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Conserved domains on  [gi|498359106|ref|WP_010673262|]
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MULTISPECIES: VOC family protein [Aeromonas]

Protein Classification

VOC family protein( domain architecture ID 10159541)

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
PhnB_like cd06588
Escherichia coli PhnB and similar proteins; The Escherichia coli phnB gene is found next to an ...
 4-140 1.82e-35

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: 119.30  E-value: 1.82e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359106   4 VSTYLNFARETEAAFLFYREVFGGDFSGPIHRFKESPgcpgqPPLSEEDGELVMHVALPILGGHVLMGTDAPasmGFTLV 83
Cdd:cd06588    1 ITPYLWFNGNAEEALEFYAEVFPGGEILSLTRYGEGP-----PDFPEGDEGKVMHAEFTLGGQTLMASDDGP---GFPFT 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 498359106  84 QGNNSYLNLEPDSRGETDRLFAALAEGGQVEMPLAEMFWGDYFGSLVDKFGTHWMFN 140
Cdd:cd06588   73 FGNAISLSVDCDSQEEADRLFEKLSEGGEVLMPLQETFWGARYGWVKDKFGVSWQIN 129
 
Name Accession Description Interval E-value
PhnB_like cd06588
Escherichia coli PhnB and similar proteins; The Escherichia coli phnB gene is found next to an ...
 4-140 1.82e-35

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: 119.30  E-value: 1.82e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359106   4 VSTYLNFARETEAAFLFYREVFGGDFSGPIHRFKESPgcpgqPPLSEEDGELVMHVALPILGGHVLMGTDAPasmGFTLV 83
Cdd:cd06588    1 ITPYLWFNGNAEEALEFYAEVFPGGEILSLTRYGEGP-----PDFPEGDEGKVMHAEFTLGGQTLMASDDGP---GFPFT 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 498359106  84 QGNNSYLNLEPDSRGETDRLFAALAEGGQVEMPLAEMFWGDYFGSLVDKFGTHWMFN 140
Cdd:cd06588   73 FGNAISLSVDCDSQEEADRLFEKLSEGGEVLMPLQETFWGARYGWVKDKFGVSWQIN 129
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
3-141 2.41e-32

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 110.72  E-value: 2.41e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359106   3 RVSTYLNFAReTEAAFLFYREVFGGDFSGpihrfkespgcpgqppLSEEDGELVMHVALPIlGGHVLMGTDAPASMGFTl 82
Cdd:COG2764    1 SVTPYLVVDD-AEEALEFYEDVFGFEVVF----------------RMTDPDGKIMHAELRI-GGSVLMLSDAPPDSPAA- 61

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359106  83 vQGNNSYLNLEPDsrgETDRLFAAL-AEGGQVEMPLAEMFWGDYFGSLVDKFGTHWMFNC 141
Cdd:COG2764   62 -EGNGVSLSLYVD---DVDALFARLvAAGATVVMPLQDTFWGDRFGMVRDPFGVLWMINT 117
PRK10148 PRK10148
VOC family metalloprotein YjdN;
4-140 1.98e-17

VOC family metalloprotein YjdN;


Pssm-ID: 236656  Cd Length: 147  Bit Score: 73.78  E-value: 1.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359106   4 VSTYLNFARETEAAFLFYREVFGGDFSGPIhRFKESP--------GCPG--QPPLSEedgelVMHVALPILGGHVLMgTD 73
Cdd:PRK10148   3 LSPYLSFAGNCADAIAYYQQTLGAELLYKI-SFGEMPksaqdseeGCPSgmQFPDTA-----IAHANVRIAGSDIMM-SD 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498359106  74 APAS-----MGFTLVqgnnsylnLEPDSRGETDRLFAALAEGGQVEMPLAEMFWGDYFGSLVDKFGTHWMFN 140
Cdd:PRK10148  76 AIPSgkahySGFTLV--------LDTQDVEEGKRWFDNLAANGKIEMAWQETFWAHGFGKVTDKFGVPWMIN 139
3-dmu-9_3-mt pfam06983
3-demethylubiquinone-9 3-methyltransferase; This family represents a conserved region ...
 2-137 5.14e-05

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: 39.98  E-value: 5.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359106    2 ARVSTYLNFARETEAAFLFYREVFGGDFSGPIHRFKEspGCPGQPplseedgELVMHVALpILGGHVLMGTDAPASMGFT 81
Cdd:pfam06983   1 QKITPCLWFDGQAEEAAEFYVSLFPNSEIGSVNRYPE--DGPGKP-------GSVLTVEF-TLNGQPFIALNGGPNFKFN 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 498359106   82 lvqgNNSYLNLEPDSRGETDRLFAALAEGGQVEMPlaemfwgdyFGSLVDKFGTHW 137
Cdd:pfam06983  71 ----EAVSFQVTCKDQEEVDRYWNALSENGGPESQ---------CGWLKDKFGVSW 113
 
Name Accession Description Interval E-value
PhnB_like cd06588
Escherichia coli PhnB and similar proteins; The Escherichia coli phnB gene is found next to an ...
 4-140 1.82e-35

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: 119.30  E-value: 1.82e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359106   4 VSTYLNFARETEAAFLFYREVFGGDFSGPIHRFKESPgcpgqPPLSEEDGELVMHVALPILGGHVLMGTDAPasmGFTLV 83
Cdd:cd06588    1 ITPYLWFNGNAEEALEFYAEVFPGGEILSLTRYGEGP-----PDFPEGDEGKVMHAEFTLGGQTLMASDDGP---GFPFT 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 498359106  84 QGNNSYLNLEPDSRGETDRLFAALAEGGQVEMPLAEMFWGDYFGSLVDKFGTHWMFN 140
Cdd:cd06588   73 FGNAISLSVDCDSQEEADRLFEKLSEGGEVLMPLQETFWGARYGWVKDKFGVSWQIN 129
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
3-141 2.41e-32

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 110.72  E-value: 2.41e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359106   3 RVSTYLNFAReTEAAFLFYREVFGGDFSGpihrfkespgcpgqppLSEEDGELVMHVALPIlGGHVLMGTDAPASMGFTl 82
Cdd:COG2764    1 SVTPYLVVDD-AEEALEFYEDVFGFEVVF----------------RMTDPDGKIMHAELRI-GGSVLMLSDAPPDSPAA- 61

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359106  83 vQGNNSYLNLEPDsrgETDRLFAAL-AEGGQVEMPLAEMFWGDYFGSLVDKFGTHWMFNC 141
Cdd:COG2764   62 -EGNGVSLSLYVD---DVDALFARLvAAGATVVMPLQDTFWGDRFGMVRDPFGVLWMINT 117
PRK10148 PRK10148
VOC family metalloprotein YjdN;
4-140 1.98e-17

VOC family metalloprotein YjdN;


Pssm-ID: 236656  Cd Length: 147  Bit Score: 73.78  E-value: 1.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359106   4 VSTYLNFARETEAAFLFYREVFGGDFSGPIhRFKESP--------GCPG--QPPLSEedgelVMHVALPILGGHVLMgTD 73
Cdd:PRK10148   3 LSPYLSFAGNCADAIAYYQQTLGAELLYKI-SFGEMPksaqdseeGCPSgmQFPDTA-----IAHANVRIAGSDIMM-SD 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498359106  74 APAS-----MGFTLVqgnnsylnLEPDSRGETDRLFAALAEGGQVEMPLAEMFWGDYFGSLVDKFGTHWMFN 140
Cdd:PRK10148  76 AIPSgkahySGFTLV--------LDTQDVEEGKRWFDNLAANGKIEMAWQETFWAHGFGKVTDKFGVPWMIN 139
VOC_like cd07246
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 4-139 1.05e-12

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: 60.77  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359106   4 VSTYLnFARETEAAFLFYREVFGGDFSGpihRFkespgcpgqpplsEEDGELVMHVALPIlGGHVLMGTDAPASMGFTLV 83
Cdd:cd07246    3 VSPYL-VVEDAAAAIAFYKKAFGAEELG---RT-------------TQEDGRVGHAELRI-GGTVVMVADENPERGALSP 64

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359106  84 Q---GNNSYLNLEPDSrgeTDRLFA-ALAEGGQVEMPLAEMFWGDYFGSLVDKFGTHWMF 139
Cdd:cd07246   65 TklgGTPVIFHLYVED---VDATFArAVAAGAVVVEPVEDQFWGDRVGKVKDPFGHVWWL 121
3-dmu-9_3-mt pfam06983
3-demethylubiquinone-9 3-methyltransferase; This family represents a conserved region ...
 2-137 5.14e-05

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: 39.98  E-value: 5.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498359106    2 ARVSTYLNFARETEAAFLFYREVFGGDFSGPIHRFKEspGCPGQPplseedgELVMHVALpILGGHVLMGTDAPASMGFT 81
Cdd:pfam06983   1 QKITPCLWFDGQAEEAAEFYVSLFPNSEIGSVNRYPE--DGPGKP-------GSVLTVEF-TLNGQPFIALNGGPNFKFN 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 498359106   82 lvqgNNSYLNLEPDSRGETDRLFAALAEGGQVEMPlaemfwgdyFGSLVDKFGTHW 137
Cdd:pfam06983  71 ----EAVSFQVTCKDQEEVDRYWNALSENGGPESQ---------CGWLKDKFGVSW 113
 
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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