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Conserved domains on  [gi|501008664|ref|WP_012061577|]
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VOC family protein [Sinorhizobium medicae]

Protein Classification

VOC family protein( domain architecture ID 10790122)

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

PubMed:  21820381

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-126 4.73e-19

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


:

Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 76.21  E-value: 4.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664   1 MPETTVNVRYMVDDVQAAVAWYTKHLGFSVLSNHAPAfadvrrGALRLLLSGPLSSAGRpMPDGERPSPGGWnRIHLVVD 80
Cdd:COG3324    1 MPGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPG------GDYAEFDTDGGQVGGL-MPGAEEPGGPGW-LLYFAVD 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 501008664  81 DLAAEVERLRAAGVDFRNDVVT-GPGGSQILLKDPAGNFVELFQPAA 126
Cdd:COG3324   73 DLDAAVARVEAAGGTVLRPPTDiPPWGRFAVFRDPEGNRFGLWQPAA 119
 
Name Accession Description Interval E-value
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-126 4.73e-19

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 76.21  E-value: 4.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664   1 MPETTVNVRYMVDDVQAAVAWYTKHLGFSVLSNHAPAfadvrrGALRLLLSGPLSSAGRpMPDGERPSPGGWnRIHLVVD 80
Cdd:COG3324    1 MPGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPG------GDYAEFDTDGGQVGGL-MPGAEEPGGPGW-LLYFAVD 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 501008664  81 DLAAEVERLRAAGVDFRNDVVT-GPGGSQILLKDPAGNFVELFQPAA 126
Cdd:COG3324   73 DLDAAVARVEAAGGTVLRPPTDiPPWGRFAVFRDPEGNRFGLWQPAA 119
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 8-121 1.91e-16

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: 69.48  E-value: 1.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664   8 VRYMVDDVQAAVAWYTKHLGFSVLS-NHAPAFADVRRGA-LRLLLSgplssagrPMPDGERPSPGGWNRIHLVVDDLAAE 85
Cdd:cd06587    2 VALRVPDLDASVAFYEEVLGFEVVSrNEGGGFAFLRLGPgLRLALL--------EGPEPERPGGGGLFHLAFEVDDVDEV 73

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 501008664  86 VERLRAAGVDFRN---DVVTGPGGSQILLKDPAGNFVEL 121
Cdd:cd06587   74 DERLREAGAEGELvapPVDDPWGGRSFYFRDPDGNLIEF 112
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
8-121 4.59e-14

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 63.62  E-value: 4.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664    8 VRYMVDDVQAAVAWYTKHLGFSVLSNHAPAFADVRRGALRLLLSGPLSSAGRPMPDGERPSPGGWNRIHLV--VDDLAAE 85
Cdd:pfam00903   5 VALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAfsVDDVDAA 84

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 501008664   86 VERLRAAGVDFRNDVVTGP-GGSQILLKDPAGNFVEL 121
Cdd:pfam00903  85 YDRLKAAGVEIVREPGRHGwGGRYSYFRDPDGNLIEL 121
PRK11478 PRK11478
VOC family protein;
11-123 8.41e-04

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 36.80  E-value: 8.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664  11 MVDDVQAAVAWYTKHLGFSVLSNHAPAFADVRRGALRL-------LLSGPLSSAgRPmpdgERPSPGGWNRIHLVVDDLA 83
Cdd:PRK11478  13 IATDYAVSKAFYCDILGFTLQSEVYREARDSWKGDLALngqyvieLFSFPFPPE-RP----SRPEACGLRHLAFSVDDID 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 501008664  84 AEVERLRAAGVD---FRNDVVTGPGGSqiLLKDPAGNFVELFQ 123
Cdd:PRK11478  88 AAVAHLESHNVKceaIRVDPYTQKRFT--FFNDPDGLPLELYE 128
 
Name Accession Description Interval E-value
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-126 4.73e-19

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 76.21  E-value: 4.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664   1 MPETTVNVRYMVDDVQAAVAWYTKHLGFSVLSNHAPAfadvrrGALRLLLSGPLSSAGRpMPDGERPSPGGWnRIHLVVD 80
Cdd:COG3324    1 MPGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPG------GDYAEFDTDGGQVGGL-MPGAEEPGGPGW-LLYFAVD 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 501008664  81 DLAAEVERLRAAGVDFRNDVVT-GPGGSQILLKDPAGNFVELFQPAA 126
Cdd:COG3324   73 DLDAAVARVEAAGGTVLRPPTDiPPWGRFAVFRDPEGNRFGLWQPAA 119
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 8-126 2.75e-18

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: 74.64  E-value: 2.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664   8 VRYMVDDVQAAVAWYTKHLGFSVLsnHAPAFADVRRGALRLLLSGPLSSAGRPMPDGER-PSPGGWNRIHLVVDDLAAEV 86
Cdd:COG0346    6 VTLRVSDLEASLAFYTDVLGLELV--KRTDFGDGGFGHAFLRLGDGTELELFEAPGAAPaPGGGGLHHLAFRVDDLDAAY 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 501008664  87 ERLRAAGVDFRNDVVTGPGGSQIL-LKDPAGNFVELFQPAA 126
Cdd:COG0346   84 ARLRAAGVEIEGEPRDRAYGYRSAyFRDPDGNLIELVEPPP 124
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 8-121 1.91e-16

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: 69.48  E-value: 1.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664   8 VRYMVDDVQAAVAWYTKHLGFSVLS-NHAPAFADVRRGA-LRLLLSgplssagrPMPDGERPSPGGWNRIHLVVDDLAAE 85
Cdd:cd06587    2 VALRVPDLDASVAFYEEVLGFEVVSrNEGGGFAFLRLGPgLRLALL--------EGPEPERPGGGGLFHLAFEVDDVDEV 73

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 501008664  86 VERLRAAGVDFRN---DVVTGPGGSQILLKDPAGNFVEL 121
Cdd:cd06587   74 DERLREAGAEGELvapPVDDPWGGRSFYFRDPDGNLIEF 112
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
8-121 4.59e-14

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 63.62  E-value: 4.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664    8 VRYMVDDVQAAVAWYTKHLGFSVLSNHAPAFADVRRGALRLLLSGPLSSAGRPMPDGERPSPGGWNRIHLV--VDDLAAE 85
Cdd:pfam00903   5 VALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAfsVDDVDAA 84

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 501008664   86 VERLRAAGVDFRNDVVTGP-GGSQILLKDPAGNFVEL 121
Cdd:pfam00903  85 YDRLKAAGVEIVREPGRHGwGGRYSYFRDPDGNLIEL 121
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
11-124 4.99e-11

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 55.63  E-value: 4.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664  11 MVDDVQAAVAWYTKHLGFSVLSNH-----APAFADVRRGALRLLLSGPlsSAGRPMPDGERPSpggwnrIHLVVDDLAAE 85
Cdd:COG2764    7 VVDDAEEALEFYEDVFGFEVVFRMtdpdgKIMHAELRIGGSVLMLSDA--PPDSPAAEGNGVS------LSLYVDDVDAL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 501008664  86 VERLRAAGVDFRNDVVTGP-GGSQILLKDPAGNFVELFQP 124
Cdd:COG2764   79 FARLVAAGATVVMPLQDTFwGDRFGMVRDPFGVLWMINTP 118
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 12-123 6.75e-11

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


Pssm-ID: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 55.38  E-value: 6.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664  12 VDDVQAAVAWYTKHLGFSVLsnhapafADVRRGALRLLLSGP---------LSSAGRPM-PDGERPSPGGWNRIHLVVDD 81
Cdd:cd07263    6 VDDQDKALDFYVEKLGFEVV-------EDVPMGGMRWVTVAPpgspgtsllLEPKAHPAqMPQSPEAAGGTPGILLATDD 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 501008664  82 LAAEVERLRAAGVDFRNDVVTGPGGSQILLKDPAGNFVELFQ 123
Cdd:cd07263   79 IDATYERLTAAGVTFVQEPTQMGGGRVANFRDPDGNLFALME 120
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 12-121 6.99e-09

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: 50.06  E-value: 6.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664  12 VDDVQAAVAWYTKHLGFS-VLSNHAPAFADVRRGALRLLLSGplsSAGRPMPDGERPSPGGWNRIHLVV----DDLAAEV 86
Cdd:cd08354    8 ADDLDAAEAFYEDVLGLKpMLRSGRHAFFRLGPQVLLVFDPG---ATSKDVRTGEVPGHGASGHGHFAFavptEELAAWE 84

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 501008664  87 ERLRAAGVDFRNDVVTGPGGSQILLKDPAGNFVEL 121
Cdd:cd08354   85 ARLEAKGVPIESYTQWPEGGKSLYFRDPAGNLVEL 119
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-124 7.13e-09

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: 50.02  E-value: 7.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664   7 NVRYMVDDVQAAVAWYTKHLGFSVLSNHAP-AFADVRRGALRLLLSGPLSSAgRPMPDGERPSPGgwnRIHLVVDDLAAE 85
Cdd:cd07264    3 YIVLYVDDFAASLRFYRDVLGLPPRFLHEEgEYAEFDTGETKLALFSRKEMA-RSGGPDRRGSAF---ELGFEVDDVEAT 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 501008664  86 VERLRAAGVDF-RNDVVTGPGGSQILLKDPAGNFVELFQP 124
Cdd:cd07264   79 VEELVERGAEFvREPANKPWGQTVAYVRDPDGNLIEICEP 118
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 12-121 1.77e-08

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: 48.85  E-value: 1.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664  12 VDDVQAAVAWYTKHLGFSVLSNhaPAFaDVRRGA---------LRLLLSGPLSSAGRPMPDGERPSPGgwnrihLVVDDL 82
Cdd:cd07245    8 CPDLERARRFYTDVLGLEEVPR--PPF-LKFGGAwlylgggqqIHLVVEQNPSELPRPEHPGRDRHPS------FSVPDL 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 501008664  83 AAEVERLRAAGVDFRNDVVTGPGGSQILLKDPAGNFVEL 121
Cdd:cd07245   79 DALKQRLKEAGIPYTESTSPGGGVTQLFFRDPDGNRLEF 117
VOC_like cd08359
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 11-123 5.22e-08

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


Pssm-ID: 319947 [Multi-domain]  Cd Length: 119  Bit Score: 47.78  E-value: 5.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664  11 MVDDVQAAVAWYTKHLGFSVLSNhAPAFADVRRGALRLLLSGPLSSAGRPMPDGERPSPGGwNRIHLVVDDLAAEVERLR 90
Cdd:cd08359    8 VTEDVAATAAFYVKHFGFRVIFD-SDWYVSLRRAERHGFELAIMDGQHGAVPAASQTQSSG-LIINFEVDDADAEYERLT 85

                         90       100       110
                 ....*....|....*....|....*....|....
gi 501008664  91 AAGVDFRNDVVTGPGGSQ-ILLKDPAGNFVELFQ 123
Cdd:cd08359   86 QAGLEFLEPPRDEPWGQRrFIVRDPNGVLIDVIQ 119
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
12-127 6.58e-08

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 48.03  E-value: 6.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664  12 VDDVQAAVAWYTKHLGFSVLSNHAPAFADVRRGALRLLLsgpLSSAGRPMPdgeRPSPGGWNRIHLVVD---DLAAEVER 88
Cdd:COG2514   11 VRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEHLLV---LEEAPGAPP---RPGAAGLDHVAFRVPsraDLDAALAR 84

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 501008664  89 LRAAGVDFRNDVVTGPGGSqILLKDPAGNFVELFQPAAR 127
Cdd:COG2514   85 LAAAGVPVEGAVDHGVGES-LYFRDPDGNLIELYTDRPR 122
Glyoxalase_6 pfam18029
Glyoxalase-like domain; This entry comprises a diverse set of domains related to the ...
 12-117 1.11e-07

Glyoxalase-like domain; This entry comprises a diverse set of domains related to the Glyoxalase domain. The exact specificity of these proteins is uncertain.


Pssm-ID: 436220  Cd Length: 110  Bit Score: 46.60  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664   12 VDDVQAAVAWYTKHLGFSVlsnHAPAFADVRRGALRLLLSGPLSSAGRPMPDGERpspgGWNRIHL--VVDDLAAEVERL 89
Cdd:pfam18029   6 CADPAALAAFWSAALGWEV---VPDDTALPDPDGGGPIGGGGPRLLFQRVPEPKP----GKNRVHLdlAVDDLEAAVARL 78

                          90       100
                  ....*....|....*....|....*...
gi 501008664   90 RAAGVDfRNDVVTGPGGSQILLKDPAGN 117
Cdd:pfam18029  79 VALGAT-VLDDGDDPDGGRWVLADPEGN 105
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 12-123 1.23e-07

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: 46.45  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664  12 VDDVQAAVAWYTKHLGFSVLSNH-APAFADVRRGALRLLLSGplssagrpMPDGERPSPGGwnRIHLVVDDLAAEVERLR 90
Cdd:cd08349    6 VRDIDKTLAFYVDVLGFEVDYERpPPGYAILSRGGVELHLFE--------HPGLDPAGSGV--AAYIRVEDIDALHAELK 75

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 501008664  91 AAGVD-FRNDVVTGP-----GGSQILLKDPAGNFVELFQ 123
Cdd:cd08349   76 AAGLPlFGIPRITPIedkpwGMREFAVVDPDGNLLRFGQ 114
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
10-96 2.96e-06

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 43.04  E-value: 2.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664   10 YMVDDVQAAVAWYTKHLGFSVL-------SNHAPAFADVRRGALRLLLSGPLSsaGRPMPDgerPSPGGWNRIHLVVDDL 82
Cdd:pfam13669   5 IAVPDLDRALALWGALLGLGPEgdyrsepQNVDLAFALLGDGPVEVELIQPLD--GDSPLA---RHGPGLHHLAYWVDDL 79

                          90
                  ....*....|....
gi 501008664   83 AAEVERLRAAGVDF 96
Cdd:pfam13669  80 DAAVARLLDQGYRV 93
VOC_like cd07246
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 4-124 3.74e-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: 319910 [Multi-domain]  Cd Length: 124  Bit Score: 43.05  E-value: 3.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664   4 TTVNVRYMVDDVQAAVAWYTKHLGFSVLSNH-----APAFADVRRGALRLLLSGPLSSAGRPMPDGERPSPGGwnrIHLV 78
Cdd:cd07246    1 TTVSPYLVVEDAAAAIAFYKKAFGAEELGRTtqedgRVGHAELRIGGTVVMVADENPERGALSPTKLGGTPVI---FHLY 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 501008664  79 VDDLAAEVERLRAAGVDFRNDVVTGPGGSQI-LLKDPAGNFVELFQP 124
Cdd:cd07246   78 VEDVDATFARAVAAGAVVVEPVEDQFWGDRVgKVKDPFGHVWWLATP 124
TioX_like cd08355
Micromonospora sp. TioX and similar proteins; Micromonospora sp. TioX is encoded by a gene of ...
 14-117 8.62e-06

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


Pssm-ID: 319943  Cd Length: 123  Bit Score: 42.02  E-value: 8.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664  14 DVQAAVAWYTKHLGFSVLSNHAPAFADVRRGALRLLLSGPLSSAGRPMPDGERP---SPGGWNRIHLVVDDLAAEVERLR 90
Cdd:cd08355    9 DAVAAIDWLVEAFGFEERMVVPGDEGTIHHAELTFGGGGVMVGSVRDEARPDRPadaGGHGTQSVYVAVADPDAHYERAR 88

                         90       100
                 ....*....|....*....|....*...
gi 501008664  91 AAGVDFRNDVVTGP-GGSQILLKDPAGN 117
Cdd:cd08355   89 AAGAEIVMEPTDTDyGSRDYSARDPEGH 116
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 11-123 2.47e-05

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: 40.71  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664  11 MVDDVQAAVAWYTKHLG--FSVLSNHAPAFADVRRGalrlllsGPLSSAGRPMPDGERPSPGGWnRIHLVVDDLAAEVER 88
Cdd:cd07247    7 PTTDLERAKAFYGAVFGwtFEDEGDGGGDYALFTAG-------GGAVGGLMRAPEEVAGAPPGW-LIYFAVDDLDAALAR 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 501008664  89 LRAAGvdfrNDVVTGP-----GGSQILLKDPAGNFVELFQ 123
Cdd:cd07247   79 VEAAG----GKVVVPPtdipgGGRFAVFADPEGNRFGLWS 114
VOC_like cd16355
uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily; The vicinal oxygen ...
 12-97 1.15e-04

uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily; 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: 319962  Cd Length: 121  Bit Score: 39.01  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664  12 VDDVQAAVAWYTKHLGFS--VLSNHAPAFADVRRGALRLLLS-GPLSSAGRPMPDG-ERPSPGGWnrIHLVVDDLAAEVE 87
Cdd:cd16355    7 VSDIPASFAWFEKVLGFQkdWDWGDPPTFGSVGSGECEIFLCqGGQGGSLRLGPCGdALPSYGAW--MSVWVDDVDALHR 84

                         90
                 ....*....|
gi 501008664  88 RLRAAGVDFR 97
Cdd:cd16355   85 ECRARGADIR 94
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 5-123 1.45e-04

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: 39.24  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664   5 TVN-VRYMVDDVQAAVAWYTKHLGFSVL-------------SNHAPAFADVRRGALR--LLLSGP-----LSSAGRPM-- 61
Cdd:cd16361    1 GVNhVGITVPDLDAAVEFYTDVLGAEVVyrstplaegdrggGEMRAAGFVPGFARARiaMLRLGPgpgieLFEYKGPEqr 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501008664  62 PDGERPSPGGWNRIHLVVDDLAAEVERLRAAG------VDFRNDVVTGPGGSQILLKDPAGNFVELFQ 123
Cdd:cd16361   81 APVPRNSDVGIFHFALQVDDVEAAAERLAAAGgkvlmgPREIPDGGPGKGNRMVYLRDPWGTLIELVS 148
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 5-96 1.88e-04

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: 39.49  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664   5 TVNVRYmvDDVQAAVAWYTKHLGFSVLS---NHAP------AFADVRRGALRLLLSGPLSsagrpmPDG-------ERPS 68
Cdd:COG3185  151 GIAVPR--GDLDEWVLFYEDVLGFEEIReedIEDPyqgvrsAVLQSPDGKVRIPLNEPTS------PDSqiaefleKYRG 222

                         90       100       110
                 ....*....|....*....|....*....|.
gi 501008664  69 PGgwnrIH---LVVDDLAAEVERLRAAGVDF 96
Cdd:COG3185  223 EG----IQhiaFATDDIEATVAALRARGVRF 249
PRK11478 PRK11478
VOC family protein;
11-123 8.41e-04

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 36.80  E-value: 8.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664  11 MVDDVQAAVAWYTKHLGFSVLSNHAPAFADVRRGALRL-------LLSGPLSSAgRPmpdgERPSPGGWNRIHLVVDDLA 83
Cdd:PRK11478  13 IATDYAVSKAFYCDILGFTLQSEVYREARDSWKGDLALngqyvieLFSFPFPPE-RP----SRPEACGLRHLAFSVDDID 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 501008664  84 AEVERLRAAGVD---FRNDVVTGPGGSqiLLKDPAGNFVELFQ 123
Cdd:PRK11478  88 AAVAHLESHNVKceaIRVDPYTQKRFT--FFNDPDGLPLELYE 128
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 10-123 1.16e-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: 36.40  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664  10 YMVDDVQAAVAWYTKHLGFSVLSN-----HAPAFADVRRGALRLLLSGPLSSAGRPMPDGERPSPGgwnrIH---LVVDD 81
Cdd:cd07249    6 IAVPDLDEALKFYEDVLGVKVSEPeeleeQGVRVAFLELGNTQIELLEPLGEDSPIAKFLDKKGGG----LHhiaFEVDD 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 501008664  82 LAAEVERLRAAGVDFRND-VVTGPGGSQILLKDPAGNF---VELFQ 123
Cdd:cd07249   82 IDAAVEELKAQGVRLLSEgPRIGAHGKRVAFLHPKDTGgvlIELVE 127
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 12-121 1.35e-03

Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily of VOC family contains human glyoxalase domain-containing protein 5 and similar proteins. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319916 [Multi-domain]  Cd Length: 123  Bit Score: 36.05  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664  12 VDDVQAAVAWYTKHLGFSVLSNHAPafadvrRGALRLllsGP----LSSAGRPM-PDGERPSPGgwnRIHL---VVDDLA 83
Cdd:cd07253   11 VKDIERTIDFYTKVLGMTVVTFKEG------RKALRF---GNqkinLHQKGKEFePKASAPTPG---SADLcfiTETPID 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 501008664  84 AEVERLRAAGVDFRNDVV-----TGPGGSqILLKDPAGNFVEL 121
Cdd:cd07253   79 EVLEHLEACGVTIEEGPVkrtgaLGPILS-IYFRDPDGNLIEL 120
PLN02367 PLN02367
lactoylglutathione lyase
 69-122 1.68e-03

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 36.52  E-value: 1.68e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 501008664  69 PGGWNRIHLVVDDLAAEVERLRAAGVDFRNDVVTGPGGSQILLKDPAGNFVELF 122
Cdd:PLN02367 167 PRGFGHIGITVDDVYKACERFEELGVEFVKKPNDGKMKGIAFIKDPDGYWIEIF 220
HPPD_C_like cd07250
C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate synthase ...
 13-96 9.45e-03

C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate synthase (HmaS); HppD and HmaS are non-heme iron-dependent dioxygenases, which modify a common substrate, 4-hydroxyphenylpyruvate (HPP), but yield different products. HPPD catalyzes the second reaction in tyrosine catabolism, the conversion of 4-hydroxyphenylpyruvate to homogentisate (2,5-dihydroxyphenylacetic acid, HG). HmaS converts HPP to 4-hydroxymandelate, a committed step in the formation of hydroxyphenylglycerine, a structural component of nonproteinogenic macrocyclic peptide antibiotics, such as vancomycin. If the emphasis is on catalytic chemistry, HPPD and HmaS are classified as members of a large family of alpha-keto acid dependent mononuclear non-heme iron oxygenases most of which require Fe(II), molecular oxygen, and an alpha-keto acid (typically alpha-ketoglutarate) to either oxygenate or oxidize a third substrate. Both enzymes are exceptions in that they require two, instead of three, substrates, do not use alpha-ketoglutarate, and incorporate both atoms of dioxygen into the aromatic product. Both HPPD and HmaS exhibit duplicate beta barrel topology in their N- and C-terminal domains which share sequence similarity, suggestive of a gene duplication. Each protein has only one catalytic site located in at the C-terminal domain. This HPPD_C_like domain represents the C-terminal domain.


Pssm-ID: 319913  Cd Length: 194  Bit Score: 34.45  E-value: 9.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501008664  13 DDVQAAVAWYTKHLGFSVL-SNHAPAFADVRRG-----------ALRLLLSGPLSSAGRPMPD-------GErpspgGWN 73
Cdd:cd07250   14 GEMDPAVEWYEKCLGFHRFwEFDDEDIGTEYSGlrsivlanpneTIKLPLNEPAPGKRKSQIQefldyhgGA-----GVQ 88

                         90       100
                 ....*....|....*....|...
gi 501008664  74 RIHLVVDDLAAEVERLRAAGVDF 96
Cdd:cd07250   89 HIALNTDDIFATVRALRARGVEF 111
 
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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