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Conserved domains on  [gi|499273740|ref|WP_010971133|]
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MULTISPECIES: VOC family protein [Agrobacterium tumefaciens complex]

Protein Classification

bleomycin resistance protein( domain architecture ID 10170075)

bleomycin resistance protein (BRP) is a binding protein with a strong affinity to the bleomycin family of antibiotics

CATH:  3.10.180.10
Gene Ontology:  GO:0046677
PubMed:  21820381

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 9-135 3.63e-36

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: 120.41  E-value: 3.63e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273740   9 VPELAVSDWQKSRAFYCDLIGFHVVYERPEEGFAYLALGDAQLMIDQIGATRtfvsgnaslepPFGRGMNLQLAVPSLQP 88
Cdd:cd08349    1 IPILPVRDIDKTLAFYVDVLGFEVDYERPPPGYAILSRGGVELHLFEHPGLD-----------PAGSGVAAYIRVEDIDA 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 499273740  89 ILFRLERAliGLVLEPEEKWYRRGTVEVGNRQFIVADPDGYLIRPFE 135
Cdd:cd08349   70 LHAELKAA--GLPLFGIPRITPIEDKPWGMREFAVVDPDGNLLRFGQ 114
 
Name Accession Description Interval E-value
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 9-135 3.63e-36

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: 120.41  E-value: 3.63e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273740   9 VPELAVSDWQKSRAFYCDLIGFHVVYERPEEGFAYLALGDAQLMIDQIGATRtfvsgnaslepPFGRGMNLQLAVPSLQP 88
Cdd:cd08349    1 IPILPVRDIDKTLAFYVDVLGFEVDYERPPPGYAILSRGGVELHLFEHPGLD-----------PAGSGVAAYIRVEDIDA 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 499273740  89 ILFRLERAliGLVLEPEEKWYRRGTVEVGNRQFIVADPDGYLIRPFE 135
Cdd:cd08349   70 LHAELKAA--GLPLFGIPRITPIEDKPWGMREFAVVDPDGNLLRFGQ 114
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 12-131 2.78e-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: 54.23  E-value: 2.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273740  12 LAVSDWQKSRAFYCDLIGFHVVYERPEE----GFAYLALGD-AQLMIdqigatrtFVSGNASLEPPFGRGMNLQLAVPSL 86
Cdd:COG0346    8 LRVSDLEASLAFYTDVLGLELVKRTDFGdggfGHAFLRLGDgTELEL--------FEAPGAAPAPGGGGLHHLAFRVDDL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 499273740  87 QPILFRLERAliGLVLEPEekwyrRGTVEVGNRQFIVADPDGYLI 131
Cdd:COG0346   80 DAAYARLRAA--GVEIEGE-----PRDRAYGYRSAYFRDPDGNLI 117
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
12-131 2.35e-07

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 46.67  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273740   12 LAVSDWQKSRAFYCDLIGFHVVYERPEEgfAYLALGDAQLMIDQIGATRTFVSgNASLEPPFGRGMNLQLAVPSLQPILF 91
Cdd:pfam00903   7 LRVGDLEKSLDFYTDVLGFKLVEETDAG--EEGGLRSAFFLAGGRVLELLLNE-TPPPAAAGFGGHHIAFIAFSVDDVDA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 499273740   92 ---RLERALIGLVLEPeekwyrrGTVEVGNRQFIVADPDGYLI 131
Cdd:pfam00903  84 aydRLKAAGVEIVREP-------GRHGWGGRYSYFRDPDGNLI 119
 
Name Accession Description Interval E-value
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 9-135 3.63e-36

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: 120.41  E-value: 3.63e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273740   9 VPELAVSDWQKSRAFYCDLIGFHVVYERPEEGFAYLALGDAQLMIDQIGATRtfvsgnaslepPFGRGMNLQLAVPSLQP 88
Cdd:cd08349    1 IPILPVRDIDKTLAFYVDVLGFEVDYERPPPGYAILSRGGVELHLFEHPGLD-----------PAGSGVAAYIRVEDIDA 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 499273740  89 ILFRLERAliGLVLEPEEKWYRRGTVEVGNRQFIVADPDGYLIRPFE 135
Cdd:cd08349   70 LHAELKAA--GLPLFGIPRITPIEDKPWGMREFAVVDPDGNLLRFGQ 114
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 11-132 1.83e-11

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: 57.15  E-value: 1.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273740  11 ELAVSDWQKSRAFYCDLIGFHVVYERPEEGFAYLALGDaqlmidqiGATRTFVSGNASLEPPFGRGMNLQLAVPSLQPIL 90
Cdd:cd06587    3 ALRVPDLDASVAFYEEVLGFEVVSRNEGGGFAFLRLGP--------GLRLALLEGPEPERPGGGGLFHLAFEVDDVDEVD 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 499273740  91 FRLERALIGLVLEPEekwyrRGTVEVGNRQFIVADPDGYLIR 132
Cdd:cd06587   75 ERLREAGAEGELVAP-----PVDDPWGGRSFYFRDPDGNLIE 111
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 12-131 2.78e-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: 54.23  E-value: 2.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273740  12 LAVSDWQKSRAFYCDLIGFHVVYERPEE----GFAYLALGD-AQLMIdqigatrtFVSGNASLEPPFGRGMNLQLAVPSL 86
Cdd:COG0346    8 LRVSDLEASLAFYTDVLGLELVKRTDFGdggfGHAFLRLGDgTELEL--------FEAPGAAPAPGGGGLHHLAFRVDDL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 499273740  87 QPILFRLERAliGLVLEPEekwyrRGTVEVGNRQFIVADPDGYLI 131
Cdd:COG0346   80 DAAYARLRAA--GVEIEGE-----PRDRAYGYRSAYFRDPDGNLI 117
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
7-132 2.37e-08

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 49.08  E-value: 2.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273740   7 ALVPELAVSDWQKSRAFYCDLIGFHVVYERPEEG----FAYLALGDAQLMidqigatrtFVSGNASLEPPFGRGMNLQLA 82
Cdd:COG2764    1 SVTPYLVVDDAEEALEFYEDVFGFEVVFRMTDPDgkimHAELRIGGSVLM---------LSDAPPDSPAAEGNGVSLSLY 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 499273740  83 VPSLQPILFRLERALIGLVLEPEEKWYrrgtvevGNRQFIVADPDGYLIR 132
Cdd:COG2764   72 VDDVDALFARLVAAGATVVMPLQDTFW-------GDRFGMVRDPFGVLWM 114
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 12-131 6.63e-08

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: 47.94  E-value: 6.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273740  12 LAVSDWQKSRAFYCDLIGFHVVYErpEEGFAYLALGDAQLMIDQIGATRTFVSGNAsleppFGRgmnLQLAVPS--LQPI 89
Cdd:cd16357    4 LAVSDLEKSIDYWSDLLGMKVFEK--SEKSALLGYGEDQAKLELVDIPEPVDHGTA-----FGR---IAFSCPAdeLPPI 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 499273740  90 LFRLERA----LIGLV-LEPEEKwyrrGTVEVgnrqFIVADPDGYLI 131
Cdd:cd16357   74 EEKVKAAgqtiLTPLVsLDTPGK----ATVQV----VILADPDGHEI 112
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 12-131 1.08e-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: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 47.31  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273740  12 LAVSDWQKSRAFYCDLIGFHVVyERPEEGF---AYLALGDAQLMidQIGATRTFVSGNASLEPPFGRgmNLQLAVPSLQP 88
Cdd:cd07245    6 LACPDLERARRFYTDVLGLEEV-PRPPFLKfggAWLYLGGGQQI--HLVVEQNPSELPRPEHPGRDR--HPSFSVPDLDA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 499273740  89 ILFRLERALIglvlepeeKWYRRGTVEVGNRQFIVADPDGYLI 131
Cdd:cd07245   81 LKQRLKEAGI--------PYTESTSPGGGVTQLFFRDPDGNRL 115
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
12-131 2.35e-07

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 46.67  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273740   12 LAVSDWQKSRAFYCDLIGFHVVYERPEEgfAYLALGDAQLMIDQIGATRTFVSgNASLEPPFGRGMNLQLAVPSLQPILF 91
Cdd:pfam00903   7 LRVGDLEKSLDFYTDVLGFKLVEETDAG--EEGGLRSAFFLAGGRVLELLLNE-TPPPAAAGFGGHHIAFIAFSVDDVDA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 499273740   92 ---RLERALIGLVLEPeekwyrrGTVEVGNRQFIVADPDGYLI 131
Cdd:pfam00903  84 aydRLKAAGVEIVREP-------GRHGWGGRYSYFRDPDGNLI 119
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 11-135 4.60e-07

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 45.78  E-value: 4.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273740  11 ELAVSDWQKSRAFYCDLIGFHVVYERPEEG-FAYLALGDaqlmidqiGATRTFVSGNaslEPPFGRGMNLQLAVPSLQPI 89
Cdd:COG3324    9 ELPVDDLERAKAFYEEVFGWTFEDDAGPGGdYAEFDTDG--------GQVGGLMPGA---EEPGGPGWLLYFAVDDLDAA 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 499273740  90 LFRLERALIGLVLEPEEkwyrrgtVEVGNRQFIVADPDGYLIRPFE 135
Cdd:COG3324   78 VARVEAAGGTVLRPPTD-------IPPWGRFAVFRDPEGNRFGLWQ 116
VOC_like cd07238
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-131 1.24e-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: 319903  Cd Length: 112  Bit Score: 44.39  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273740   8 LVPELAVSDWQKSRAFYCDLIGFHVVyerpeegfaylalgdaqlmIDQiGATRTFVS-GNASLEPPFGRGMNLQLAVPSL 86
Cdd:cd07238    2 IVANIATADPERAAAFYGDHLGLPLV-------------------MDH-GWIVTFASpGNAHAQISLAREGGSGTVVPDL 61

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499273740  87 -------QPILFRLERALIGLVLEP-EEKWyrrgtvevGNRQFIVADPDGYLI 131
Cdd:cd07238   62 sievddvDAVHARVVAAGLRIEYGPtTEAW--------GVRRFFVRDPFGRLI 106
HPCD_N_class_II cd07266
N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 3-44 3.54e-06

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: 43.17  E-value: 3.54e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 499273740   3 IIRNALVpELAVSDWQKSRAFYCDLIGFHVVYErpEEGFAYL 44
Cdd:cd07266    2 IIRLAHA-ELVVTDLAASREFYVDTLGLHVTDE--DDNAIYL 40
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 14-128 1.38e-05

vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; uncharacterized subfamily of vicinal oxygen chelate (VOC) family contains Bacillus subtilis YwkD 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: 319940 [Multi-domain]  Cd Length: 123  Bit Score: 41.76  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273740  14 VSDWQKSRAFYCDLIGFHVVYE--RPEEGfAY---LALGDAQLMIdqigatrtFVSGNASLEPPFG--RGMN-LQLAVPS 85
Cdd:cd08352   10 CSDYEKSKDFYVDKLGFEIIREhyRPERN-DIkldLALGGYQLEL--------FIKPDAPARPSYPeaLGLRhLAFKVED 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 499273740  86 LQPILFRLERAliGLVLEPeekwyRRGTVEVGNRQFIVADPDG 128
Cdd:cd08352   81 VEATVAELKSL--GIETEP-----IRVDDFTGKKFTFFFDPDG 116
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 12-130 4.10e-04

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 37.89  E-value: 4.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273740  12 LAVSDWQKSRAFYCDLiGFHVVYERPEEGFAYLALGDAQ-LMIDQIGATRTFVsGNASLEPPFGRGMNLQLAVPSLQ--- 87
Cdd:COG3607    9 LPVADLERSRAFYEAL-GFTFNPQFSDEGAACFVLGEGIvLMLLPREKFATFT-GKPIADATGFTEVLLALNVESREevd 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 499273740  88 PILFRLERALIGLVLEPEEKWyrrgtvevGNRQFIVADPDGYL 130
Cdd:COG3607   87 ALVAKALAAGGTVLKPPQDVG--------GMYSGYFADPDGHL 121
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 12-135 4.47e-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: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 37.70  E-value: 4.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273740  12 LAVSDWQKSRAFYCDLIGFHVVYERPEEGFAYLALGDAQLMIDQIGATRTfvSGNASLEPPfgrGMNLQLAVPSLQPILF 91
Cdd:cd07264    6 LYVDDFAASLRFYRDVLGLPPRFLHEEGEYAEFDTGETKLALFSRKEMAR--SGGPDRRGS---AFELGFEVDDVEATVE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499273740  92 RLERALIGLVLEPEEKwyrrgtvEVGNRQFIVADPDGYLIRPFE 135
Cdd:cd07264   81 ELVERGAEFVREPANK-------PWGQTVAYVRDPDGNLIEICE 117
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
11-131 5.05e-04

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 38.02  E-value: 5.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273740  11 ELAVSDWQKSRAFYCDLIGFHVVYErpEEGFAYLALGDAQLMIdqigatrTFVSGNASLEPPFGRGMN-LQLAVPS---L 86
Cdd:COG2514    8 TLRVRDLERSAAFYTDVLGLEVVER--EGGRVYLRADGGEHLL-------VLEEAPGAPPRPGAAGLDhVAFRVPSradL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 499273740  87 QPILFRLERALIGLVlEPEEKWYRRGtvevgnrqFIVADPDGYLI 131
Cdd:COG2514   79 DAALARLAAAGVPVE-GAVDHGVGES--------LYFRDPDGNLI 114
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 12-48 6.35e-04

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: 37.26  E-value: 6.35e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 499273740  12 LAVSDWQKSRAFYCDLIGFHVVyERPEEGfAYLALGD 48
Cdd:cd07244    7 LAVSDLERSLAFYVDLLGFKPH-VRWDKG-AYLTAGD 41
TioX_like cd08355
Micromonospora sp. TioX and similar proteins; Micromonospora sp. TioX is encoded by a gene of ...
 8-130 6.64e-04

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: 37.40  E-value: 6.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273740   8 LVPELAVSDWQKSRAFYCDLIGFH--VVYERPEEGF--AYLALGDAQLMIDQIGATRTFVSGNASLEppfGRGMNLQLAV 83
Cdd:cd08355    1 VVPTLRYRDAVAAIDWLVEAFGFEerMVVPGDEGTIhhAELTFGGGGVMVGSVRDEARPDRPADAGG---HGTQSVYVAV 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 499273740  84 PSLQPILFRLERALIGLVLEPEEKWYrrgtvevGNRQFIVADPDGYL 130
Cdd:cd08355   78 ADPDAHYERARAAGAEIVMEPTDTDY-------GSRDYSARDPEGHL 117
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 12-131 1.86e-03

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: 36.05  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273740  12 LAVSDWQKSRAFYCDLIGFHVVyeRPEEGFAYLALGDAQLMIDQIGatrtfvsgnASLEPPFGRGM----NLQLAV-PSL 86
Cdd:cd07253    9 LTVKDIERTIDFYTKVLGMTVV--TFKEGRKALRFGNQKINLHQKG---------KEFEPKASAPTpgsaDLCFITeTPI 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 499273740  87 QPILFRLERALIGLVLEPEEKWYRRGTVevgnRQFIVADPDGYLI 131
Cdd:cd07253   78 DEVLEHLEACGVTIEEGPVKRTGALGPI----LSIYFRDPDGNLI 118
VOC_like cd09011
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-137 2.30e-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: 319953  Cd Length: 122  Bit Score: 35.91  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273740   8 LVPELAVSDWQKSRAFYCDLI--------GFHVVYerpEEGFAyLALGDAQLmidqigatrTFVSGNASLEPPFGRGMNL 79
Cdd:cd09011    4 VNPLLVVKDIEKSKKFYEDVLgqkilldfGENVVF---EGGFA-LQEKKSWL---------ETIIISDLSIKQQSNNFEL 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499273740  80 QLAVPSLQPILFRLERAL-IGLVLEPEEKwyrrgtvEVGNRQFIVADPDGYLIRPFESL 137
Cdd:cd09011   71 YFEVDDFDAFFEKLNPHKdIEFIHPILEH-------PWGQRVFRFYDPDGHIIEIGESM 122
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 12-132 2.33e-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: 35.74  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499273740  12 LAVSDWQKSRAFYCDLIGFHVVYERPEEGFAYLALGDAqlmiDQIGAtrTFVSGNASLEPPFGRGMNLQLAVPSLQpiLF 91
Cdd:cd07263    4 LYVDDQDKALDFYVEKLGFEVVEDVPMGGMRWVTVAPP----GSPGT--SLLLEPKAHPAQMPQSPEAAGGTPGIL--LA 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 499273740  92 ---------RLERALIGLVLEPEEKWYrrGTVevgnrqFIVADPDGYLIR 132
Cdd:cd07263   76 tddidatyeRLTAAGVTFVQEPTQMGG--GRV------ANFRDPDGNLFA 117
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 12-55 3.42e-03

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: 35.23  E-value: 3.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 499273740  12 LAVSDWQKSRAFYCDLIGFHVVYERPEEGF-----AYLALGDAQLMIDQ 55
Cdd:cd08345    4 LIVRDLEKSTAFLQDIFGAREVYSSGDKTFslskeKFFLLGGLWIALME 52
 
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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