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Conserved domains on  [gi|582337162|gb|EVW32843|]
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glyoxalase [Staphylococcus aureus T47181]

Protein Classification

VOC family protein( domain architecture ID 11457526)

vicinal oxygen chelate (VOC) family protein uses a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms

CATH:  3.10.180.10
Gene Ontology:  GO:0046872|GO:0003824
PubMed:  21820381|11076500

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
10-132 9.07e-26

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


:

Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 98.49  E-value: 9.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582337162  10 VNGITLNVRDKNELKPFYEDILGLNIINETLTSIQYEVGQNNHVITLVELQNGRePLMSEAGLFHIAIKLPQISDLANLL 89
Cdd:COG2514    4 LGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEHLLVLEEAPGAP-PRPGAAGLDHVAFRVPSRADLDAAL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 582337162  90 IHLSEYDIPVNGGIQPA-SLSLFFEDPEGNGFKFYVDKDEAQWT 132
Cdd:COG2514   83 ARLAAAGVPVEGAVDHGvGESLYFRDPDGNLIELYTDRPRFEHV 126
VOC super family cl14632
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 169-242 5.01e-06

vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases.


The actual alignment was detected with superfamily member cd16359:

Pssm-ID: 472697  Cd Length: 110  Bit Score: 44.28  E-value: 5.01e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 582337162 169 GALHIKTIHLSEVKEYYLDYFGLE-QSAYMDdySIFLASNGYYQHLAMNDWVSATKRVENFDTYGLAIVDFHYPE 242
Cdd:cd16359    1 GHIHLRVSDLKAASHFYHQVLGFDiKSRRPG--ALFLSAGGYHHHIGLNTWAGRGLPLPPEDATGLAYFTIVLPD 73
 
Name Accession Description Interval E-value
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
10-132 9.07e-26

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 98.49  E-value: 9.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582337162  10 VNGITLNVRDKNELKPFYEDILGLNIINETLTSIQYEVGQNNHVITLVELQNGRePLMSEAGLFHIAIKLPQISDLANLL 89
Cdd:COG2514    4 LGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEHLLVLEEAPGAP-PRPGAAGLDHVAFRVPSRADLDAAL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 582337162  90 IHLSEYDIPVNGGIQPA-SLSLFFEDPEGNGFKFYVDKDEAQWT 132
Cdd:COG2514   83 ARLAAAGVPVEGAVDHGvGESLYFRDPDGNLIELYTDRPRFEHV 126
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 10-131 1.38e-25

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: 97.38  E-value: 1.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582337162  10 VNGITLNVRDKNELKPFYEDILGLNIINETLTSIQYEVGQNNHVITLVELQNGREPLMSEAGLFHIAIKLPQISDLANLL 89
Cdd:cd07255    3 IGRVTLKVADLERQSAFYQNVIGLSVLKQNASRAYLGVDGKQVLLVLEAIPDAVLAPRSTTGLYHFAILLPDRKALGRAL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 582337162  90 IHLSEYDIPVNGGIQPASLSLFFEDPEGNGFKFYVDKDEAQW 131
Cdd:cd07255   83 AHLAEHGPLIGAADHGVSEAIYLSDPEGNGIEIYADRPREQW 124
VOC_BsCatE_like_C cd16359
C-terminal of Bacillus subtilis CatE like protein, a vicinal oxygen chelate subfamily; ...
 169-242 5.01e-06

C-terminal of Bacillus subtilis CatE like protein, a vicinal oxygen chelate subfamily; Uncharacterized subfamily of vicinal oxygen chelate (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: 319966  Cd Length: 110  Bit Score: 44.28  E-value: 5.01e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 582337162 169 GALHIKTIHLSEVKEYYLDYFGLE-QSAYMDdySIFLASNGYYQHLAMNDWVSATKRVENFDTYGLAIVDFHYPE 242
Cdd:cd16359    1 GHIHLRVSDLKAASHFYHQVLGFDiKSRRPG--ALFLSAGGYHHHIGLNTWAGRGLPLPPEDATGLAYFTIVLPD 73
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
13-122 3.14e-05

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 42.44  E-value: 3.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582337162   13 ITLNVRDKNELKPFYEDILGLNIINET-------LTSIQYEVGQNNHVITLVELQNGREPLMSEAGLFHIAIKLpqiSDL 85
Cdd:pfam00903   5 VALRVGDLEKSLDFYTDVLGFKLVEETdageeggLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSV---DDV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 582337162   86 ANLLIHLSEYDIPVNGGIQPA---SLSLFFEDPEGNGFKF 122
Cdd:pfam00903  82 DAAYDRLKAAGVEIVREPGRHgwgGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
10-132 9.07e-26

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 98.49  E-value: 9.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582337162  10 VNGITLNVRDKNELKPFYEDILGLNIINETLTSIQYEVGQNNHVITLVELQNGRePLMSEAGLFHIAIKLPQISDLANLL 89
Cdd:COG2514    4 LGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEHLLVLEEAPGAP-PRPGAAGLDHVAFRVPSRADLDAAL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 582337162  90 IHLSEYDIPVNGGIQPA-SLSLFFEDPEGNGFKFYVDKDEAQWT 132
Cdd:COG2514   83 ARLAAAGVPVEGAVDHGvGESLYFRDPDGNLIELYTDRPRFEHV 126
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 10-131 1.38e-25

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: 97.38  E-value: 1.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582337162  10 VNGITLNVRDKNELKPFYEDILGLNIINETLTSIQYEVGQNNHVITLVELQNGREPLMSEAGLFHIAIKLPQISDLANLL 89
Cdd:cd07255    3 IGRVTLKVADLERQSAFYQNVIGLSVLKQNASRAYLGVDGKQVLLVLEAIPDAVLAPRSTTGLYHFAILLPDRKALGRAL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 582337162  90 IHLSEYDIPVNGGIQPASLSLFFEDPEGNGFKFYVDKDEAQW 131
Cdd:cd07255   83 AHLAEHGPLIGAADHGVSEAIYLSDPEGNGIEIYADRPREQW 124
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 10-128 4.70e-09

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


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 53.46  E-value: 4.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582337162  10 VNGITLNVRDKNELKPFYEDILGLNIINET------LTSIQYEVGqNNHVITLVELQnGREPLMSEAGLFHIAIklpQIS 83
Cdd:COG0346    3 LHHVTLRVSDLEASLAFYTDVLGLELVKRTdfgdggFGHAFLRLG-DGTELELFEAP-GAAPAPGGGGLHHLAF---RVD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 582337162  84 DLANLLIHLSEYDIPVNGGIQPASL---SLFFEDPEGNGFKFYVDKDE 128
Cdd:COG0346   78 DLDAAYARLRAAGVEIEGEPRDRAYgyrSAYFRDPDGNLIELVEPPPG 125
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 13-122 3.47e-08

vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases.


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 50.60  E-value: 3.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582337162  13 ITLNVRDKNELKPFYEDILGLNIINETLTSIQYEVGQNNHvITLVELQNGREPLMSEAGLFHIAIKLPQISDLANLLIHL 92
Cdd:cd06587    2 VALRVPDLDASVAFYEEVLGFEVVSRNEGGGFAFLRLGPG-LRLALLEGPEPERPGGGGLFHLAFEVDDVDEVDERLREA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 582337162  93 SEYDIPVNGGIQPA--SLSLFFEDPEGNGFKF 122
Cdd:cd06587   81 GAEGELVAPPVDDPwgGRSFYFRDPDGNLIEF 112
BphC2-C3-RGP6_C_like cd08348
The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus ...
 26-125 8.34e-08

The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus globerulus P6 BphC2-RGP6 and BphC3-RGP6, and similar proteins. BphC catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, yielding 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid. This is 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. Most type I extradiol dioxygenases are activated by Fe(II). Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. 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. BphC2-RGP6 and BphC3-RGP6 are one-domain dioxygenases, which form hexamers. BphC1-RGP6 has an internal duplication, it is a two-domain dioxygenase which forms octamers, its two domains do not belong to this subfamily.


Pssm-ID: 319936  Cd Length: 137  Bit Score: 50.21  E-value: 8.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582337162  26 FYEDILGLNII--NETLTSIQYevGQNNHVITLVELQNGREPLMSE---AGLFHIAIKLPQISDLANLLIHLSEYDI--- 97
Cdd:cd08348   20 WYLDILGARIVarNAKGCFLSF--DEEHHRIAIFGAPGGAQPPDKRptrVGLAHIAFTYASLDDLARNYAQLKERGIkpv 97

                         90       100
                 ....*....|....*....|....*....
gi 582337162  98 -PVNGGIqpaSLSLFFEDPEGNGFKFYVD 125
Cdd:cd08348   98 wPVNHGV---TTSIYYRDPDGNMLEMQVD 123
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 10-122 2.47e-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: 45.39  E-value: 2.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582337162  10 VNGITLNVRDKNELKPFYEDILGLnIINETLTSIQYEV-------GQNNHvitLVELQNGREPLMSEAGLF--HIAIklp 80
Cdd:cd07245    1 LDHVALACPDLERARRFYTDVLGL-EEVPRPPFLKFGGawlylggGQQIH---LVVEQNPSELPRPEHPGRdrHPSF--- 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 582337162  81 QISDLANLLIHLSEYDIP-----VNGGIQPAslsLFFEDPEGNGFKF 122
Cdd:cd07245   74 SVPDLDALKQRLKEAGIPytestSPGGGVTQ---LFFRDPDGNRLEF 117
VOC_BsCatE_like_C cd16359
C-terminal of Bacillus subtilis CatE like protein, a vicinal oxygen chelate subfamily; ...
 169-242 5.01e-06

C-terminal of Bacillus subtilis CatE like protein, a vicinal oxygen chelate subfamily; Uncharacterized subfamily of vicinal oxygen chelate (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: 319966  Cd Length: 110  Bit Score: 44.28  E-value: 5.01e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 582337162 169 GALHIKTIHLSEVKEYYLDYFGLE-QSAYMDdySIFLASNGYYQHLAMNDWVSATKRVENFDTYGLAIVDFHYPE 242
Cdd:cd16359    1 GHIHLRVSDLKAASHFYHQVLGFDiKSRRPG--ALFLSAGGYHHHIGLNTWAGRGLPLPPEDATGLAYFTIVLPD 73
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
13-122 3.14e-05

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 42.44  E-value: 3.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582337162   13 ITLNVRDKNELKPFYEDILGLNIINET-------LTSIQYEVGQNNHVITLVELQNGREPLMSEAGLFHIAIKLpqiSDL 85
Cdd:pfam00903   5 VALRVGDLEKSLDFYTDVLGFKLVEETdageeggLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSV---DDV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 582337162   86 ANLLIHLSEYDIPVNGGIQPA---SLSLFFEDPEGNGFKF 122
Cdd:pfam00903  82 DAAYDRLKAAGVEIVREPGRHgwgGRYSYFRDPDGNLIEL 121
HPCD_N_class_II cd07266
N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 15-127 1.09e-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: 37.77  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582337162  15 LNVRDKNELKPFYEDILGLNIINETLTSIQYEVGQNNHVITLVELQNgreplmSEAGLFHIAIKLPQISDLANLLIHLSE 94
Cdd:cd07266   10 LVVTDLAASREFYVDTLGLHVTDEDDNAIYLRGVEEFIHHTLVLRKA------PEAAVGHLGFRVRDEADLDKAAAFYKE 83

                         90       100       110
                 ....*....|....*....|....*....|....
gi 582337162  95 YDIPVNGGIQPA-SLSLFFEDPEGNGFKFYVDKD 127
Cdd:cd07266   84 LGLPTEWREEPGqGRTLRVEDPFGFPIEFYLEMD 117
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 15-118 2.26e-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: 36.96  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582337162  15 LNVRDKNELKPFYEDILGLNIINETLTSIQYEVGqnNHVITLVELQNGREPLMSEA-------GLFHIAIKLPQiSDLAN 87
Cdd:cd08354    6 LYADDLDAAEAFYEDVLGLKPMLRSGRHAFFRLG--PQVLLVFDPGATSKDVRTGEvpghgasGHGHFAFAVPT-EELAA 82

                         90       100       110
                 ....*....|....*....|....*....|...
gi 582337162  88 LLIHLSEYDIPVNGGIQ--PASLSLFFEDPEGN 118
Cdd:cd08354   83 WEARLEAKGVPIESYTQwpEGGKSLYFRDPAGN 115
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 13-124 2.65e-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: 36.77  E-value: 2.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582337162  13 ITLNVRDKNELKPFYEDILGLNIINETLTSIQYEVGQNNHVITLVELQNGREPLMSEAGLFHIAIKLpQISDLANLLIHL 92
Cdd:cd08345    2 ITLIVRDLEKSTAFLQDIFGAREVYSSGDKTFSLSKEKFFLLGGLWIALMEGESLQERSYTHIAFQI-QSEDFDRYAERL 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 582337162  93 SEYDI---PVNGGIQPASLSLFFEDPEGNGFKFYV 124
Cdd:cd08345   81 GALGVemrPPRPRVEGEGRSIYFYDPDNHLFELHT 115
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 14-125 3.77e-03

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: 36.14  E-value: 3.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582337162  14 TLNVRDKNELKPFYEDILGLNIINETLTSIqYEVGQNNHVITLVeLQNGREPlmseaGLFHIAIKLPQISDLANLLIHLS 93
Cdd:cd16360    3 ELGVPDLEKALEFYTDVLGLQVAKRDGNSV-YLRGYEDEHHSLV-LYEAPEA-----GLKHFAFEVASEEDLERAAASLT 75

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 582337162  94 EYDIPV----NGGIQPASLSLFFEDPEGNGFKFYVD 125
Cdd:cd16360   76 ALGCDVtwgpDGEVPGGGKGFRFQDPSGHLLELFVE 111
PpCmtC_C cd07258
C-terminal domain of 2,3-dihydroxy-p-cumate-3,4-dioxygenase (PpCmtC); This subfamily contains ...
 68-128 6.27e-03

C-terminal domain of 2,3-dihydroxy-p-cumate-3,4-dioxygenase (PpCmtC); This subfamily contains the C-terminal, catalytic, domain of PpCmtC. 2,3-dihydroxy-p-cumate-3,4-dioxygenase (CmtC of Pseudomonas putida F1) is a dioxygenase involved in the eight-step catabolism pathway of p-cymene. CmtC acts upon the reaction intermediate 2,3-dihydroxy-p-cumate, yielding 2-hydroxy-3-carboxy-6-oxo-7-methylocta-2,4-dienoate. The CmtC belongs to the type I family of extradiol dioxygenases. Fe2+ was suggested as a cofactor, same as for other enzymes in the family. The type I family of extradiol dioxygenases contains two structurally homologous barrel-shaped domains at the N- and C-terminal. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism.


Pssm-ID: 319921  Cd Length: 138  Bit Score: 36.02  E-value: 6.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 582337162  68 SEAGLFHIAIKLPQISDLANLLIHLSEYDIPV--NGGIQPASLS--LFFEDPEGNGFKFYVDKDE 128
Cdd:cd07258   50 SSSGIQHINHQVTSIDDVLRSYYRLKEHDVPIvfGPGRHPTSGArfLYFKGPDGMTFEYSVGVDE 114
 
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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