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Conserved domains on  [gi|499271008|ref|WP_010968401|]
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MULTISPECIES: VOC family protein [Sinorhizobium]

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 ...
 4-122 1.12e-48

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 cd08359:

Pssm-ID: 472697 [Multi-domain]  Cd Length: 119  Bit Score: 152.17  E-value: 1.12e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271008   4 TSYYPVIMTQDVRQTADFYVRHLSFEALFVSDWYMHLQSTENEHVTLAVLDYRHETVPERHRAPVQGLLLNFEVEDPDRL 83
Cdd:cd08359    1 QSLGPVIVTEDVAATAAFYVKHFGFRVIFDSDWYVSLRRAERHGFELAIMDGQHGAVPAASQTQSSGLIINFEVDDADAE 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 499271008  84 YTQMREAGLPILKPICDEDFGQRHFITADPNGVMIDIIK 122
Cdd:cd08359   81 YERLTQAGLEFLEPPRDEPWGQRRFIVRDPNGVLIDVIQ 119
 
Name Accession Description Interval E-value
VOC_like cd08359
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 4-122 1.12e-48

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: 319947 [Multi-domain]  Cd Length: 119  Bit Score: 152.17  E-value: 1.12e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271008   4 TSYYPVIMTQDVRQTADFYVRHLSFEALFVSDWYMHLQSTENEHVTLAVLDYRHETVPERHRAPVQGLLLNFEVEDPDRL 83
Cdd:cd08359    1 QSLGPVIVTEDVAATAAFYVKHFGFRVIFDSDWYVSLRRAERHGFELAIMDGQHGAVPAASQTQSSGLIINFEVDDADAE 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 499271008  84 YTQMREAGLPILKPICDEDFGQRHFITADPNGVMIDIIK 122
Cdd:cd08359   81 YERLTQAGLEFLEPPRDEPWGQRRFIVRDPNGVLIDVIQ 119
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
7-123 4.47e-19

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 76.82  E-value: 4.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271008   7 YPVIMTQDVRQTADFYVRHLSFEALFVSD------WYMHLQStenEHVTLAVLDyrheTVPERHRAPVQGLLLNFEVEDP 80
Cdd:COG2764    3 TPYLVVDDAEEALEFYEDVFGFEVVFRMTdpdgkiMHAELRI---GGSVLMLSD----APPDSPAAEGNGVSLSLYVDDV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 499271008  81 DRLYTQMREAGLPILKPICDEDFGQRHFITADPNGVMIDIIKP 123
Cdd:COG2764   76 DALFARLVAAGATVVMPLQDTFWGDRFGMVRDPFGVLWMINTP 118
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
9-120 3.94e-10

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 53.61  E-value: 3.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271008    9 VIMTQDVRQTADFYVRHLSFEALFVSD-----WYMHLQSTENEHVtlAVLDYRHETVPERHRAPVQGLLLN-FEVEDPDR 82
Cdd:pfam00903   6 ALRVGDLEKSLDFYTDVLGFKLVEETDageegGLRSAFFLAGGRV--LELLLNETPPPAAAGFGGHHIAFIaFSVDDVDA 83

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 499271008   83 LYTQMREAGLPILKPICDEDFGQRHFITADPNGVMIDI 120
Cdd:pfam00903  84 AYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
VOC_like cd08359
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 4-122 1.12e-48

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: 319947 [Multi-domain]  Cd Length: 119  Bit Score: 152.17  E-value: 1.12e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271008   4 TSYYPVIMTQDVRQTADFYVRHLSFEALFVSDWYMHLQSTENEHVTLAVLDYRHETVPERHRAPVQGLLLNFEVEDPDRL 83
Cdd:cd08359    1 QSLGPVIVTEDVAATAAFYVKHFGFRVIFDSDWYVSLRRAERHGFELAIMDGQHGAVPAASQTQSSGLIINFEVDDADAE 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 499271008  84 YTQMREAGLPILKPICDEDFGQRHFITADPNGVMIDIIK 122
Cdd:cd08359   81 YERLTQAGLEFLEPPRDEPWGQRRFIVRDPNGVLIDVIQ 119
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
7-123 4.47e-19

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 76.82  E-value: 4.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271008   7 YPVIMTQDVRQTADFYVRHLSFEALFVSD------WYMHLQStenEHVTLAVLDyrheTVPERHRAPVQGLLLNFEVEDP 80
Cdd:COG2764    3 TPYLVVDDAEEALEFYEDVFGFEVVFRMTdpdgkiMHAELRI---GGSVLMLSD----APPDSPAAEGNGVSLSLYVDDV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 499271008  81 DRLYTQMREAGLPILKPICDEDFGQRHFITADPNGVMIDIIKP 123
Cdd:COG2764   76 DALFARLVAAGATVVMPLQDTFWGDRFGMVRDPFGVLWMINTP 118
VOC_like cd07238
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-121 8.25e-14

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: 319903  Cd Length: 112  Bit Score: 63.26  E-value: 8.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271008   8 PVIMTQDVRQTADFYVRHLSFEALFVSDWYMHLQSTENEH--VTLAVLDYRHETVPErhrapvqgllLNFEVEDPDRLYT 85
Cdd:cd07238    4 ANIATADPERAAAFYGDHLGLPLVMDHGWIVTFASPGNAHaqISLAREGGSGTVVPD----------LSIEVDDVDAVHA 73

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499271008  86 QMREAGLPILKPICDEDFGQRHFITADPNGVMIDII 121
Cdd:cd07238   74 RVVAAGLRIEYGPTTEAWGVRRFFVRDPFGRLINIL 109
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 9-121 3.88e-10

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: 53.84  E-value: 3.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271008   9 VIMTQDVRQTADFYVRHLSFEALFVSDWymhlqstENEHVTLAVLDYRHETV------PERHRAPVQGLL--LNFEVEDP 80
Cdd:COG0346    7 TLRVSDLEASLAFYTDVLGLELVKRTDF-------GDGGFGHAFLRLGDGTElelfeaPGAAPAPGGGGLhhLAFRVDDL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 499271008  81 DRLYTQMREAGLPILKPICDEDFGQRHFITADPNGVMIDII 121
Cdd:COG0346   80 DAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELV 120
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
9-120 3.94e-10

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 53.61  E-value: 3.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271008    9 VIMTQDVRQTADFYVRHLSFEALFVSD-----WYMHLQSTENEHVtlAVLDYRHETVPERHRAPVQGLLLN-FEVEDPDR 82
Cdd:pfam00903   6 ALRVGDLEKSLDFYTDVLGFKLVEETDageegGLRSAFFLAGGRV--LELLLNETPPPAAAGFGGHHIAFIaFSVDDVDA 83

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 499271008   83 LYTQMREAGLPILKPICDEDFGQRHFITADPNGVMIDI 120
Cdd:pfam00903  84 AYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 7-125 1.18e-09

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 52.33  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271008   7 YPVIMTQDVRQTADFYVRHLSFEALFVSDWYMHLQSTENEHVTLAVLdYRHETVPErhrapVQGLLLNFEVEDPDRLYTQ 86
Cdd:COG3324    7 WVELPVDDLERAKAFYEEVFGWTFEDDAGPGGDYAEFDTDGGQVGGL-MPGAEEPG-----GPGWLLYFAVDDLDAAVAR 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 499271008  87 MREAGLPILKPICDEDFGQRHFITADPNGVMIDIIKPIP 125
Cdd:COG3324   81 VEAAGGTVLRPPTDIPPWGRFAVFRDPEGNRFGLWQPAA 119
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 7-120 8.11e-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: 47.52  E-value: 8.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271008   7 YPVIMTQDVRQTADFYVRHLSFEALFVSDWYMHLQSTENEHVTLAVLDYRHETVPERHRapvqGLLLNFEVEDPDRLYTQ 86
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGFAFLRLGPGLRLALLEGPEPERPGGGG----LFHLAFEVDDVDEVDER 76

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499271008  87 MREAGL--PILKPICDEDFGQRHFITADPNGVMIDI 120
Cdd:cd06587   77 LREAGAegELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-123 3.84e-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: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 45.79  E-value: 3.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271008   7 YPVIMTQDVRQTADFYVRHLSFE--ALFVSDWYMHLQSTEnehVTLAVLDYR---HETVPERHRAPvqgLLLNFEVEDPD 81
Cdd:cd07264    3 YIVLYVDDFAASLRFYRDVLGLPprFLHEEGEYAEFDTGE---TKLALFSRKemaRSGGPDRRGSA---FELGFEVDDVE 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 499271008  82 RLYTQMREAGLPILKPICDEDFGQRHFITADPNGVMIDIIKP 123
Cdd:cd07264   77 ATVEELVERGAEFVREPANKPWGQTVAYVRDPDGNLIEICEP 118
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 8-115 2.03e-06

Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance protein, confers Bm resistance by directly binding to Bm. Bm is a glycopeptide antibiotic produced naturally by actinomycetes. It is a potent anti-cancer drug, which acts as a strong DNA-cutting agent, thereby causing cell death. BLMA is produced by actinomycetes to protect themselves against their own lethal compound. BLMA has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMAs are dimers and each dimer binds to two Bm molecules at the Bm-binding pockets formed at the dimer interface; two Bm molecules are bound per dimer. BLMA belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. As for the larger superfamily, this family contains members with or without domain swapping.


Pssm-ID: 319937 [Multi-domain]  Cd Length: 114  Bit Score: 43.75  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271008   8 PVIMTQDVRQTADFYVRHLSFEA---------LFVS--DWYMHLQSTenehvtlavldyrHETVPERHRAPVQglllnFE 76
Cdd:cd08349    2 PILPVRDIDKTLAFYVDVLGFEVdyerpppgyAILSrgGVELHLFEH-------------PGLDPAGSGVAAY-----IR 63

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499271008  77 VEDPDRLYTQMREAGLP-----ILKPICDEDFGQRHFITADPNG 115
Cdd:cd08349   64 VEDIDALHAELKAAGLPlfgipRITPIEDKPWGMREFAVVDPDG 107
TioX_like cd08355
Micromonospora sp. TioX and similar proteins; Micromonospora sp. TioX is encoded by a gene of ...
 7-115 2.06e-06

Micromonospora sp. TioX and similar proteins; Micromonospora sp. TioX is encoded by a gene of the thiocoraline biosynthetic gene cluster. Thiocoraline is a thiodepsipeptide with potent antitumor activity. TioX may be involved in thiocoraline resistance or secretion. TioX belongs to vicinal oxygen chelate (VOC) superfamily that 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: 319943  Cd Length: 123  Bit Score: 43.95  E-value: 2.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271008   7 YPVIMTQDVRQTADFYVRHLSFEALFV----SDWYMHLQ-STENEHVTLAVL--DYRHETVPERHRAPVQGLLLnfEVED 79
Cdd:cd08355    2 VPTLRYRDAVAAIDWLVEAFGFEERMVvpgdEGTIHHAElTFGGGGVMVGSVrdEARPDRPADAGGHGTQSVYV--AVAD 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499271008  80 PDRLYTQMREAGLPILKPICDEDFGQRHFITADPNG 115
Cdd:cd08355   80 PDAHYERARAAGAEIVMEPTDTDYGSRDYSARDPEG 115
MRD cd07235
Mitomycin C resistance protein (MRD); Mitomycin C (MC) is a naturally occurring antibiotic, ...
 10-120 5.88e-05

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: 40.17  E-value: 5.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271008  10 IMTQDVRQTADFYvRHLSFEALFVSDWYMHLQSTENEHVTLAvLDyRHETVPERH---RAPVQG--LLLNFEVEDP---D 81
Cdd:cd07235    6 IVVEDMAKSLEFY-RKLGFEVPEEADSAPHTEAALPGGIRLA-LD-TEETIRSYDpgwQAPTGGgrFAIAFLCPTPaevD 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 499271008  82 RLYTQMREAGLPILKPICDEDFGQRHFITADPNGVMIDI 120
Cdd:cd07235   83 AKYAELTGAGYEGHLKPWNAPWGQRYAIVKDPDGNVVDL 121
EhpR_like cd07261
phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter ...
 14-115 3.25e-04

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: 37.77  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271008  14 DVRQTADFYVRHLSFEALFVSDWYMHLQSTENehVTLAvLDYRHETVPERHRAPvQGLLLNFEV---EDPDRLYTQMREA 90
Cdd:cd07261    8 NPERSTEFYRFLLGKEPVESSPTFASFVLSGG--AKLG-LWSSEEVEPKVAVTG-GGAELSFMVpsgEQVDEVYAEWKAM 83

                         90       100
                 ....*....|....*....|....*
gi 499271008  91 GLPILKPICDEDFGqRHFITADPNG 115
Cdd:cd07261   84 GIPIIQEPTTMDFG-YTFVATDPDG 107
PsjN_like cd16356
Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme ...
 7-115 1.59e-03

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: 36.25  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271008   7 YPVIMTQDVRQTADFYVRHLSFEALF--VSDWYMHLQSTENEHVTLAVLDYRHETVPERHRAPVQGLLLNFEVEDP---D 81
Cdd:cd16356    1 YVNIFTADIVALSDFYSELFGLEEIFeiRSPIFRGLRTGDSCLGFNAPEAYELLGLPEFSDTPGIRILLTFDVDDVeavD 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 499271008  82 RLYTQMREAGLPILKPICDEDFGQRHFITADPNG 115
Cdd:cd16356   81 RLVPRAAALGATLIKPPYDTYYGWYQAVLLDPEG 114
VOC_like cd07246
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 12-117 2.32e-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: 319910 [Multi-domain]  Cd Length: 124  Bit Score: 35.74  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271008  12 TQDVRQTADFYVRHLSFEALFVSDwymhlqsTENEHVTLAVLDYRHETV------PER-----HRAPVQGLLLNFEVEDP 80
Cdd:cd07246    9 VEDAAAAIAFYKKAFGAEELGRTT-------QEDGRVGHAELRIGGTVVmvadenPERgalspTKLGGTPVIFHLYVEDV 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 499271008  81 DRLYTQMREAGLPILKPICDEDFGQRHFITADPNGVM 117
Cdd:cd07246   82 DATFARAVAAGAVVVEPVEDQFWGDRVGKVKDPFGHV 118
BLMT_like cd08350
BLMT, a bleomycin resistance protein encoded on the transposon Tn5, and similar proteins; BLMT ...
 18-121 4.02e-03

BLMT, a bleomycin resistance protein encoded on the transposon Tn5, and similar proteins; BLMT is a bleomycin (Bm) resistance protein, encoded by the ble gene on the transposon Tn5. This protein confers a survival advantage to Escherichia coli host cells. Bm is a glycopeptide antibiotic produced naturally by actinomycetes. It is a potent anti-cancer drug, which acts as a strong DNA-cutting agent, thereby causing cell death. BLMT has strong binding affinity to Bm and it protects against this lethal compound through drug sequestering. BLMT has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMT is a dimer with two Bm-binding pockets formed at the dimer interface.


Pssm-ID: 319938  Cd Length: 118  Bit Score: 34.95  E-value: 4.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271008  18 TADFYVRhLSFEALFVSDWYMHLQSTEnehVTLAVldYRH-ETVPERHRAPVqglllNFEVEDPDRLYTQMREAGLPI-- 94
Cdd:cd08350   16 TAAFYAR-LGFQTVYRDDGWMILRRGD---LTLEF--FPHpDLDPAASWFSC-----CLRVDDLDALYAQWSAAGIPEdt 84

                         90       100       110
                 ....*....|....*....|....*....|..
gi 499271008  95 -----LKPICDEDFGQRHFITADPNGVMIDII 121
Cdd:cd08350   85 rgiprLHPPQTQPWGIRMFALIDPDGSLLRLI 116
 
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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