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Conserved domains on  [gi|1486887798|ref|WP_120351671|]
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MULTISPECIES: VOC family protein [unclassified Sulfitobacter]

Protein Classification

VOC family protein( domain architecture ID 10007568)

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
COG3565 COG3565
Predicted dioxygenase of extradiol dioxygenase family [General function prediction only];
1-136 1.15e-90

Predicted dioxygenase of extradiol dioxygenase family [General function prediction only];


:

Pssm-ID: 442786  Cd Length: 139  Bit Score: 258.95  E-value: 1.15e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798   1 MLTPFHLAYNVRDLDETRAFYGDVLGCTEGRSTETWVDYSFFGHQISMHLGEPFA-TEATGKVGEHMVPMPHLGVVLQMD 79
Cdd:COG3565     2 MLPPFHLAFPVTDLDAARRFYGDVLGCEEGRSSDTWVDFDFFGHQLVAHLAPPFAfTAATNPVDGHDVPVPHFGVVLDWD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1486887798  80 DWKALAERLKGAKVDFVIEPSLRFEGEPGEQATMFFRDPSGNPIEVKGFADMERVFA 136
Cdd:COG3565    82 DWHALAERLKAAGVEFVIEPYIRFEGQPGEQATMFFLDPSGNALEFKAFKDESQVFA 138
 
Name Accession Description Interval E-value
COG3565 COG3565
Predicted dioxygenase of extradiol dioxygenase family [General function prediction only];
1-136 1.15e-90

Predicted dioxygenase of extradiol dioxygenase family [General function prediction only];


Pssm-ID: 442786  Cd Length: 139  Bit Score: 258.95  E-value: 1.15e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798   1 MLTPFHLAYNVRDLDETRAFYGDVLGCTEGRSTETWVDYSFFGHQISMHLGEPFA-TEATGKVGEHMVPMPHLGVVLQMD 79
Cdd:COG3565     2 MLPPFHLAFPVTDLDAARRFYGDVLGCEEGRSSDTWVDFDFFGHQLVAHLAPPFAfTAATNPVDGHDVPVPHFGVVLDWD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1486887798  80 DWKALAERLKGAKVDFVIEPSLRFEGEPGEQATMFFRDPSGNPIEVKGFADMERVFA 136
Cdd:COG3565    82 DWHALAERLKAAGVEFVIEPYIRFEGQPGEQATMFFLDPSGNALEFKAFKDESQVFA 138
VOC_like cd08357
uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and ...
 5-128 4.57e-69

uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and type I ring-cleaving dioxygenases; 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: 319945 [Multi-domain]  Cd Length: 124  Bit Score: 203.77  E-value: 4.57e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798   5 FHLAYNVRDLDETRAFYGDVLGCTEGRSTETWVDYSFFGHQISMHLGEPFATEATGKVGEHMVPMPHLGVVLQMDDWKAL 84
Cdd:cd08357     1 FHLAIPVRDLEAARDFYGDVLGCPEGRSSETWIDFNFFGHQVVAHLVPNYASTSTNAVDGHSVPVPHFGLALTVDDFDAL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1486887798  85 AERLKGAKVDFVIEPSLRFEGEPGEQATMFFRDPSGNPIEVKGF 128
Cdd:cd08357    81 AERLKAAGVKFYIEPYVRFEGEPGEQWTMFLLDPSGNALEFKAM 124
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
6-125 1.33e-11

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 57.46  E-value: 1.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798   6 HLAYNVRDLDETRAFYGDVLGCTEGRSTETWVDYSFFGHQisMHLGEP---FATEATGKVGEHMVPMPHLGV-VLQMDDW 81
Cdd:pfam00903   4 HVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAF--FLAGGRvleLLLNETPPPAAAGFGGHHIAFiAFSVDDV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1486887798  82 KALAERLKGAKVDFVIEPSLRFEGepgeQATMFFRDPSGNPIEV 125
Cdd:pfam00903  82 DAAYDRLKAAGVEIVREPGRHGWG----GRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
COG3565 COG3565
Predicted dioxygenase of extradiol dioxygenase family [General function prediction only];
1-136 1.15e-90

Predicted dioxygenase of extradiol dioxygenase family [General function prediction only];


Pssm-ID: 442786  Cd Length: 139  Bit Score: 258.95  E-value: 1.15e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798   1 MLTPFHLAYNVRDLDETRAFYGDVLGCTEGRSTETWVDYSFFGHQISMHLGEPFA-TEATGKVGEHMVPMPHLGVVLQMD 79
Cdd:COG3565     2 MLPPFHLAFPVTDLDAARRFYGDVLGCEEGRSSDTWVDFDFFGHQLVAHLAPPFAfTAATNPVDGHDVPVPHFGVVLDWD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1486887798  80 DWKALAERLKGAKVDFVIEPSLRFEGEPGEQATMFFRDPSGNPIEVKGFADMERVFA 136
Cdd:COG3565    82 DWHALAERLKAAGVEFVIEPYIRFEGQPGEQATMFFLDPSGNALEFKAFKDESQVFA 138
VOC_like cd08357
uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and ...
 5-128 4.57e-69

uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and type I ring-cleaving dioxygenases; 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: 319945 [Multi-domain]  Cd Length: 124  Bit Score: 203.77  E-value: 4.57e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798   5 FHLAYNVRDLDETRAFYGDVLGCTEGRSTETWVDYSFFGHQISMHLGEPFATEATGKVGEHMVPMPHLGVVLQMDDWKAL 84
Cdd:cd08357     1 FHLAIPVRDLEAARDFYGDVLGCPEGRSSETWIDFNFFGHQVVAHLVPNYASTSTNAVDGHSVPVPHFGLALTVDDFDAL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1486887798  85 AERLKGAKVDFVIEPSLRFEGEPGEQATMFFRDPSGNPIEVKGF 128
Cdd:cd08357    81 AERLKAAGVKFYIEPYVRFEGEPGEQWTMFLLDPSGNALEFKAM 124
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-125 8.49e-16

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: 68.48  E-value: 8.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798   6 HLAYNVRDLDETRAFYGDVLGCTEGRSTE------TWVDYSfFGHQISMHLGE-PFATEATGKVGEHmvpmpHLGvvLQM 78
Cdd:COG0346     5 HVTLRVSDLEASLAFYTDVLGLELVKRTDfgdggfGHAFLR-LGDGTELELFEaPGAAPAPGGGGLH-----HLA--FRV 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1486887798  79 DDWKALAERLKGAKVDFVIEPSLRFEGEPgeqaTMFFRDPSGNPIEV 125
Cdd:COG0346    77 DDLDAAYARLRAAGVEIEGEPRDRAYGYR----SAYFRDPDGNLIEL 119
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
6-134 8.68e-13

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 61.13  E-value: 8.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798   6 HLAYNVRDLDETRAFYGDVLGCTEGRSTETWVDYSFFGHQISMHLgepfaTEATGKVGEHMVP-MPHLGV-VLQMDDWKA 83
Cdd:COG2514     6 HVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEHLLVL-----EEAPGAPPRPGAAgLDHVAFrVPSRADLDA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1486887798  84 LAERLKGAKVDFViEPSLRFEGEpgeqaTMFFRDPSGNPIEVkgFADMERV 134
Cdd:COG2514    81 ALARLAAAGVPVE-GAVDHGVGE-----SLYFRDPDGNLIEL--YTDRPRF 123
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 6-125 1.14e-12

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: 60.23  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798   6 HLAYNVRDLDETRAFYGDVLGCTEGRSTE--TWVDYSFF-GHQISMHLGEPFATEATGKVGehmvpmpHLGVVLqmDDWK 82
Cdd:cd06587     1 HVALRVPDLDASVAFYEEVLGFEVVSRNEggGFAFLRLGpGLRLALLEGPEPERPGGGGLF-------HLAFEV--DDVD 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1486887798  83 ALAERLKGAKVDFVIEPSLRFEGEPGEQAtmFFRDPSGNPIEV 125
Cdd:cd06587    72 EVDERLREAGAEGELVAPPVDDPWGGRSF--YFRDPDGNLIEF 112
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 6-127 3.45e-12

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: 59.16  E-value: 3.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798   6 HLAYNVRDLDETRAFYGDVLGCTEGRSTETWVDYSfFGHQ-ISMH-LGEPFATEAtgkvgEHMVP-MPHLGVVLQmDDWK 82
Cdd:cd07253     6 HLVLTVKDIERTIDFYTKVLGMTVVTFKEGRKALR-FGNQkINLHqKGKEFEPKA-----SAPTPgSADLCFITE-TPID 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1486887798  83 ALAERLKGAKVDfVIEPSLRFEGEPGEQATMFFRDPSGNPIEVKG 127
Cdd:cd07253    79 EVLEHLEACGVT-IEEGPVKRTGALGPILSIYFRDPDGNLIELSN 122
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
6-125 1.33e-11

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 57.46  E-value: 1.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798   6 HLAYNVRDLDETRAFYGDVLGCTEGRSTETWVDYSFFGHQisMHLGEP---FATEATGKVGEHMVPMPHLGV-VLQMDDW 81
Cdd:pfam00903   4 HVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAF--FLAGGRvleLLLNETPPPAAAGFGGHHIAFiAFSVDDV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1486887798  82 KALAERLKGAKVDFVIEPSLRFEGepgeQATMFFRDPSGNPIEV 125
Cdd:pfam00903  82 DAAYDRLKAAGVEIVREPGRHGWG----GRYSYFRDPDGNLIEL 121
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-125 7.09e-11

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 55.41  E-value: 7.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798   1 MLTPFHLAYNVRDLDETRAFYGDVLGCTEGRSTETWVDYSFFghqiSMHLGEPFATEATGKVGEHMVPMPHLGVvlqmDD 80
Cdd:COG3324     2 PGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPGGDYAEF----DTDGGQVGGLMPGAEEPGGPGWLLYFAV----DD 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1486887798  81 WKALAERLKGAKVDFVIEPslrFEGEPGEqATMFFRDPSGNPIEV 125
Cdd:COG3324    74 LDAAVARVEAAGGTVLRPP---TDIPPWG-RFAVFRDPEGNRFGL 114
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 6-125 5.49e-09

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: 50.39  E-value: 5.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798   6 HLAYNVRDLDETRAFYGDVLGCTEGRSTE------TWVdysFFGHQISMHLGE-PFATEATGKVGEHMVPMPHLGVvlqm 78
Cdd:cd07245     3 HVALACPDLERARRFYTDVLGLEEVPRPPflkfggAWL---YLGGGQQIHLVVeQNPSELPRPEHPGRDRHPSFSV---- 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1486887798  79 DDWKALAERLKGAKVDFVIEPSLrfegePGEQATMFFRDPSGNPIEV 125
Cdd:cd07245    76 PDLDALKQRLKEAGIPYTESTSP-----GGGVTQLFFRDPDGNRLEF 117
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
5-99 7.50e-07

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 44.58  E-value: 7.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798   5 FHLAYNVRDLDETRAFYGDVLGCT---EGRSTETWVDYSFFGH---QISMHLGEPfaTEATGKVGEHMVPMPHLGvvLQM 78
Cdd:pfam13669   1 HHVGIAVPDLDRALALWGALLGLGpegDYRSEPQNVDLAFALLgdgPVEVELIQP--LDGDSPLARHGPGLHHLA--YWV 76

                          90       100
                  ....*....|....*....|.
gi 1486887798  79 DDWKALAERLKGAKVDFVIEP 99
Cdd:pfam13669  77 DDLDAAVARLLDQGYRVAPKG 97
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 6-125 2.64e-05

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: 40.78  E-value: 2.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798   6 HLAYNVRDLDETRAFYGDVLGCTEGRSTETwVDYSFFGHqismhlGEP---FATEATGKVGEHMVPM-PHLGVVLQMDDW 81
Cdd:cd07264     3 YIVLYVDDFAASLRFYRDVLGLPPRFLHEE-GEYAEFDT------GETklaLFSRKEMARSGGPDRRgSAFELGFEVDDV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1486887798  82 KALAERLKGAKVDFVIEPSlrfEGEPGeQATMFFRDPSGNPIEV 125
Cdd:cd07264    76 EATVEELVERGAEFVREPA---NKPWG-QTVAYVRDPDGNLIEI 115
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 11-125 4.78e-05

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: 40.04  E-value: 4.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798  11 VRDLDETRAFYGDVLGCT----EGRStetwvdySFFGHQISM-HLGEPFATEATGKVGEhmVPmPHLGV--------VL- 76
Cdd:cd08354     8 ADDLDAAEAFYEDVLGLKpmlrSGRH-------AFFRLGPQVlLVFDPGATSKDVRTGE--VP-GHGASghghfafaVPt 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1486887798  77 -QMDDWKAlaeRLKGAKVDfvIEpslRFEGEPGEQATMFFRDPSGNPIEV 125
Cdd:cd08354    78 eELAAWEA---RLEAKGVP--IE---SYTQWPEGGKSLYFRDPAGNLVEL 119
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 6-125 2.05e-04

vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; This subfamily of vicinal oxygen chelate (VOC) family protein includes Streptomyces hygroscopicus ValD protein and similar proteins. ValD protein functions in validamycin biosynthetic pathway. 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: 319968  Cd Length: 150  Bit Score: 38.85  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798   6 HLAYNVRDLDETRAFYGDVLGC------TEGRSTETWVdysffGHQISMHLGEPFAT-----------------EATGKV 62
Cdd:cd16361     4 HVGITVPDLDAAVEFYTDVLGAevvyrsTPLAEGDRGG-----GEMRAAGFVPGFARariamlrlgpgpgielfEYKGPE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1486887798  63 GEHMVPMPH-LGVV---LQMDDWKALAERLKGAKVDFVIEPSLRFEGEPGEQATM-FFRDPSGNPIEV 125
Cdd:cd16361    79 QRAPVPRNSdVGIFhfaLQVDDVEAAAERLAAAGGKVLMGPREIPDGGPGKGNRMvYLRDPWGTLIEL 146
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 6-125 2.22e-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: 319923 [Multi-domain]  Cd Length: 121  Bit Score: 38.36  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798   6 HLAYNVRDLDETRAFYGDV---LGCTEGRSTETWVdysFFGHQ--ISMHLGEPFATEAtGKVGEHMvpmpHLGVVL---- 76
Cdd:cd07262     3 HVTIGVNDLERSRAFYDAAlapLGYKRGFEDGGRV---GYGLEggPDFWVTEPFDGEP-ATAGNGT----HVAFAApsra 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1486887798  77 QMDDWKALAERLKGakvdfviepslRFEGEPGEQATM-------FFRDPSGNPIEV 125
Cdd:cd07262    75 AVDAFHAAALAAGG-----------TDNGAPGLRPHYhpgyyaaYVRDPDGNKIEA 119
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 11-123 6.39e-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: 36.86  E-value: 6.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798  11 VRDLDETRAFYGDVLGCTEGRSTETWVDYSFFGHQismhlGEPFAteATGKVGEHMVPMP-HLGVVLQMDDWKALAERLK 89
Cdd:cd07247     8 TTDLERAKAFYGAVFGWTFEDEGDGGGDYALFTAG-----GGAVG--GLMRAPEEVAGAPpGWLIYFAVDDLDAALARVE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1486887798  90 --GAKVdfVIEPSlrfegEPGEQATMF-FRDPSGNPI 123
Cdd:cd07247    81 aaGGKV--VVPPT-----DIPGGGRFAvFADPEGNRF 110
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 11-121 1.27e-03

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: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 36.12  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798  11 VRDLDETRAFYGDVLGcTEGRSTETWVDYSFF------GHQISMHLGEPFATEATGKVGEHMVPMPhlGVVLQMDDWKAL 84
Cdd:cd07263     6 VDDQDKALDFYVEKLG-FEVVEDVPMGGMRWVtvappgSPGTSLLLEPKAHPAQMPQSPEAAGGTP--GILLATDDIDAT 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1486887798  85 AERLKGAKVDFVIEPSlrfegEPGEQATMFFRDPSGN 121
Cdd:cd07263    83 YERLTAAGVTFVQEPT-----QMGGGRVANFRDPDGN 114
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
10-125 2.27e-03

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 35.60  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798  10 NVRDLDETRAFYGDVLGCTEG---RSTETWVDYSFFGH-QISMHLGEPFAteatgkvGEHMVPMPHLGVVLQMDDWKALA 85
Cdd:COG2764     7 VVDDAEEALEFYEDVFGFEVVfrmTDPDGKIMHAELRIgGSVLMLSDAPP-------DSPAAEGNGVSLSLYVDDVDALF 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1486887798  86 ERLKGAKVDFVIEPSLRFEGepgeQATMFFRDPSGNPIEV 125
Cdd:COG2764    80 ARLVAAGATVVMPLQDTFWG----DRFGMVRDPFGVLWMI 115
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-125 5.74e-03

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: 319917 [Multi-domain]  Cd Length: 120  Bit Score: 34.36  E-value: 5.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486887798   5 FHLAYNVRDLDETRAFYGDVLGcTEGRSTETwvDYSFFghqismHLGEP---FATEATGKVGEHMVpmPHLGVvlQMDDW 81
Cdd:cd07254     3 FHLSLNVTDLERSIRFYSDLFG-AEPAKRKA--DYAKF------MLEDPplnLALLVNDRKEPYGL--NHLGI--QVDSK 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1486887798  82 KALA---ERLKGAKVDFVIEPSLRFEGEPGEQatMFFRDPSGNPIEV 125
Cdd:cd07254    70 EEVAalkARAEAAGLPVRKEPRTTCCYAVQDK--FWLTDPDGNAWEF 114
 
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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