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Conserved domains on  [gi|488409610|ref|WP_002478995|]
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MULTISPECIES: VOC family protein [Staphylococcus]

Protein Classification

VOC family protein( domain architecture ID 11611485)

vicinal oxygen chelate (VOC) family protein uses a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms; similar to Actinomyces sp. 2-epi-5-epi-valiolone epimerase, which catalyzes the epimerization of 2-epi-5-epi-valiolone to 5-epi-valiolone

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 10-159 2.27e-55

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: 172.13  E-value: 2.27e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409610  10 GINHIGLTVPDIEQATTFFQTALDGKIAYDSQKLTDEPRAGQfVERVLGIEKGAKIIKKRMMVFGHGPNIEMFEFKDASQ 89
Cdd:cd16361    1 GVNHVGITVPDLDAAVEFYTDVLGAEVVYRSTPLAEGDRGGG-EMRAAGFVPGFARARIAMLRLGPGPGIELFEYKGPEQ 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488409610  90 ASAI-TLQDMGYTHISFYVDDFPAALEKVKKAGGIPLSEPHANTRYEDTPGNQTVYIQTPWGSLLELQTVP 159
Cdd:cd16361   80 RAPVpRNSDVGIFHFALQVDDVEAAAERLAAAGGKVLMGPREIPDGGPGKGNRMVYLRDPWGTLIELVSHP 150
 
Name Accession Description Interval E-value
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 10-159 2.27e-55

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: 172.13  E-value: 2.27e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409610  10 GINHIGLTVPDIEQATTFFQTALDGKIAYDSQKLTDEPRAGQfVERVLGIEKGAKIIKKRMMVFGHGPNIEMFEFKDASQ 89
Cdd:cd16361    1 GVNHVGITVPDLDAAVEFYTDVLGAEVVYRSTPLAEGDRGGG-EMRAAGFVPGFARARIAMLRLGPGPGIELFEYKGPEQ 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488409610  90 ASAI-TLQDMGYTHISFYVDDFPAALEKVKKAGGIPLSEPHANTRYEDTPGNQTVYIQTPWGSLLELQTVP 159
Cdd:cd16361   80 RAPVpRNSDVGIFHFALQVDDVEAAAERLAAAGGKVLMGPREIPDGGPGKGNRMVYLRDPWGTLIELVSHP 150
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 9-161 6.85e-19

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: 78.11  E-value: 6.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409610   9 RGINHIGLTVPDIEQATTFFQTALDGKIAYDsqkltdepragqfvervlgIEKGAKIIKKRMMVFGHGPNIEMFEFKDAS 88
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKR-------------------TDFGDGGFGHAFLRLGDGTELELFEAPGAA 61

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488409610  89 QASAITlqdmGYTHISFYVDDFPAALEKVKKAGGIPLSEPHantryEDTPGNQTVYIQTPWGSLLELQTVPQG 161
Cdd:COG0346   62 PAPGGG----GLHHLAFRVDDLDAAYARLRAAGVEIEGEPR-----DRAYGYRSAYFRDPDGNLIELVEPPPG 125
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
10-155 1.35e-08

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 50.91  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409610   10 GINHIGLTVPDIEQATTFFQTALDGKIaydsqkltdepragqfVERVLGIEKGakiiKKRMMVFGHGPN-IEMFEFKDAS 88
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKL----------------VEETDAGEEG----GLRSAFFLAGGRvLELLLNETPP 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488409610   89 qaSAITLQDMGYT-HISFYVDDFPAALEKVKKAGGIPLSEPhantryEDTPGNQTV-YIQTPWGSLLEL 155
Cdd:pfam00903  61 --PAAAGFGGHHIaFIAFSVDDVDAAYDRLKAAGVEIVREP------GRHGWGGRYsYFRDPDGNLIEL 121
PRK04101 PRK04101
metallothiol transferase FosB;
9-157 2.20e-04

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 39.54  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409610   9 RGINHIGLTVPDIEQATTFFQTALDGKIAYDSQKLTDEPRAGQFVerVLGIEKgakiikkrmmvfghgpNIEMFEFKDAs 88
Cdd:PRK04101   3 KGINHICFSVSNLEKSIEFYEKVLGAKLLVKGRKTAYFDLNGLWI--ALNEEK----------------DIPRNEIHQS- 63

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488409610  89 qasaitlqdmgYTHISFYVD--DFPAALEKVKKAGGIPLsephaNTRYEDTPGNQTVYIQTPWGSLLELQT 157
Cdd:PRK04101  64 -----------YTHIAFSIEeeDFDHWYQRLKENDVNIL-----PGRERDERDKKSIYFTDPDGHKFEFHT 118
 
Name Accession Description Interval E-value
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 10-159 2.27e-55

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: 172.13  E-value: 2.27e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409610  10 GINHIGLTVPDIEQATTFFQTALDGKIAYDSQKLTDEPRAGQfVERVLGIEKGAKIIKKRMMVFGHGPNIEMFEFKDASQ 89
Cdd:cd16361    1 GVNHVGITVPDLDAAVEFYTDVLGAEVVYRSTPLAEGDRGGG-EMRAAGFVPGFARARIAMLRLGPGPGIELFEYKGPEQ 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488409610  90 ASAI-TLQDMGYTHISFYVDDFPAALEKVKKAGGIPLSEPHANTRYEDTPGNQTVYIQTPWGSLLELQTVP 159
Cdd:cd16361   80 RAPVpRNSDVGIFHFALQVDDVEAAAERLAAAGGKVLMGPREIPDGGPGKGNRMVYLRDPWGTLIELVSHP 150
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 9-161 6.85e-19

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: 78.11  E-value: 6.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409610   9 RGINHIGLTVPDIEQATTFFQTALDGKIAYDsqkltdepragqfvervlgIEKGAKIIKKRMMVFGHGPNIEMFEFKDAS 88
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKR-------------------TDFGDGGFGHAFLRLGDGTELELFEAPGAA 61

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488409610  89 QASAITlqdmGYTHISFYVDDFPAALEKVKKAGGIPLSEPHantryEDTPGNQTVYIQTPWGSLLELQTVPQG 161
Cdd:COG0346   62 PAPGGG----GLHHLAFRVDDLDAAYARLRAAGVEIEGEPR-----DRAYGYRSAYFRDPDGNLIELVEPPPG 125
VOC_like cd08353
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 11-155 7.34e-12

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: 319941  Cd Length: 142  Bit Score: 59.90  E-value: 7.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409610  11 INHIGLTVPDIEQATTFFqTALDgkiaydsqkLTDEPRA---GQFVERVLGIEKG-AKIIkkrMMVF--GHGpNIEMFEF 84
Cdd:cd08353    4 MDHVGIVVEDLDAAIAFF-TELG---------LELEGRMtveGEWADRVVGLDGVrVEIA---MLRTpdGHG-RLELSKF 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488409610  85 ------KDASQASAITLqdmGYTHISFYVDDFPAALEKVKKAGGIPLSEPHantRYEDTpgNQTVYIQTPWGSLLEL 155
Cdd:cd08353   70 ltpaaiPGHRPAPANAL---GLRHVAFAVDDIDAVVARLRKHGAELVGEVV---QYEDS--YRLCYVRGPEGIIVEL 138
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 13-155 2.26e-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: 57.92  E-value: 2.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409610  13 HIGLTVPDIEQATTFFQTALDGKIAYdsqkltdEPRAGQFVervlgiekgakiikkrMMVFGHGPNIEMFEFKDASQASA 92
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVS-------RNEGGGFA----------------FLRLGPGLRLALLEGPEPERPGG 57

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488409610  93 ItlqdmGYTHISFYVDDFPAALEKVKKAGGIPLSEPHantRYEDTPGNQTVYIQTPWGSLLEL 155
Cdd:cd06587   58 G-----GLFHLAFEVDDVDEVDERLREAGAEGELVAP---PVDDPWGGRSFYFRDPDGNLIEF 112
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
10-155 1.35e-08

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 50.91  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409610   10 GINHIGLTVPDIEQATTFFQTALDGKIaydsqkltdepragqfVERVLGIEKGakiiKKRMMVFGHGPN-IEMFEFKDAS 88
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKL----------------VEETDAGEEG----GLRSAFFLAGGRvLELLLNETPP 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488409610   89 qaSAITLQDMGYT-HISFYVDDFPAALEKVKKAGGIPLSEPhantryEDTPGNQTV-YIQTPWGSLLEL 155
Cdd:pfam00903  61 --PAAAGFGGHHIaFIAFSVDDVDAAYDRLKAAGVEIVREP------GRHGWGGRYsYFRDPDGNLIEL 121
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 10-155 2.55e-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: 2.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409610  10 GINHIGLTVPDIEQATTFFQTALDGKIAydsqklTDEPRAGQFVervlgiekgakiikkrMMVFGHGPNIEMFEFKDASQ 89
Cdd:COG3324    4 TIVWVELPVDDLERAKAFYEEVFGWTFE------DDAGPGGDYA----------------EFDTDGGQVGGLMPGAEEPG 61

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488409610  90 AsaitlqdmGYTHISFYVDDFPAALEKVKKAGGIPLSEPHantryEDTPGNQTVYIQTPWGSLLEL 155
Cdd:COG3324   62 G--------PGWLLYFAVDDLDAAVARVEAAGGTVLRPPT-----DIPPWGRFAVFRDPEGNRFGL 114
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 11-155 3.63e-08

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: 49.88  E-value: 3.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409610  11 INHIGLTVPDIEQATTFFQTALDGKiaydsqKLTDEPRAGQFVERVLGIEKGAKIikKRMMVFGHGPNIEMFEFKDASqa 90
Cdd:cd07249    1 LDHIGIAVPDLDEALKFYEDVLGVK------VSEPEELEEQGVRVAFLELGNTQI--ELLEPLGEDSPIAKFLDKKGG-- 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488409610  91 saitlqdmGYTHISFYVDDFPAALEKVKKAGGIPLSEphanTRYEDTPGNQTVYIQTPW--GSLLEL 155
Cdd:cd07249   71 --------GLHHIAFEVDDIDAAVEELKAQGVRLLSE----GPRIGAHGKRVAFLHPKDtgGVLIEL 125
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
9-167 6.01e-06

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 43.79  E-value: 6.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409610   9 RGINHIGLTVPDIEQATTFFQTALDgkiaydsqkLTDEPRAGQFVerVLGIEkgakiikkrmmvfGHGPNIEMFEFKDAS 88
Cdd:COG2514    2 TRLGHVTLRVRDLERSAAFYTDVLG---------LEVVEREGGRV--YLRAD-------------GGEHLLVLEEAPGAP 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409610  89 QASAITlqdmGYTHISFYVD---DFPAALEKVKKAGgIPLSEPhantryEDTPGNQTVYIQTPWGSLLELQTVPQGFYYP 165
Cdd:COG2514   58 PRPGAA----GLDHVAFRVPsraDLDAALARLAAAG-VPVEGA------VDHGVGESLYFRDPDGNLIELYTDRPRFEHV 126


                 ..
gi 488409610 166 KD 167
Cdd:COG2514  127 GD 128
FosX cd08364
fosfomycin resistant protein subfamily FosX; This subfamily family contains FosX, a fosfomycin ...
 8-121 4.54e-05

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


Pssm-ID: 319952  Cd Length: 130  Bit Score: 41.49  E-value: 4.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409610   8 TRGINHIGLTVPDIEQATTFFQTALDGKIAYDSqkltdepragqfvervlgiekGAKIikkrmmvFGHGPniEMFeFKDA 87
Cdd:cd08364    1 IEGISHITFIVKDLDRTAAFLTEIFGAEEVYDS---------------------GAET-------FSLSP--EKF-FLIG 49

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 488409610  88 SQASAI----TLQDMGYTHISFYVD--DFPAALEKVKKAG 121
Cdd:cd08364   50 GLWIAImegePLLERSYNHIAFKVSegDLDEYRARIKKLG 89
PRK04101 PRK04101
metallothiol transferase FosB;
9-157 2.20e-04

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 39.54  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409610   9 RGINHIGLTVPDIEQATTFFQTALDGKIAYDSQKLTDEPRAGQFVerVLGIEKgakiikkrmmvfghgpNIEMFEFKDAs 88
Cdd:PRK04101   3 KGINHICFSVSNLEKSIEFYEKVLGAKLLVKGRKTAYFDLNGLWI--ALNEEK----------------DIPRNEIHQS- 63

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488409610  89 qasaitlqdmgYTHISFYVD--DFPAALEKVKKAGGIPLsephaNTRYEDTPGNQTVYIQTPWGSLLELQT 157
Cdd:PRK04101  64 -----------YTHIAFSIEeeDFDHWYQRLKENDVNIL-----PGRERDERDKKSIYFTDPDGHKFEFHT 118
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 45-155 1.88e-03

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


Pssm-ID: 319942  Cd Length: 122  Bit Score: 36.57  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409610  45 DEPRAGQFVERVLGIEKGAKiiKKRMMVFGHGPNIeMFEFKDASQASAITL------QDMGYTHISFYV-DDFPAALEKV 117
Cdd:cd08354   10 DLDAAEAFYEDVLGLKPMLR--SGRHAFFRLGPQV-LLVFDPGATSKDVRTgevpghGASGHGHFAFAVpTEELAAWEAR 86

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488409610 118 KKAGGIPLsephanTRYEDTP-GNQTVYIQTPWGSLLEL 155
Cdd:cd08354   87 LEAKGVPI------ESYTQWPeGGKSLYFRDPAGNLVEL 119
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 99-139 6.45e-03

N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth disturbances caused by high osmolarity and a high concentration of A-factor, a microbial hormone, during the early growth phase in Streptomyces griseus. A-factor (2-isocapryloyl-3R-hydroxymethyl-gamma-butyrolactone) controls morphological differentiation and secondary metabolism in Streptomyces griseus. It is a chemical signaling molecule that at a very low concentration acts as a switch for yellow pigment production, aerial mycelium formation, streptomycin production, and streptomycin resistance. The structure and amino acid sequence of SgaA are closely related to a group of antibiotics resistance proteins, including bleomycin resistance protein, mitomycin resistance protein, and fosfomycin resistance proteins. SgaA might also function as a streptomycin resistance protein.


Pssm-ID: 319911 [Multi-domain]  Cd Length: 114  Bit Score: 34.93  E-value: 6.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 488409610  99 GYTHISFYVDDFPAALEKVKKAGGIPLSEPHantryeDTPG 139
Cdd:cd07247   61 PGWLIYFAVDDLDAALARVEAAGGKVVVPPT------DIPG 95
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 44-157 6.66e-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: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 35.00  E-value: 6.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409610  44 TDEPRAGQFVERVLGIEKGAKIIKKRMMVFGHG-PNIEMFEFKDASQasaITLQDMGYTH--ISFYVDDFPAALEKVKKA 120
Cdd:cd07264    9 DDFAASLRFYRDVLGLPPRFLHEEGEYAEFDTGeTKLALFSRKEMAR---SGGPDRRGSAfeLGFEVDDVEATVEELVER 85

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488409610 121 GGIPLSEPHantryEDTPGNQTVYIQTPWGSLLELQT 157
Cdd:cd07264   86 GAEFVREPA-----NKPWGQTVAYVRDPDGNLIEICE 117
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 13-157 7.47e-03

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


Pssm-ID: 319931  Cd Length: 132  Bit Score: 34.98  E-value: 7.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409610  13 HIGLTVPDIEQATTFFQTALDGKIaydsqkltdepragqfVERVLGIekgakiiKKRMMVFGHGPNIE---MFEFKdasQ 89
Cdd:cd08343    2 HVVLCSPDVEASRDFYTDVLGFRV----------------SDRIVDP-------GVDGGAFLHCDRGTdhhTVALA---G 55

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488409610  90 ASAITLQdmgytHISFYVDDFpaalEKVKKAGgiplsEPHANTRYEDTPG--------NQTVYIQTPWGSLLELQT 157
Cdd:cd08343   56 GPHPGLH-----HVAFEVHDL----DDVGRGH-----DRLREKGYKIEWGpgrhglgsQVFDYWFDPSGNRVEYYT 117
 
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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