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Conserved domains on  [gi|1525783404|gb|AZG17356|]
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dioxygenase (plasmid) [Cupriavidus pauculus]

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];
1-137 9.33e-83

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


:

Pssm-ID: 442786  Cd Length: 139  Bit Score: 238.92  E-value: 9.33e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525783404   1 MQSVFHLAFNITDLDEARRFYGGVLGCKEGRSTDTWVDFDFFGHQISLHLGKPF-ETARTGRVGNALVPMPHFGIILLLP 79
Cdd:COG3565     2 MLPPFHLAFPVTDLDAARRFYGDVLGCEEGRSSDTWVDFDFFGHQLVAHLAPPFaFTAATNPVDGHDVPVPHFGVVLDWD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1525783404  80 AWRTLADRLTAAGTDFVLNPQVRFEGEPGEQWTMFFVDPFGNPIEVKGFKTWEAVYAH 137
Cdd:COG3565    82 DWHALAERLKAAGVEFVIEPYIRFEGQPGEQATMFFLDPSGNALEFKAFKDESQVFAK 139
 
Name Accession Description Interval E-value
COG3565 COG3565
Predicted dioxygenase of extradiol dioxygenase family [General function prediction only];
1-137 9.33e-83

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


Pssm-ID: 442786  Cd Length: 139  Bit Score: 238.92  E-value: 9.33e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525783404   1 MQSVFHLAFNITDLDEARRFYGGVLGCKEGRSTDTWVDFDFFGHQISLHLGKPF-ETARTGRVGNALVPMPHFGIILLLP 79
Cdd:COG3565     2 MLPPFHLAFPVTDLDAARRFYGDVLGCEEGRSSDTWVDFDFFGHQLVAHLAPPFaFTAATNPVDGHDVPVPHFGVVLDWD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1525783404  80 AWRTLADRLTAAGTDFVLNPQVRFEGEPGEQWTMFFVDPFGNPIEVKGFKTWEAVYAH 137
Cdd:COG3565    82 DWHALAERLKAAGVEFVIEPYIRFEGQPGEQATMFFLDPSGNALEFKAFKDESQVFAK 139
VOC_like cd08357
uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and ...
 5-128 6.42e-65

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: 193.37  E-value: 6.42e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525783404   5 FHLAFNITDLDEARRFYGGVLGCKEGRSTDTWVDFDFFGHQISLHLGKPFETARTGRVGNALVPMPHFGIILLLPAWRTL 84
Cdd:cd08357     1 FHLAIPVRDLEAARDFYGDVLGCPEGRSSETWIDFNFFGHQVVAHLVPNYASTSTNAVDGHSVPVPHFGLALTVDDFDAL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1525783404  85 ADRLTAAGTDFVLNPQVRFEGEPGEQWTMFFVDPFGNPIEVKGF 128
Cdd:cd08357    81 AERLKAAGVKFYIEPYVRFEGEPGEQWTMFLLDPSGNALEFKAM 124
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
6-125 1.60e-06

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 43.98  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525783404   6 HLAFNITDLDEARRFYGGVLGCKEGRSTDT-----WVDFDFFGHQISLHLGkPFETARTGRVGnalVPMPHFGIILLLPA 80
Cdd:pfam00903   4 HVALRVGDLEKSLDFYTDVLGFKLVEETDAgeeggLRSAFFLAGGRVLELL-LNETPPPAAAG---FGGHHIAFIAFSVD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1525783404  81 -WRTLADRLTAAGtdfvlnpqVRFEGEPGEQWT----MFFVDPFGNPIEV 125
Cdd:pfam00903  80 dVDAAYDRLKAAG--------VEIVREPGRHGWggrySYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
COG3565 COG3565
Predicted dioxygenase of extradiol dioxygenase family [General function prediction only];
1-137 9.33e-83

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


Pssm-ID: 442786  Cd Length: 139  Bit Score: 238.92  E-value: 9.33e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525783404   1 MQSVFHLAFNITDLDEARRFYGGVLGCKEGRSTDTWVDFDFFGHQISLHLGKPF-ETARTGRVGNALVPMPHFGIILLLP 79
Cdd:COG3565     2 MLPPFHLAFPVTDLDAARRFYGDVLGCEEGRSSDTWVDFDFFGHQLVAHLAPPFaFTAATNPVDGHDVPVPHFGVVLDWD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1525783404  80 AWRTLADRLTAAGTDFVLNPQVRFEGEPGEQWTMFFVDPFGNPIEVKGFKTWEAVYAH 137
Cdd:COG3565    82 DWHALAERLKAAGVEFVIEPYIRFEGQPGEQATMFFLDPSGNALEFKAFKDESQVFAK 139
VOC_like cd08357
uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and ...
 5-128 6.42e-65

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: 193.37  E-value: 6.42e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525783404   5 FHLAFNITDLDEARRFYGGVLGCKEGRSTDTWVDFDFFGHQISLHLGKPFETARTGRVGNALVPMPHFGIILLLPAWRTL 84
Cdd:cd08357     1 FHLAIPVRDLEAARDFYGDVLGCPEGRSSETWIDFNFFGHQVVAHLVPNYASTSTNAVDGHSVPVPHFGLALTVDDFDAL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1525783404  85 ADRLTAAGTDFVLNPQVRFEGEPGEQWTMFFVDPFGNPIEVKGF 128
Cdd:cd08357    81 AERLKAAGVKFYIEPYVRFEGEPGEQWTMFLLDPSGNALEFKAM 124
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-125 8.64e-12

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: 58.08  E-value: 8.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525783404   6 HLAFNITDLDEARRFYGGVLGCKEGRSTD------TWVDFDfFGHQISLHLGKPFETARTGRVGNalvpMPHFGIIllLP 79
Cdd:COG0346     5 HVTLRVSDLEASLAFYTDVLGLELVKRTDfgdggfGHAFLR-LGDGTELELFEAPGAAPAPGGGG----LHHLAFR--VD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1525783404  80 AWRTLADRLTAAGTDFVLNPQVRFEGepgeQWTMFFVDPFGNPIEV 125
Cdd:COG0346    78 DLDAAYARLRAAGVEIEGEPRDRAYG----YRSAYFRDPDGNLIEL 119
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
6-125 1.02e-11

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 58.43  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525783404   6 HLAFNITDLDEARRFYGGVLGCKEGRSTDTWVDFDFFGHQISLHL-GKPFETARTGRVGnalvpMPHFGIilLLPAWRTL 84
Cdd:COG2514     6 HVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEHLLVLeEAPGAPPRPGAAG-----LDHVAF--RVPSRADL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1525783404  85 AD---RLTAAGtdfvlnpqVRFEG--EPGEQWTMFFVDPFGNPIEV 125
Cdd:COG2514    79 DAalaRLAAAG--------VPVEGavDHGVGESLYFRDPDGNLIEL 116
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 6-127 1.64e-09

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: 52.23  E-value: 1.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525783404   6 HLAFNITDLDEARRFYGGVLGCKEGRSTDTWVDFDfFGHQ-ISLH-LGKPFETArtgrvgnALVPMP---HFGIILLLPa 80
Cdd:cd07253     6 HLVLTVKDIERTIDFYTKVLGMTVVTFKEGRKALR-FGNQkINLHqKGKEFEPK-------ASAPTPgsaDLCFITETP- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1525783404  81 WRTLADRLTAAGTDFVLNPqVRFEGEPGEQWTMFFVDPFGNPIEVKG 127
Cdd:cd07253    77 IDEVLEHLEACGVTIEEGP-VKRTGALGPILSIYFRDPDGNLIELSN 122
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 6-125 9.83e-08

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: 47.13  E-value: 9.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525783404   6 HLAFNITDLDEARRFYGGVLGCKE--GRSTDTWVDFDFF-GHQISLHLGKPFETARTGRVGnalvpmpHFGIilLLPAWR 82
Cdd:cd06587     1 HVALRVPDLDASVAFYEEVLGFEVvsRNEGGGFAFLRLGpGLRLALLEGPEPERPGGGGLF-------HLAF--EVDDVD 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1525783404  83 TLADRLTAAGTDFVlnPQVRFEGEPGEQWTMFFVDPFGNPIEV 125
Cdd:cd06587    72 EVDERLREAGAEGE--LVAPPVDDPWGGRSFYFRDPDGNLIEF 112
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
6-125 1.60e-06

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 43.98  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525783404   6 HLAFNITDLDEARRFYGGVLGCKEGRSTDT-----WVDFDFFGHQISLHLGkPFETARTGRVGnalVPMPHFGIILLLPA 80
Cdd:pfam00903   4 HVALRVGDLEKSLDFYTDVLGFKLVEETDAgeeggLRSAFFLAGGRVLELL-LNETPPPAAAG---FGGHHIAFIAFSVD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1525783404  81 -WRTLADRLTAAGtdfvlnpqVRFEGEPGEQWT----MFFVDPFGNPIEV 125
Cdd:pfam00903  80 dVDAAYDRLKAAG--------VEIVREPGRHGWggrySYFRDPDGNLIEL 121
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 6-125 2.47e-06

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: 43.46  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525783404   6 HLAFNITDLDEARRFYGGVLGCKEGRSTDTwvdFDFFGH------QISLHLGK---PFETARTGRVGNAlvpmPHFGiiL 76
Cdd:cd07245     3 HVALACPDLERARRFYTDVLGLEEVPRPPF---LKFGGAwlylggGQQIHLVVeqnPSELPRPEHPGRD----RHPS--F 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1525783404  77 LLPAWRTLADRLTAAGTDFVlnPQVRFEGEPgeqWTMFFVDPFGNPIEV 125
Cdd:cd07245    74 SVPDLDALKQRLKEAGIPYT--ESTSPGGGV---TQLFFRDPDGNRLEF 117
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-125 4.78e-06

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 42.70  E-value: 4.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525783404   1 MQSVFHLAFNITDLDEARRFYGGVLGCKEGRSTDTWVDFDFF--GHQISLHLGKPFETARTGRvgnalvPMPHFGIilll 78
Cdd:COG3324     2 PGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPGGDYAEFdtDGGQVGGLMPGAEEPGGPG------WLLYFAV---- 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1525783404  79 PAWRTLADRLTAAGTDFVLNPQVrfEGEPGeqWTMFFVDPFGNPIEV 125
Cdd:COG3324    72 DDLDAAVARVEAAGGTVLRPPTD--IPPWG--RFAVFRDPEGNRFGL 114
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 3-125 8.39e-06

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: 42.70  E-value: 8.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525783404   3 SVFHLAFNITDLDEARRFYGGVLGCK------EGRSTDTWVdfdffGHQISLHLGKPFETARTG--RVGNAL-------- 66
Cdd:cd16361     1 GVNHVGITVPDLDAAVEFYTDVLGAEvvyrstPLAEGDRGG-----GEMRAAGFVPGFARARIAmlRLGPGPgielfeyk 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1525783404  67 -------VPMPH----FGIILLLPAWRTLADRLTAAGTDFVLNPQVRFEGEPGEQWTMFFV-DPFGNPIEV 125
Cdd:cd16361    76 gpeqrapVPRNSdvgiFHFALQVDDVEAAAERLAAAGGKVLMGPREIPDGGPGKGNRMVYLrDPWGTLIEL 146
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 6-125 1.04e-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: 39.13  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525783404   6 HLAFNITDLDEARRFYG---GVLGCKEGRSTDTWVdfdFFGHQ--ISLHLGKPFEtARTGRVGNALvpmpHFGiiLLLP- 79
Cdd:cd07262     3 HVTIGVNDLERSRAFYDaalAPLGYKRGFEDGGRV---GYGLEggPDFWVTEPFD-GEPATAGNGT----HVA--FAAPs 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1525783404  80 -----AWRTLAdrLTAAGTDfvlnpqvrfEGEPGEQ-------WTMFFVDPFGNPIEV 125
Cdd:cd07262    73 raavdAFHAAA--LAAGGTD---------NGAPGLRphyhpgyYAAYVRDPDGNKIEA 119
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 13-125 1.77e-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: 319942  Cd Length: 122  Bit Score: 38.50  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525783404  13 DLDEARRFYGGVLGCKEGRSTDTWVDFDfFGHQIsLHLGKPFETARTGRVG----NALVPMPHFGIILL---LPAWRTla 85
Cdd:cd08354    10 DLDAAEAFYEDVLGLKPMLRSGRHAFFR-LGPQV-LLVFDPGATSKDVRTGevpgHGASGHGHFAFAVPteeLAAWEA-- 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1525783404  86 dRLTAAGTdfvlnPQVRFEGEPGEQWTMFFVDPFGNPIEV 125
Cdd:cd08354    86 -RLEAKGV-----PIESYTQWPEGGKSLYFRDPAGNLVEL 119
HPCD_N_class_II cd07266
N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 6-124 8.23e-04

N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily contains the N-terminal, non-catalytic, domain of HPCD. HPCD catalyses the second step in the degradation of 4-hydroxyphenylacetate to succinate and pyruvate. The aromatic ring of 4-hydroxyphenylacetate is opened by this dioxygenase to yield the 3,4-diol product, 2-hydroxy-5-carboxymethylmuconate semialdehyde. HPCD is a homotetramer and each monomer contains two structurally homologous barrel-shaped domains at the N- and C-terminus. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism. Most extradiol dioxygenases contain Fe(II) in their active site, but HPCD can be activated by either Mn(II) or Fe(II). These enzymes belong to the type I class II family of extradiol dioxygenases. The class III 3,4-dihydroxyphenylacetate 2,3-dioxygenases belong to a different superfamily.


Pssm-ID: 319927  Cd Length: 118  Bit Score: 36.62  E-value: 8.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525783404   6 HLAFNITDLDEARRFYGGVLGCKEGRSTDTWV---DFDFFGHQiSLHLGKpfetARTGRVGnalvpmpHFGIILllpawR 82
Cdd:cd07266     7 HAELVVTDLAASREFYVDTLGLHVTDEDDNAIylrGVEEFIHH-TLVLRK----APEAAVG-------HLGFRV-----R 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1525783404  83 TLADRLTAAGTDFVLNPQVRFEGEPGEQWTMFFVDPFGNPIE 124
Cdd:cd07266    70 DEADLDKAAAFYKELGLPTEWREEPGQGRTLRVEDPFGFPIE 111
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-125 2.20e-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: 35.52  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1525783404   5 FHLAFNITDLDEARRFYGGVLGCKEGRSTDTWVDFDFFGHQISLHLgkpfeTARTGRVGNALvpmPHFGI-ILLLPAWRT 83
Cdd:cd07254     3 FHLSLNVTDLERSIRFYSDLFGAEPAKRKADYAKFMLEDPPLNLAL-----LVNDRKEPYGL---NHLGIqVDSKEEVAA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1525783404  84 LADRLTAAGTDFVLNPQVRFEGEPGEQ-WTmffVDPFGNPIEV 125
Cdd:cd07254    75 LKARAEAAGLPVRKEPRTTCCYAVQDKfWL---TDPDGNAWEF 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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