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Conserved domains on  [gi|2621405839|ref|WP_318936406|]
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VOC family protein [Pseudidiomarina sp.]

Protein Classification

VOC family protein( domain architecture ID 50733)

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
VOC super family cl14632
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 8-133 3.72e-44

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.


The actual alignment was detected with superfamily member cd07251:

Pssm-ID: 472697 [Multi-domain]  Cd Length: 120  Bit Score: 140.51  E-value: 3.72e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   8 ITLGVDDLQRSLAFYRDLlGFPTDGIVgeaydYGAVVFFKmTNGQVLALWERKSIAADCGVTQGTPDPTAFMLAHNVSGK 87
Cdd:cd07251     2 ITLGVRDLERSARFYEAL-GWKPNLDP-----NDGVVFFQ-LGGTVLALYPRDALAEDAGVSVTGAGFSGVTLAHNVRSR 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2621405839  88 DEVDQLMNELARAGTHICKPARKLAWGGYGGVFQDPDQHLWEVVYN 133
Cdd:cd07251    75 EEVDQLLAKAVAAGGKILKPPQEVFWGGYSGYFADPDGHIWEVAYN 120
 
Name Accession Description Interval E-value
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-133 3.72e-44

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: 319914 [Multi-domain]  Cd Length: 120  Bit Score: 140.51  E-value: 3.72e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   8 ITLGVDDLQRSLAFYRDLlGFPTDGIVgeaydYGAVVFFKmTNGQVLALWERKSIAADCGVTQGTPDPTAFMLAHNVSGK 87
Cdd:cd07251     2 ITLGVRDLERSARFYEAL-GWKPNLDP-----NDGVVFFQ-LGGTVLALYPRDALAEDAGVSVTGAGFSGVTLAHNVRSR 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2621405839  88 DEVDQLMNELARAGTHICKPARKLAWGGYGGVFQDPDQHLWEVVYN 133
Cdd:cd07251    75 EEVDQLLAKAVAAGGKILKPPQEVFWGGYSGYFADPDGHIWEVAYN 120
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 2-132 1.85e-41

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 133.80  E-value: 1.85e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   2 KPLISYITLGVDDLQRSLAFYRDLlGFPTDgivgEAYDYGAVVFFKMTNGQVLALWERKSIAADCGVT-QGTPDPTAFML 80
Cdd:COG3607     1 MPRIIFVNLPVADLERSRAFYEAL-GFTFN----PQFSDEGAACFVLGEGIVLMLLPREKFATFTGKPiADATGFTEVLL 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2621405839  81 AHNVSGKDEVDQLMNELARAGTHICKPARKlAWGGYGGVFQDPDQHLWEVVY 132
Cdd:COG3607    76 ALNVESREEVDALVAKALAAGGTVLKPPQD-VGGMYSGYFADPDGHLWEVAW 126
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
5-130 1.33e-16

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 70.55  E-value: 1.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   5 ISYITLGVDDLQRSLAFYRDLLGFPTDGIVGEAYDYGAVVFFKMTNGQVLALWERKSIAADcgvtqgTPDPTAFMLAHNV 84
Cdd:pfam00903   2 IDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLNETPPPA------AAGFGGHHIAFIA 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2621405839  85 SGKDEVDQLMNELARAGTHICKPARKLAWGGYGGVFQDPDQHLWEV 130
Cdd:pfam00903  76 FSVDDVDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-133 3.72e-44

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: 319914 [Multi-domain]  Cd Length: 120  Bit Score: 140.51  E-value: 3.72e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   8 ITLGVDDLQRSLAFYRDLlGFPTDGIVgeaydYGAVVFFKmTNGQVLALWERKSIAADCGVTQGTPDPTAFMLAHNVSGK 87
Cdd:cd07251     2 ITLGVRDLERSARFYEAL-GWKPNLDP-----NDGVVFFQ-LGGTVLALYPRDALAEDAGVSVTGAGFSGVTLAHNVRSR 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2621405839  88 DEVDQLMNELARAGTHICKPARKLAWGGYGGVFQDPDQHLWEVVYN 133
Cdd:cd07251    75 EEVDQLLAKAVAAGGKILKPPQEVFWGGYSGYFADPDGHIWEVAYN 120
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 2-132 1.85e-41

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 133.80  E-value: 1.85e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   2 KPLISYITLGVDDLQRSLAFYRDLlGFPTDgivgEAYDYGAVVFFKMTNGQVLALWERKSIAADCGVT-QGTPDPTAFML 80
Cdd:COG3607     1 MPRIIFVNLPVADLERSRAFYEAL-GFTFN----PQFSDEGAACFVLGEGIVLMLLPREKFATFTGKPiADATGFTEVLL 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2621405839  81 AHNVSGKDEVDQLMNELARAGTHICKPARKlAWGGYGGVFQDPDQHLWEVVY 132
Cdd:COG3607    76 ALNVESREEVDALVAKALAAGGTVLKPPQD-VGGMYSGYFADPDGHLWEVAW 126
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 5-136 2.75e-21

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: 82.35  E-value: 2.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   5 ISYITLGVDDLQRSLAFYRDLLGFPTDGIVGEAYDYGAVVFFKMTNGQVLALWERKSIAADCGVTQGTpdptafMLAHNV 84
Cdd:COG0346     3 LHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTELELFEAPGAAPAPGGGGLH------HLAFRV 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2621405839  85 sgkDEVDQLMNELARAGTHICKPARKLAWGGYGGVFQDPDQHLWEVVYNPNS 136
Cdd:COG0346    77 ---DDLDAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVEPPPG 125
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
5-130 1.33e-16

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 70.55  E-value: 1.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   5 ISYITLGVDDLQRSLAFYRDLLGFPTDGIVGEAYDYGAVVFFKMTNGQVLALWERKSIAADcgvtqgTPDPTAFMLAHNV 84
Cdd:pfam00903   2 IDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLNETPPPA------AAGFGGHHIAFIA 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2621405839  85 SGKDEVDQLMNELARAGTHICKPARKLAWGGYGGVFQDPDQHLWEV 130
Cdd:pfam00903  76 FSVDDVDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-130 6.88e-16

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: 68.51  E-value: 6.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   5 ISYITLGVDDLQRSLAFYRDLLGFPTDGIVGEAyDYGAVVffkmTNGQVLALWERKSIAADCGvtqGTPDPTAFMLAHNV 84
Cdd:cd07264     1 IAYIVLYVDDFAASLRFYRDVLGLPPRFLHEEG-EYAEFD----TGETKLALFSRKEMARSGG---PDRRGSAFELGFEV 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2621405839  85 sgkDEVDQLMNELARAGTHICKPARKLAWGGYGGVFQDPDQHLWEV 130
Cdd:cd07264    73 ---DDVEATVEELVERGAEFVREPANKPWGQTVAYVRDPDGNLIEI 115
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 7-130 1.36e-15

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: 67.55  E-value: 1.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   7 YITLGVDDLQRSLAFYRDLLGFPtdgiVGEAYDYGAVVFFKMTNGQVLALWERKSIaadcgvtQGTPDPTAFMLAHNVSG 86
Cdd:cd06587     1 HVALRVPDLDASVAFYEEVLGFE----VVSRNEGGGFAFLRLGPGLRLALLEGPEP-------ERPGGGGLFHLAFEVDD 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2621405839  87 KDEVDQLMNELARAGTHICKPARKlAWGGYGGVFQDPDQHLWEV 130
Cdd:cd06587    70 VDEVDERLREAGAEGELVAPPVDD-PWGGRSFYFRDPDGNLIEF 112
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-131 1.42e-15

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 67.74  E-value: 1.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   1 MKPLISYITLGVDDLQRSLAFYRDLLGFPTDGIVGEAYDYgavVFFKMTNGQVLALWERKsiaadcgvtqGTPDPTAFML 80
Cdd:COG3324     1 MPGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPGGDY---AEFDTDGGQVGGLMPGA----------EEPGGPGWLL 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2621405839  81 AHNVsgkDEVDQLMNELARAGTHICKPARKLAWGGYGGVFQDPDQHLWEVV 131
Cdd:COG3324    68 YFAV---DDLDAAVARVEAAGGTVLRPPTDIPPWGRFAVFRDPEGNRFGLW 115
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
5-132 8.75e-14

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 63.44  E-value: 8.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   5 ISYITLGVDDLQRSLAFYRDLLGFPtdgivgEAYDYGAVVFFKMTNG-QVLALWERKSIAADCGvtQGTPDPTAFmlahN 83
Cdd:COG2514     4 LGHVTLRVRDLERSAAFYTDVLGLE------VVEREGGRVYLRADGGeHLLVLEEAPGAPPRPG--AAGLDHVAF----R 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2621405839  84 VSGKDEVDQLMNELARAGTHIckPARKLAWGGYGGVFQDPDQHLWEVVY 132
Cdd:COG2514    72 VPSRADLDAALARLAAAGVPV--EGAVDHGVGESLYFRDPDGNLIELYT 118
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
7-132 1.04e-10

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 54.86  E-value: 1.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   7 YITLGVDDLQRSLAFYRDLLGFPTDGIVGEAYDYGAVVFFKmTNGQVLALwerksiaADCGVTQGTPDPTAFMLAHNVsg 86
Cdd:COG2764     3 TPYLVVDDAEEALEFYEDVFGFEVVFRMTDPDGKIMHAELR-IGGSVLML-------SDAPPDSPAAEGNGVSLSLYV-- 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2621405839  87 kDEVDQLMNELARAGTHICKPARKLAWGGYGGVFQDPDQHLWEVVY 132
Cdd:COG2764    73 -DDVDALFARLVAAGATVVMPLQDTFWGDRFGMVRDPFGVLWMINT 117
EhpR_like cd07261
phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter ...
 8-126 2.13e-09

phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter agglomerans confers resistance by binding D-alanyl-griseoluteic acid and acting as a chaperone involved in exporting the antibiotic rather than by altering it chemically. EhpR is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319922  Cd Length: 114  Bit Score: 51.63  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   8 ITLGVDDLQRSLAFYRDLLG------FPTdgivgeaydygaVVFFKMTNGQVLALWERKSIAAdcgvtQGTPDPTAFMLA 81
Cdd:cd07261     2 VILYVDNPERSTEFYRFLLGkepvesSPT------------FASFVLSGGAKLGLWSSEEVEP-----KVAVTGGGAELS 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2621405839  82 HNVSGKDEVDQLMNELARAGTHICKPARKLAWgGYGGVFQDPDQH 126
Cdd:cd07261    65 FMVPSGEQVDEVYAEWKAMGIPIIQEPTTMDF-GYTFVATDPDGH 108
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 5-28 4.12e-07

fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin resistant protein. FosA is a Mn(II) and K(+)-dependent glutathione transferase. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosA, catalyzes the addition of glutathione to the antibiotic fosfomycin, (1R,2S)-epoxypropylphosphonic acid, making it inactive. FosA is a Mn(II) dependent enzyme. It is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319908 [Multi-domain]  Cd Length: 121  Bit Score: 45.74  E-value: 4.12e-07
                          10        20
                  ....*....|....*....|....
gi 2621405839   5 ISYITLGVDDLQRSLAFYRDLLGF 28
Cdd:cd07244     2 INHITLAVSDLERSLAFYVDLLGF 25
PsjN_like cd16356
Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme ...
 7-124 9.21e-07

Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme and similar proteins; Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme 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: 319963  Cd Length: 119  Bit Score: 44.72  E-value: 9.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   7 YITLGVDDLQRSLAFYRDLLGFPtdgivgEAYDYGAVVFFKM-TNGQVLALWERKSIAADCGVTQGTPDPTAFMLAHNVS 85
Cdd:cd16356     1 YVNIFTADIVALSDFYSELFGLE------EIFEIRSPIFRGLrTGDSCLGFNAPEAYELLGLPEFSDTPGIRILLTFDVD 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2621405839  86 GKDEVDQLMNELARAGTHICKPARKLAWGGYGGVFQDPD 124
Cdd:cd16356    75 DVEAVDRLVPRAAALGATLIKPPYDTYYGWYQAVLLDPE 113
VOC_like cd09012
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-132 9.39e-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: 319954  Cd Length: 127  Bit Score: 44.68  E-value: 9.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   7 YITLGVDDLQRSLAFYRDLlGFP-----TDgivgeayDYGAVVFFkmtNGQVLAL---------WERKSIAADcgvTQGT 72
Cdd:cd09012     3 FINLPVTDLEASTAFYEAL-GFKknpqfSD-------EHASCMVV---SDNIFVMllahdrfktFIPEPIAVD---AKKS 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2621405839  73 pdpTAFMLAHNVSGKDEVDQLMNELARAGTHICKPARKLAWGG-YGGVFQDPDQHLWEVVY 132
Cdd:cd09012    69 ---TEVLLTLSAKSRQEVDAFVDKAVEAGGKADPYVNGGDEGFmYGRSFEDLDGHLWEVVW 126
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 7-131 1.54e-06

N-terminal domain of type I, class II extradiol dioxygenases; This family contains the N-terminal non-catalytic domain of type I, class II extradiol dioxygenases. Dioxygenases catalyze the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms, resulting in the cleavage of aromatic rings. Two major groups of dioxygenases have been identified according to the cleavage site; extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon, whereas intradiol enzymes cleave the aromatic ring between two hydroxyl groups. Extradiol dioxygenases are classified into type I and type II enzymes. Type I extradiol dioxygenases include class I and class II enzymes. These two classes of enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. The extradiol dioxygenases represented in this family are type I, class II enzymes, and are composed of the N- and C-terminal domains of similar structure fold, resulting from an ancient gene duplication. The active site is located in a funnel-shaped space of the C-terminal domain. A catalytically essential metal, Fe(II) or Mn(II), presents in all the enzymes in this family.


Pssm-ID: 319967  Cd Length: 111  Bit Score: 43.84  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   7 YITLGVDDLQRSLAFYRDLLGfptdgiVGEAYDYGAVVFFKMTNgqvlalwerkSIAADCGVTQGtPDPTAFMLAHNVSG 86
Cdd:cd16360     1 YAELGVPDLEKALEFYTDVLG------LQVAKRDGNSVYLRGYE----------DEHHSLVLYEA-PEAGLKHFAFEVAS 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2621405839  87 KDEVDQLMNELARAGthiCKPAR----KLAWGGYGGVFQDPDQHLWEVV 131
Cdd:cd16360    64 EEDLERAAASLTALG---CDVTWgpdgEVPGGGKGFRFQDPSGHLLELF 109
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 5-131 7.93e-06

N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from Rhodococcus rhodochrous K37, and similar proteins; 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). The enzyme contains a N-terminal and a C-terminal domain of similar structure fold, resulting from an ancient gene duplication. BphC belongs to the type I extradiol dioxygenase family, which requires a metal in the active site for its catalytic activity. Polychlorinated biphenyl degrading bacteria demonstrate multiplicity of BphCs. Bacterium Rhodococcus rhodochrous K37 has eight genes encoding BphC enzymes. This family includes the N-terminal domain of BphC5-RrK37. The crystal structure of the protein from Novosphingobium aromaticivorans has a Mn(II)in the active site, although most proteins of type I extradiol dioxygenases are activated by Fe(II).


Pssm-ID: 319950 [Multi-domain]  Cd Length: 120  Bit Score: 42.24  E-value: 7.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   5 ISYITLGVDDLQRSLAFYRDLLGFPTdgiVGEAYDygaVVFFKMTNGQ--VLALweRKSIAADCGVtqgtpdptafmLAH 82
Cdd:cd08362     4 LRYVALGVPDLAAEREFYTEVWGLEE---VAEDDD---VVYLRAEGSEhhVLRL--RQSDENRLDL-----------IAF 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2621405839  83 NVSGKDEVDQLMNELARAGTHICKPARKL--AWGGYGGVFQDPDQHLWEVV 131
Cdd:cd08362    65 AAATRADVDALAARLAAAGVRILSEPGPLddPGGGYGFRFFDPDGRTIEVS 115
FosX cd08364
fosfomycin resistant protein subfamily FosX; This subfamily family contains FosX, a fosfomycin ...
 5-129 8.14e-06

fosfomycin resistant protein subfamily FosX; This subfamily family contains FosX, a fosfomycin resistant protein. FosX is a Mn(II)-dependent fosfomycin-specific epoxide hydrolase. Fosfomycin inhibits the enzyme UDP-Nacetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosX catalyzes the addition of a water molecule to the C1 position of the antibiotic with inversion of the configuration at C1 in the presence of Mn(II). The hydrated fosfomycin loses the inhibition activity. FosX is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319952  Cd Length: 130  Bit Score: 42.26  E-value: 8.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   5 ISYITLGVDDLQRSLAFYRDLLGfptdgiVGEAYDYGAVVF------FKMTNGQVLALWERKSIAadcgvtqgtpDPTAF 78
Cdd:cd08364     4 ISHITFIVKDLDRTAAFLTEIFG------AEEVYDSGAETFslspekFFLIGGLWIAIMEGEPLL----------ERSYN 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2621405839  79 MLAHNVSgKDEVDQLMNELARAGTHIcKPARKLAWG-GYGGVFQDPDQHLWE 129
Cdd:cd08364    68 HIAFKVS-EGDLDEYRARIKKLGLEI-RPPRSRVQGeGRSLYFYDFDNHLFE 117
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 7-129 1.52e-05

Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. The three types of fosfomycin resistance proteins, employ different mechanisms to render fosfomycin [(1R,2S)-epoxypropylphosphonic acid] inactive. FosB catalyzes the addition of L-cysteine to the epoxide ring of fosfomycin. FosX catalyzes the addition of a water molecule to the C1 position of the antibiotic with inversion of configuration at C1. FosA catalyzes the addition of glutathione to the antibiotic fosfomycin, making it inactive. Catalytic activities of both FosX and FosA are Mn(II)-dependent, but FosB is activated by Mg(II). Fosfomycin resistant proteins are evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319933  Cd Length: 118  Bit Score: 41.39  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   7 YITLGVDDLQRSLAFYRDLLGF-PTDGIVGEAYDYGAVVFFKMtNGQVLALWERKSIAADcgvtqgTPDPTAFMLAhnvs 85
Cdd:cd08345     1 HITLIVRDLEKSTAFLQDIFGArEVYSSGDKTFSLSKEKFFLL-GGLWIALMEGESLQER------SYTHIAFQIQ---- 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2621405839  86 gKDEVDQLMNELARAGTHICKPARKLAWGGYGGVFQDPDQHLWE 129
Cdd:cd08345    70 -SEDFDRYAERLGALGVEMRPPRPRVEGEGRSIYFYDPDNHLFE 112
VOC_like cd09011
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 12-130 1.97e-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: 319953  Cd Length: 122  Bit Score: 41.30  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839  12 VDDLQRSLAFYRDLLGFPTdgivgeAYDYGAVVFFKmtNG---QVLALWERKSIAADCGVTQGTPDptaFMLAHNVsgkD 88
Cdd:cd09011    10 VKDIEKSKKFYEDVLGQKI------LLDFGENVVFE--GGfalQEKKSWLETIIISDLSIKQQSNN---FELYFEV---D 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2621405839  89 EVDQLMNELAR-AGTHICKPARKLAWGGYGGVFQDPDQHLWEV 130
Cdd:cd09011    76 DFDAFFEKLNPhKDIEFIHPILEHPWGQRVFRFYDPDGHIIEI 118
VOC_BsYqjT cd07242
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; The vicinal ...
 5-131 1.91e-04

vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; 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: 319906  Cd Length: 126  Bit Score: 38.62  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   5 ISYITLGVDDLQRSLAFYRDLLGFPTDGIVGEAYDYGavvfFKMTNGQVLALWERKSIAADcgvTQGTPDPTAFMLAHNV 84
Cdd:cd07242     2 VSHVELAVSDLHRSFKWFEWILGLGWKEYDTWSFGPS----WKLSGGSLLVVQQTDEFATP---EFDRARVGLNHLAFHA 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2621405839  85 SGKDEVDQLMNELARAGTHICKPARKLAWGG---YGGVFQDPDQHLWEVV 131
Cdd:cd07242    75 ESREAVDELTEKLAKIGGVRTYGDRHPFAGGpphYAAFCEDPDGIKLELV 124
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-46 2.29e-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: 2.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2621405839   5 ISYITLGVDDLQRSLAFYRDLLGfpTDGIVgEAYDYGAVVFF 46
Cdd:cd07262     1 ISHVTIGVNDLERSRAFYDAALA--PLGYK-RGFEDGGRVGY 39
MRD cd07235
Mitomycin C resistance protein (MRD); Mitomycin C (MC) is a naturally occurring antibiotic, ...
 5-127 3.26e-04

Mitomycin C resistance protein (MRD); Mitomycin C (MC) is a naturally occurring antibiotic, and antitumor agent used in the treatment of cancer. Its antitumor activity is exerted primarily through monofunctional and bifunctional alkylation of DNA. MRD binds to MC and functions as a component of the MC exporting system. MC is bound to MRD by a stacking interaction between a His and a Trp. MRD adopts a structural fold similar to bleomycin resistance protein, glyoxalase I, and extradiol dioxygenases; and it has binding sites at an identical location to binding sites in these evolutionarily related enzymes.


Pssm-ID: 319901  Cd Length: 123  Bit Score: 37.86  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   5 ISYITLGVDDLQRSLAFYRdLLGFPtdgiVGEAYDYGAVVFFKMTNGQVLALWERKSIAadcGVTQGTPDPTA---FMLA 81
Cdd:cd07235     1 ISLIAIVVEDMAKSLEFYR-KLGFE----VPEEADSAPHTEAALPGGIRLALDTEETIR---SYDPGWQAPTGggrFAIA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2621405839  82 HNVSGKDEVDQLMNELARAGTHICKPARKLAWGGYGGVFQDPDQHL 127
Cdd:cd07235    73 FLCPTPAEVDAKYAELTGAGYEGHLKPWNAPWGQRYAIVKDPDGNV 118
VOC_like cd16355
uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily; The vicinal oxygen ...
 5-126 5.74e-04

uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily; 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: 319962  Cd Length: 121  Bit Score: 37.09  E-value: 5.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   5 ISYItLGVDDLQRSLAFYRDLLGFPTDGIVGEAYDYGAVvffKMTNGQVLALWERKSIAADCGvTQGTPDPTAFMLAHNV 84
Cdd:cd16355     1 LTPV-LNVSDIPASFAWFEKVLGFQKDWDWGDPPTFGSV---GSGECEIFLCQGGQGGSLRLG-PCGDALPSYGAWMSVW 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2621405839  85 SgkDEVDQLMNELARAGTHICKPARKLAWGGYGGVFQDPDQH 126
Cdd:cd16355    76 V--DDVDALHRECRARGADIRQPPTDMPWGMREMHVRHPDGH 115
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 6-129 1.56e-03

C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family contains the C-terminal, catalytic domain of type I, class II extradiol dioxygenases. Dioxygenases catalyze the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms, resulting in the cleavage of aromatic rings. Two major groups of dioxygenases have been identified according to the cleavage site; extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon, whereas intradiol enzymes cleave the aromatic ring between two hydroxyl groups. Extradiol dioxygenases are classified into type I and type II enzymes. Type I extradiol dioxygenases include class I and class II enzymes. These two classes of enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. The extradiol dioxygenases represented in this family are type I, class II enzymes, and are composed of the N- and C-terminal domains of similar structure fold, resulting from an ancient gene duplication. The active site is located in a funnel-shaped space of the C-terminal domain. A catalytically essential metal, Fe(II) or Mn(II), presents in all the enzymes in this family.


Pssm-ID: 319931  Cd Length: 132  Bit Score: 36.14  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   6 SYITLGVDDLQRSLAFYRDLLGF-PTDGIVGEAYDYGAvvfFKMTNGQV----LALwerksiaadcgvtQGTPDPTAFML 80
Cdd:cd08343     1 GHVVLCSPDVEASRDFYTDVLGFrVSDRIVDPGVDGGA---FLHCDRGTdhhtVAL-------------AGGPHPGLHHV 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2621405839  81 AHNVSGKDEVDQLMNELARAGTHIC-KPARKLAWGGYGGVFQDPDQHLWE 129
Cdd:cd08343    65 AFEVHDLDDVGRGHDRLREKGYKIEwGPGRHGLGSQVFDYWFDPSGNRVE 114
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 12-131 1.77e-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: 319942  Cd Length: 122  Bit Score: 35.80  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839  12 VDDLQRSLAFYRDLLGFPtdgIVGEAydyGAVVFFKMTNGQVLALWERKSiaadcgvtqGTPDPTAFMLAHNVSGK---- 87
Cdd:cd08354     8 ADDLDAAEAFYEDVLGLK---PMLRS---GRHAFFRLGPQVLLVFDPGAT---------SKDVRTGEVPGHGASGHghfa 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2621405839  88 -----DEVDQLMNELARAGTHICKPARklaW--GGYGGVFQDPDQHLWEVV 131
Cdd:cd08354    73 favptEELAAWEARLEAKGVPIESYTQ---WpeGGKSLYFRDPAGNLVELA 120
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 5-124 2.75e-03

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: 35.32  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   5 ISYITLGVDDLQRSLAFYRDLLG--FPTDGIVGEAYdygaVVFfkMTNGQVLAlwerksiaadcGVTQGTPD----PTAF 78
Cdd:cd07247     1 PVWFELPTTDLERAKAFYGAVFGwtFEDEGDGGGDY----ALF--TAGGGAVG-----------GLMRAPEEvagaPPGW 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2621405839  79 MLAHNVsgkDEVDQLMNELARAGTHICKPARKLAWGGYGGVFQDPD 124
Cdd:cd07247    64 LIYFAV---DDLDAALARVEAAGGKVVVPPTDIPGGGRFAVFADPE 106
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-124 3.02e-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: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 35.37  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   8 ITLGVDDLQRSLAFYRDLLGFpTDGIVGEAYDYGaVVFFKMTNGQVLALWERKSIAADCGVTQGTpdptafMLAHNVSGK 87
Cdd:cd07245     4 VALACPDLERARRFYTDVLGL-EEVPRPPFLKFG-GAWLYLGGGQQIHLVVEQNPSELPRPEHPG------RDRHPSFSV 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2621405839  88 DEVDQLMNELARAGTHIckPARKLAWGGYGGVF-QDPD 124
Cdd:cd07245    76 PDLDALKQRLKEAGIPY--TESTSPGGGVTQLFfRDPD 111
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-131 3.86e-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: 34.97  E-value: 3.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2621405839   8 ITLGVDDLQRSLAFYRDLLGFptdgIVGEAYDYGAVVFFKMT----NGQVLALwERKSIAADCG----VTQGTPdptAFM 79
Cdd:cd07263     2 VMLYVDDQDKALDFYVEKLGF----EVVEDVPMGGMRWVTVAppgsPGTSLLL-EPKAHPAQMPqspeAAGGTP---GIL 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2621405839  80 LAhnvsgKDEVDQLMNELARAGTHICKPARKLaWGGYGGVFQDPDQHLWEVV 131
Cdd:cd07263    74 LA-----TDDIDATYERLTAAGVTFVQEPTQM-GGGRVANFRDPDGNLFALM 119
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 7-29 4.62e-03

C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. VOC 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: 319964  Cd Length: 114  Bit Score: 34.45  E-value: 4.62e-03
                          10        20
                  ....*....|....*....|...
gi 2621405839   7 YITLGVDDLQRSLAFYRDLLGFP 29
Cdd:cd16357     1 KVSLAVSDLEKSIDYWSDLLGMK 23
 
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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