAISLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1005601728  84 VTCDTEEEIETAFNKLAEDGAVLMPLGAYPFSKKFGWLNDKYGVSWQLT 132
Cdd:cd06588    81 VDCDSQEEADRLFEKLSEGGEVLMPLQETFWGARYGWVKDKFGVSWQIN 129
COG3865 COG3865
Glyoxalase superfamily enzyme, possible 3-demethylubiquinone-9 3-methyltransferase [General ...
 6-135 4.74e-47

Glyoxalase superfamily enzyme, possible 3-demethylubiquinone-9 3-methyltransferase [General function prediction only];


Pssm-ID: 443074  Cd Length: 156  Bit Score: 149.15  E-value: 4.74e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005601728   6 QKITTFLMFEGKAEAAMNFYTSLFDQSEIVNISRYDENGP-GKEGTVIQATFTLHGQEFMCIdsyvNH--NFTFTPAMSL 82
Cdd:COG3865     2 QKITPCLWFDGQAEEAAEFYVSVFPDSRITAVTRYPEDGPgGPAGSVLTVEFTLAGQPFMAL----NGgpLFKFNEAVSF 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1005601728  83 YVTCDTEEEIETAFNKLAEDGAvlmplgaypfSKKFGWLNDKYGVSWQLTLAE 135
Cdd:COG3865    78 QVNCEDQAEVDRLWDALSAGGE----------ESQCGWLKDRFGLSWQIVPRR 120
 
Name Accession Description Interval E-value
3-dmu-9_3-mt pfam06983
3-demethylubiquinone-9 3-methyltransferase; This family represents a conserved region ...
 6-132 6.81e-60

3-demethylubiquinone-9 3-methyltransferase; This family represents a conserved region approximately 100 residues long within a number of bacterial and archaeal 3-demethylubiquinone-9 3-methyltransferases (EC:2.1.1.64). Note that some family members contain more than one copy of this region, and that many members are hypothetical proteins.


Pssm-ID: 399756  Cd Length: 116  Bit Score: 180.19  E-value: 6.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005601728   6 QKITTFLMFEGKAEAAMNFYTSLFDQSEIVNISRYDENGPGKEGTVIQATFTLHGQEFMCIDSyvNHNFTFTPAMSLYVT 85
Cdd:pfam06983   1 QKITPCLWFDGQAEEAAEFYVSLFPNSEIGSVNRYPEDGPGKPGSVLTVEFTLNGQPFIALNG--GPNFKFNEAVSFQVT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1005601728  86 CDTEEEIETAFNKLAEDGAvlmplgayPFSkKFGWLNDKYGVSWQLT 132
Cdd:pfam06983  79 CKDQEEVDRYWNALSENGG--------PES-QCGWLKDKFGVSWQIV 116
PhnB_like cd06588
Escherichia coli PhnB and similar proteins; The Escherichia coli phnB gene is found next to an ...
 8-132 5.79e-56

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: 170.53  E-value: 5.79e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005601728   8 ITTFLMFEGKAEAAMNFYTSLFDQSEIVNISRYDENGP----GKEGTVIQATFTLHGQEFMCIDSYVNHNFTFTPAMSLY 83
Cdd:cd06588     1 ITPYLWFNGNAEEALEFYAEVFPGGEILSLTRYGEGPPdfpeGDEGKVMHAEFTLGGQTLMASDDGPGFPFTFGNAISLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1005601728  84 VTCDTEEEIETAFNKLAEDGAVLMPLGAYPFSKKFGWLNDKYGVSWQLT 132
Cdd:cd06588    81 VDCDSQEEADRLFEKLSEGGEVLMPLQETFWGARYGWVKDKFGVSWQIN 129
COG3865 COG3865
Glyoxalase superfamily enzyme, possible 3-demethylubiquinone-9 3-methyltransferase [General ...
 6-135 4.74e-47

Glyoxalase superfamily enzyme, possible 3-demethylubiquinone-9 3-methyltransferase [General function prediction only];


Pssm-ID: 443074  Cd Length: 156  Bit Score: 149.15  E-value: 4.74e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005601728   6 QKITTFLMFEGKAEAAMNFYTSLFDQSEIVNISRYDENGP-GKEGTVIQATFTLHGQEFMCIdsyvNH--NFTFTPAMSL 82
Cdd:COG3865     2 QKITPCLWFDGQAEEAAEFYVSVFPDSRITAVTRYPEDGPgGPAGSVLTVEFTLAGQPFMAL----NGgpLFKFNEAVSF 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1005601728  83 YVTCDTEEEIETAFNKLAEDGAvlmplgaypfSKKFGWLNDKYGVSWQLTLAE 135
Cdd:COG3865    78 QVNCEDQAEVDRLWDALSAGGE----------ESQCGWLKDRFGLSWQIVPRR 120
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
7-131 3.11e-18

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 74.51  E-value: 3.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005601728   7 KITTFLMFEGkAEAAMNFYTSLFDqSEIVNISRYDEngpgkeGTVIQATFTLHGQEFMCIDSYVNHNFTFTPAMSLYVTC 86
Cdd:COG2764     1 SVTPYLVVDD-AEEALEFYEDVFG-FEVVFRMTDPD------GKIMHAELRIGGSVLMLSDAPPDSPAAEGNGVSLSLYV 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1005601728  87 DteeEIETAFNKLAEDGA-VLMPLGAYPFSKKFGWLNDKYGVSWQL 131
Cdd:COG2764    73 D---DVDALFARLVAAGAtVVMPLQDTFWGDRFGMVRDPFGVLWMI 115
VOC_like cd07246
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 17-132 2.44e-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: 319910 [Multi-domain]  Cd Length: 124  Bit Score: 46.14  E-value: 2.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005601728  17 KAEAAMNFYTSLFDQSEIvnisrydENGPGKEGTVIQATFTLHGQEFMCIDSYVNHNFTFTPA-------MSLYVtcdte 89
Cdd:cd07246    11 DAAAAIAFYKKAFGAEEL-------GRTTQEDGRVGHAELRIGGTVVMVADENPERGALSPTKlggtpviFHLYV----- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1005601728  90 EEIETAFNKLAEDGAVL-MPLGAYPFSKKFGWLNDKYGVSWQLT 132
Cdd:cd07246    79 EDVDATFARAVAAGAVVvEPVEDQFWGDRVGKVKDPFGHVWWLA 122
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
18-131 2.58e-05

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 40.89  E-value: 2.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005601728  18 AEAAMNFYTSLFDQSEIvnisryDENGPGKEGTVIQATFTLHGQEFMCIDSY-VNHNFTFTPAMSLYVTCDTEEEIETAF 96
Cdd:pfam00903  12 LEKSLDFYTDVLGFKLV------EETDAGEEGGLRSAFFLAGGRVLELLLNEtPPPAAAGFGGHHIAFIAFSVDDVDAAY 85

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1005601728  97 NKLAEDGA-VLMPLGAYPFSKKFGWLNDKYGVSWQL 131
Cdd:pfam00903  86 DRLKAAGVeIVREPGRHGWGGRYSYFRDPDGNLIEL 121
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH