NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|502821475|ref|WP_013056451|]
View 

MULTISPECIES: ArsI/CadI family heavy metal resistance metalloenzyme [Priestia]

Protein Classification

glyoxalase/bleomycin resistance/dioxygenase family protein( domain architecture ID 10163540)

glyoxalase/bleomycin resistance/dioxygenase family protein similar to Mycobacterium bovis cadmium-induced protein CadI and Bacillus sp. MD1 ArsI C-As lyase, the latter cleaves the carbon-arsenic bond in a range of trivalent organoarsenicals

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ArsI_CadI_VOC NF041414
ArsI/CadI family heavy metal resistance metalloenzyme; This family belong to the broader VOC ...
 3-144 7.95e-78

ArsI/CadI family heavy metal resistance metalloenzyme; This family belong to the broader VOC (Vicinal Oxygen Chelate) domain family (see PF00903), which includes glyoxalase I, fosfomycin resistance proteins FosA and FosB, and dioxygenases such as 4-hydroxyphenylpyruvate dioxygenase. Members of this specific family include none of those, but instead include CadI from Mycobacterium tuberculosis and ArsI from Bacillus sp. MD1. They have an invariant CC motif at about position 95, and have poorly conserved C-terminal extension regions that nearly always contain at least one addition CC motif, often several. ArsI has been characterized as an organoarsenical lyase.


:

Pssm-ID: 469305  Cd Length: 144  Bit Score: 226.71  E-value: 7.95e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   3 YVHVGINVTNLEASIEFYQKVFGVHPVKTKVDYAKFLLDEPRLNFTLnVQDEVKGNQVNHFGFQVETPQEIHSHKSRLEK 82
Cdd:NF041414   1 RVQLALNVDDLDASVAFYSKLFGVEPAKRKPGYANFAIAEPPLKLVL-LENPGAGGTLNHLGVEVESSEEVHAAIARLEE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502821475  83 EGFFARQEMDTTCCYAVQDKFWVTDPDGNEWEFFYTKSDSEVHKGEDSVGPNE---KLPVNNACC 144
Cdd:NF041414  80 AGLFTFEEIDTTCCYATQDKVWVTDPDGERWEVYTVLADSETFGTSPALAAGAaccATAAASSCC 144
 
Name Accession Description Interval E-value
ArsI_CadI_VOC NF041414
ArsI/CadI family heavy metal resistance metalloenzyme; This family belong to the broader VOC ...
 3-144 7.95e-78

ArsI/CadI family heavy metal resistance metalloenzyme; This family belong to the broader VOC (Vicinal Oxygen Chelate) domain family (see PF00903), which includes glyoxalase I, fosfomycin resistance proteins FosA and FosB, and dioxygenases such as 4-hydroxyphenylpyruvate dioxygenase. Members of this specific family include none of those, but instead include CadI from Mycobacterium tuberculosis and ArsI from Bacillus sp. MD1. They have an invariant CC motif at about position 95, and have poorly conserved C-terminal extension regions that nearly always contain at least one addition CC motif, often several. ArsI has been characterized as an organoarsenical lyase.


Pssm-ID: 469305  Cd Length: 144  Bit Score: 226.71  E-value: 7.95e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   3 YVHVGINVTNLEASIEFYQKVFGVHPVKTKVDYAKFLLDEPRLNFTLnVQDEVKGNQVNHFGFQVETPQEIHSHKSRLEK 82
Cdd:NF041414   1 RVQLALNVDDLDASVAFYSKLFGVEPAKRKPGYANFAIAEPPLKLVL-LENPGAGGTLNHLGVEVESSEEVHAAIARLEE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502821475  83 EGFFARQEMDTTCCYAVQDKFWVTDPDGNEWEFFYTKSDSEVHKGEDSVGPNE---KLPVNNACC 144
Cdd:NF041414  80 AGLFTFEEIDTTCCYATQDKVWVTDPDGERWEVYTVLADSETFGTSPALAAGAaccATAAASSCC 144
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 2-121 7.13e-65

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319917 [Multi-domain]  Cd Length: 120  Bit Score: 193.45  E-value: 7.13e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   2 KYVHVGINVTNLEASIEFYQKVFGVHPVKTKVDYAKFLLDEPRLNFTLNVQDEVKGNQVNHFGFQVETPQEIHSHKSRLE 81
Cdd:cd07254    1 KRFHLSLNVTDLERSIRFYSDLFGAEPAKRKADYAKFMLEDPPLNLALLVNDRKEPYGLNHLGIQVDSKEEVAALKARAE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 502821475  82 KEGFFARQEMDTTCCYAVQDKFWVTDPDGNEWEFFYTKSD 121
Cdd:cd07254   81 AAGLPVRKEPRTTCCYAVQDKFWLTDPDGNAWEFYATLTE 120
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-115 2.69e-18

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 75.18  E-value: 2.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475    2 KYVHVGINVTNLEASIEFYQKVFG-------VHPVKTKVDYAKFLLDEPRLNFTLNVQDEVKGNQVN--HFGFQVETPQE 72
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGfklveetDAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGghHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 502821475   73 IHSHKSRLEKEGFFARQEMDTTCCYAVQdkFWVTDPDGNEWEF 115
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHGWGGRY--SYFRDPDGNLIEL 121
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-121 2.56e-16

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 70.02  E-value: 2.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   1 MKYVHVGINVTNLEASIEFYQKVFGVHPVKT------KVDYAKFLL-DEPRLNFT--LNVQDEVKGNQVNHFGFQVETPQ 71
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRtdfgdgGFGHAFLRLgDGTELELFeaPGAAPAPGGGGLHHLAFRVDDLD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 502821475  72 EIHshkSRLEKEGF-FARQEMDTTCCYAVqdkFWVTDPDGNEWEFFYTKSD 121
Cdd:COG0346   81 AAY---ARLRAAGVeIEGEPRDRAYGYRS---AYFRDPDGNLIELVEPPPG 125
PRK04101 PRK04101
metallothiol transferase FosB;
7-115 2.26e-05

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 41.47  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   7 GIN-----VTNLEASIEFYQKVFGVHP-VKTKvDYAKFLLDEprLNFTLNVQDEVKGNQVN----HFGFQVEtPQEIHSH 76
Cdd:PRK04101   4 GINhicfsVSNLEKSIEFYEKVLGAKLlVKGR-KTAYFDLNG--LWIALNEEKDIPRNEIHqsytHIAFSIE-EEDFDHW 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 502821475  77 KSRLEKEGFF-----ARQEMDttccyavQDKFWVTDPDGNEWEF 115
Cdd:PRK04101  80 YQRLKENDVNilpgrERDERD-------KKSIYFTDPDGHKFEF 116
 
Name Accession Description Interval E-value
ArsI_CadI_VOC NF041414
ArsI/CadI family heavy metal resistance metalloenzyme; This family belong to the broader VOC ...
 3-144 7.95e-78

ArsI/CadI family heavy metal resistance metalloenzyme; This family belong to the broader VOC (Vicinal Oxygen Chelate) domain family (see PF00903), which includes glyoxalase I, fosfomycin resistance proteins FosA and FosB, and dioxygenases such as 4-hydroxyphenylpyruvate dioxygenase. Members of this specific family include none of those, but instead include CadI from Mycobacterium tuberculosis and ArsI from Bacillus sp. MD1. They have an invariant CC motif at about position 95, and have poorly conserved C-terminal extension regions that nearly always contain at least one addition CC motif, often several. ArsI has been characterized as an organoarsenical lyase.


Pssm-ID: 469305  Cd Length: 144  Bit Score: 226.71  E-value: 7.95e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   3 YVHVGINVTNLEASIEFYQKVFGVHPVKTKVDYAKFLLDEPRLNFTLnVQDEVKGNQVNHFGFQVETPQEIHSHKSRLEK 82
Cdd:NF041414   1 RVQLALNVDDLDASVAFYSKLFGVEPAKRKPGYANFAIAEPPLKLVL-LENPGAGGTLNHLGVEVESSEEVHAAIARLEE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502821475  83 EGFFARQEMDTTCCYAVQDKFWVTDPDGNEWEFFYTKSDSEVHKGEDSVGPNE---KLPVNNACC 144
Cdd:NF041414  80 AGLFTFEEIDTTCCYATQDKVWVTDPDGERWEVYTVLADSETFGTSPALAAGAaccATAAASSCC 144
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 2-121 7.13e-65

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319917 [Multi-domain]  Cd Length: 120  Bit Score: 193.45  E-value: 7.13e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   2 KYVHVGINVTNLEASIEFYQKVFGVHPVKTKVDYAKFLLDEPRLNFTLNVQDEVKGNQVNHFGFQVETPQEIHSHKSRLE 81
Cdd:cd07254    1 KRFHLSLNVTDLERSIRFYSDLFGAEPAKRKADYAKFMLEDPPLNLALLVNDRKEPYGLNHLGIQVDSKEEVAALKARAE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 502821475  82 KEGFFARQEMDTTCCYAVQDKFWVTDPDGNEWEFFYTKSD 121
Cdd:cd07254   81 AAGLPVRKEPRTTCCYAVQDKFWLTDPDGNAWEFYATLTE 120
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-115 2.69e-18

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 75.18  E-value: 2.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475    2 KYVHVGINVTNLEASIEFYQKVFG-------VHPVKTKVDYAKFLLDEPRLNFTLNVQDEVKGNQVN--HFGFQVETPQE 72
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGfklveetDAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGghHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 502821475   73 IHSHKSRLEKEGFFARQEMDTTCCYAVQdkFWVTDPDGNEWEF 115
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHGWGGRY--SYFRDPDGNLIEL 121
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 5-115 2.91e-17

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: 72.17  E-value: 2.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   5 HVGINVTNLEASIEFYQKVFGVHPVKTKV-DYAKFLLDEPRLNFTLNVQDEVK---GNQVNHFGFQVETPQEIHSHKSRL 80
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEgGGFAFLRLGPGLRLALLEGPEPErpgGGGLFHLAFEVDDVDEVDERLREA 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 502821475  81 EKEGFFARQEMDTtccYAVQDKFWVTDPDGNEWEF 115
Cdd:cd06587   81 GAEGELVAPPVDD---PWGGRSFYFRDPDGNLIEF 112
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-121 2.56e-16

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 70.02  E-value: 2.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   1 MKYVHVGINVTNLEASIEFYQKVFGVHPVKT------KVDYAKFLL-DEPRLNFT--LNVQDEVKGNQVNHFGFQVETPQ 71
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRtdfgdgGFGHAFLRLgDGTELELFeaPGAAPAPGGGGLHHLAFRVDDLD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 502821475  72 EIHshkSRLEKEGF-FARQEMDTTCCYAVqdkFWVTDPDGNEWEFFYTKSD 121
Cdd:COG0346   81 AAY---ARLRAAGVeIEGEPRDRAYGYRS---AYFRDPDGNLIELVEPPPG 125
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
5-117 1.23e-14

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 66.13  E-value: 1.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   5 HVGINVTNLEASIEFYQKVFGVHPVKTKVDYAKFLL--DEPRLNFTL--NVQDEVKGNQVNHFGFQVETPQEIHSHKSRL 80
Cdd:COG2514    6 HVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRAdgGEHLLVLEEapGAPPRPGAAGLDHVAFRVPSRADLDAALARL 85

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 502821475  81 EKEGFFARQEMDttccYAVQDKFWVTDPDGNEWEFFY 117
Cdd:COG2514   86 AAAGVPVEGAVD----HGVGESLYFRDPDGNLIELYT 118
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 5-116 1.80e-09

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: 51.93  E-value: 1.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   5 HVGINVTNLEASIEFYQKVFGVHPVKTKVDYAKFLLDEPRlNFTLnVQDEVKGNQVNHFGFQVETPQEIHSHKSRLEKEG 84
Cdd:cd16360    1 YAELGVPDLEKALEFYTDVLGLQVAKRDGNSVYLRGYEDE-HHSL-VLYEAPEAGLKHFAFEVASEEDLERAAASLTALG 78

                         90       100       110
                 ....*....|....*....|....*....|..
gi 502821475  85 fFARQEMDTTCCYAVQDKFWVTDPDGNEWEFF 116
Cdd:cd16360   79 -CDVTWGPDGEVPGGGKGFRFQDPSGHLLELF 109
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
4-117 4.95e-09

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 51.01  E-value: 4.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   4 VHVGINVTNLEASIEFYQKVFGVHPV------KTKVDYAKFLLDEPRLNFTlNVQDEVKGNQVNHFGFQVETPqEIHSHK 77
Cdd:COG2764    2 VTPYLVVDDAEEALEFYEDVFGFEVVfrmtdpDGKIMHAELRIGGSVLMLS-DAPPDSPAAEGNGVSLSLYVD-DVDALF 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 502821475  78 SRLEKEGffARQEMdttccyAVQDKFW------VTDPDGNEWEFFY 117
Cdd:COG2764   80 ARLVAAG--ATVVM------PLQDTFWgdrfgmVRDPFGVLWMINT 117
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-116 1.04e-08

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 50.02  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   1 MKYVHVGINVTNLEASIEFYQKVFG---VHPVKTKVDYAKFLLDEPRlNFTLNVQDEVKGNQVNHFGFQVETPQEIHshk 77
Cdd:COG3324    3 GTIVWVELPVDDLERAKAFYEEVFGwtfEDDAGPGGDYAEFDTDGGQ-VGGLMPGAEEPGGPGWLLYFAVDDLDAAV--- 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 502821475  78 SRLEKEGFfarqemdtTCCYAVQDK------FWVTDPDGNEWEFF 116
Cdd:COG3324   79 ARVEAAGG--------TVLRPPTDIppwgrfAVFRDPEGNRFGLW 115
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 5-115 1.97e-07

fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin resistant protein. FosB is a Mg(2+)-dependent L-cysteine thiol transferase. Fosfomycin inhibits the enzyme UDP-nacetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosB catalyzes the Mg(II) dependent addition of L-cysteine to the epoxide ring of fosfomycin, (1R,2S)-epoxypropylphosphonic acid, rendering it inactive. FosB is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319951 [Multi-domain]  Cd Length: 131  Bit Score: 46.96  E-value: 1.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   5 HVGINVTNLEASIEFYQKVFGVHPVKTKVDYAKFLLDEprLNFTLNVQDEVKGNQVN----HFGFQVeTPQEIHSHKSRL 80
Cdd:cd08363    3 HITFSVSNLNKSIAFYKDVLDAKLLVLGEKTAYFDLNG--LWLALNVQEDIPRNEIShsytHIAFSI-DEEDLDAFKERL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 502821475  81 EKEGFF-----ARQEMDttccyavQDKFWVTDPDGNEWEF 115
Cdd:cd08363   80 KDNGVNilegrKRDILE-------GQSIYFTDPDGHLFEL 112
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-115 1.32e-06

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 44.62  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   5 HVGINVTNLEASIEFYQKVFGVHPVKtKVDYAKF--------------LLDEPrlNFTLNVQDEVKGNqVNHFGFQVEtp 70
Cdd:cd07245    3 HVALACPDLERARRFYTDVLGLEEVP-RPPFLKFggawlylgggqqihLVVEQ--NPSELPRPEHPGR-DRHPSFSVP-- 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 502821475  71 qEIHSHKSRLEKEG--FFARQEMDTTccyavQDKFWVTDPDGNEWEF 115
Cdd:cd07245   77 -DLDALKQRLKEAGipYTESTSPGGG-----VTQLFFRDPDGNRLEF 117
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 5-115 1.37e-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: 44.55  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   5 HVGINVTNLEASIEFYQKVFGVHPVKTkVDYAKFLLDEPRLNFTLNVQDEVKgNQVNHFGFQVETPQEIHSHKSRLEKEG 84
Cdd:cd08362    6 YVALGVPDLAAEREFYTEVWGLEEVAE-DDDVVYLRAEGSEHHVLRLRQSDE-NRLDLIAFAAATRADVDALAARLAAAG 83

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 502821475  85 ---FFARQEMDTTCC-YAvqdkFWVTDPDGNEWEF 115
Cdd:cd08362   84 vriLSEPGPLDDPGGgYG----FRFFDPDGRTIEV 114
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 10-117 2.05e-06

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 44.05  E-value: 2.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475  10 VTNLEASIEFYQKV-FGVHPVKTKVDYAKF---------LLDEPRL-NFT-LNVQDEVKGNQVnHFGFQVETPQEIHSHK 77
Cdd:COG3607   11 VADLERSRAFYEALgFTFNPQFSDEGAACFvlgegivlmLLPREKFaTFTgKPIADATGFTEV-LLALNVESREEVDALV 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 502821475  78 SRLEKEGffARQEMDTtccyavQDKFW-----VTDPDGNEWEFFY 117
Cdd:COG3607   90 AKALAAG--GTVLKPP------QDVGGmysgyFADPDGHLWEVAW 126
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 5-115 6.93e-06

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: 42.55  E-value: 6.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   5 HVGINVTNLEASIEFYQKVFGVHPVKTKVDYAKFLLDEPRLNF-----TLNVQDEVKGNQVNHFGFQVeTPQEIHSHKSR 79
Cdd:cd08345    1 HITLIVRDLEKSTAFLQDIFGAREVYSSGDKTFSLSKEKFFLLgglwiALMEGESLQERSYTHIAFQI-QSEDFDRYAER 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 502821475  80 LEKEGFFARQEMDTTccYAVQDKFWVTDPDGNEWEF 115
Cdd:cd08345   80 LGALGVEMRPPRPRV--EGEGRSIYFYDPDNHLFEL 113
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-111 1.58e-05

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 41.55  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   5 HVGINVTNLEASIEFYQKVFGvHPVKTKVD---YAKFLLDEPRLNFTL--NVQDEVKGNQVNH---FGFQVE----TPQE 72
Cdd:cd07264    3 YIVLYVDDFAASLRFYRDVLG-LPPRFLHEegeYAEFDTGETKLALFSrkEMARSGGPDRRGSafeLGFEVDdveaTVEE 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 502821475  73 IHSHKSRLEKEgffARQEMDTtccyavQDKFWVTDPDGN 111
Cdd:cd07264   82 LVERGAEFVRE---PANKPWG------QTVAYVRDPDGN 111
PRK04101 PRK04101
metallothiol transferase FosB;
7-115 2.26e-05

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 41.47  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   7 GIN-----VTNLEASIEFYQKVFGVHP-VKTKvDYAKFLLDEprLNFTLNVQDEVKGNQVN----HFGFQVEtPQEIHSH 76
Cdd:PRK04101   4 GINhicfsVSNLEKSIEFYEKVLGAKLlVKGR-KTAYFDLNG--LWIALNEEKDIPRNEIHqsytHIAFSIE-EEDFDHW 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 502821475  77 KSRLEKEGFF-----ARQEMDttccyavQDKFWVTDPDGNEWEF 115
Cdd:PRK04101  80 YQRLKENDVNilpgrERDERD-------KKSIYFTDPDGHKFEF 116
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-117 5.64e-05

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319923 [Multi-domain]  Cd Length: 121  Bit Score: 40.29  E-value: 5.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   5 HVGINVTNLEASIEFYQKVF---GVHPVK--------TKVDYAKFLLDEPRlnftlNVQDEVKGNQvNHFGFQVETPQEI 73
Cdd:cd07262    3 HVTIGVNDLERSRAFYDAALaplGYKRGFedggrvgyGLEGGPDFWVTEPF-----DGEPATAGNG-THVAFAAPSRAAV 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 502821475  74 HS-HKSRLE-------KEGFFARQEMDTTCCYavqdkfwVTDPDGNEWEFFY 117
Cdd:cd07262   77 DAfHAAALAaggtdngAPGLRPHYHPGYYAAY-------VRDPDGNKIEAVC 121
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 5-73 3.18e-04

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: 38.45  E-value: 3.18e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502821475   5 HVGINVTNLEASIEFYQKVFGVHP----VKTKVDYAKFL-LDEPRLNFTLNVQdEVKGNQVNHFGFQVETPQEI 73
Cdd:cd08343    2 HVVLCSPDVEASRDFYTDVLGFRVsdriVDPGVDGGAFLhCDRGTDHHTVALA-GGPHPGLHHVAFEVHDLDDV 74
BphC1-RGP6_N_like cd07252
N-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase; This subfamily contains the ...
 6-117 6.74e-04

N-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase; This subfamily contains the N-terminal, non-catalytic, domain of BphC1-RGP6 and similar proteins. BphC catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). This subfamily of BphCs belongs to the type I extradiol dioxygenase family, which require a metal in the active site in its catalytic mechanism. Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of 2,3-dihydroxybiphenyl 1,2-dioxygenases. For example, three types of BphC enzymes have been found in Rhodococcus globerulus (BphC1-RGP6 - BphC3-RGP6), all three enzymes are type I extradiol dioxygenases. BphC1-RGP6 has an internal duplication, it is a two-domain dioxygenase which forms octamers, and has Fe(II) at the catalytic site. Its N-terminal repeat is represented in this subfamily. BphC2-RGP6 and BphC3-RGP6 are one-domain dioxygenases, they belong to a different family, the ED_TypeI_classII_C (C-terminal domain of type I, class II extradiol dioxygenases) family.


Pssm-ID: 319915  Cd Length: 120  Bit Score: 37.19  E-value: 6.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   6 VGINVTNLEASIEFYQKVFGVHPVKTKVDYAKFL-LDEPRLNFTLnVQDEVkgNQVNHFGFQVETPQEIHSHKSRLEKEG 84
Cdd:cd07252    6 LGFEVSDLDAWREFATDVLGLQVADDGPDDALYLrMDDRAHRIAV-HPGEV--DDLAYAGWEVADEAALDALAERLEAAG 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 502821475  85 FFARQEMDTTCC-YAVQDKFWVTDPDGNEWEFFY 117
Cdd:cd07252   83 IEVTTGSAELAAeRGVLGLIKFTDPSGNPHEIFY 116
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 5-34 1.09e-03

Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) interconverts (2R)-methylmalonyl-CoA and (2S)-methylmalonyl-CoA. MMCE has been found in bacteria, archaea, and in animals. In eukaryotes, MMCE is an essential enzyme in a pathway that converts propionyl-CoA to succinyl-CoA, and is important in the breakdown of odd-chain length fatty acids, branched-chain amino acids, and other metabolites. In bacteria, MMCE participates in the reverse pathway for propionate fermentation, glyoxylate regeneration, and the biosynthesis of polyketide antibiotics. MMCE is closely related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319912 [Multi-domain]  Cd Length: 127  Bit Score: 36.79  E-value: 1.09e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 502821475   5 HVGINVTNLEASIEFYQKVFGVHPVKTKVD 34
Cdd:cd07249    3 HIGIAVPDLDEALKFYEDVLGVKVSEPEEL 32
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 5-29 1.29e-03

vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; This subfamily of vicinal oxygen chelate (VOC) family protein includes Streptomyces hygroscopicus ValD protein and similar proteins. ValD protein functions in validamycin biosynthetic pathway. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319968  Cd Length: 150  Bit Score: 36.93  E-value: 1.29e-03
                         10        20
                 ....*....|....*....|....*
gi 502821475   5 HVGINVTNLEASIEFYQKVFGVHPV 29
Cdd:cd16361    4 HVGITVPDLDAAVEFYTDVLGAEVV 28
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 5-31 2.54e-03

4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and metabolism, General function prediction only];


Pssm-ID: 442418 [Multi-domain]  Cd Length: 333  Bit Score: 36.79  E-value: 2.54e-03
                         10        20
                 ....*....|....*....|....*....
gi 502821475   5 HVGINV--TNLEASIEFYQKVFGVHPVKT 31
Cdd:COG3185  149 HIGIAVprGDLDEWVLFYEDVLGFEEIRE 177
HPCD_N_class_II cd07266
N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 5-117 2.85e-03

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: 35.46  E-value: 2.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   5 HVGINVTNLEASIEFYQKVFGVHpVKTKVDYAKFL--LDEPRLNFTLNVQDEVKGnqVNHFGFQVETPQEihshksrLEK 82
Cdd:cd07266    7 HAELVVTDLAASREFYVDTLGLH-VTDEDDNAIYLrgVEEFIHHTLVLRKAPEAA--VGHLGFRVRDEAD-------LDK 76

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 502821475  83 EGFFArQEMDTTCCYAVQ----DKFWVTDPDGNEWEFFY 117
Cdd:cd07266   77 AAAFY-KELGLPTEWREEpgqgRTLRVEDPFGFPIEFYL 114
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 10-111 3.98e-03

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: 34.89  E-value: 3.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475  10 VTNLEASIEFYQKV--FGVHPVKTKVDYAKFLLDEPRLNFTLNVQDEVKGNQVNHFgFQVETPQEIHSHKSRLEKEGFFA 87
Cdd:cd08349    6 VRDIDKTLAFYVDVlgFEVDYERPPPGYAILSRGGVELHLFEHPGLDPAGSGVAAY-IRVEDIDALHAELKAAGLPLFGI 84

                         90       100       110
                 ....*....|....*....|....*....|
gi 502821475  88 RQEmdttccYAVQDKFW------VTDPDGN 111
Cdd:cd08349   85 PRI------TPIEDKPWgmrefaVVDPDGN 108
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 5-116 6.64e-03

N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC superfamily contains Bacillus subtilis CatE and similar proteins. CatE is proposed to function as Catechol-2,3-dioxygenase. 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: 319918  Cd Length: 124  Bit Score: 34.59  E-value: 6.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475   5 HVGINVTNLEASIEFYQKVFGVHPVKTKVDYAKFLLDEPRLNFTLNVQDEVKGNQVN-----HFGFQVETPQEIHSHKSR 79
Cdd:cd07255    5 RVTLKVADLERQSAFYQNVIGLSVLKQNASRAYLGVDGKQVLLVLEAIPDAVLAPRSttglyHFAILLPDRKALGRALAH 84

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 502821475  80 LEKEGFfarqeMDTTCCYAVQDKFWVTDPDGNEWEFF 116
Cdd:cd07255   85 LAEHGP-----LIGAADHGVSEAIYLSDPEGNGIEIY 116
EhpR_like cd07261
phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter ...
 10-110 7.73e-03

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: 34.30  E-value: 7.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502821475  10 VTNLEASIEFYQKVFGVHPVKTKVDYAKFLLDEPrLNFTLNVQDEVKGNQVNHFG-----FQVETPQEIHSHKSRLEKEG 84
Cdd:cd07261    6 VDNPERSTEFYRFLLGKEPVESSPTFASFVLSGG-AKLGLWSSEEVEPKVAVTGGgaelsFMVPSGEQVDEVYAEWKAMG 84

                         90       100
                 ....*....|....*....|....*..
gi 502821475  85 F-FARQEMDTTCCYAvqdkFWVTDPDG 110
Cdd:cd07261   85 IpIIQEPTTMDFGYT----FVATDPDG 107
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH