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Conserved domains on  [gi|188035928|ref|NP_115990|]
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methylmalonyl-CoA epimerase, mitochondrial precursor [Homo sapiens]

Protein Classification

methylmalonyl-CoA epimerase( domain architecture ID 10798993)

methylmalonyl-CoA epimerase is a vicinal oxygen chelate (VOC) family protein that catalyzes the interconversion of (2R)-methylmalonyl-CoA and (2S)-methylmalonyl-CoA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
 47-175 7.73e-76

methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA epimerase (EC 5.1.99.1), also called methylmalonyl-CoA racemase. This enzyme converts (2R)-methylmalonyl-CoA to (2S)-methylmalonyl-CoA, which is then a substrate for methylmalonyl-CoA mutase (TIGR00642). It is known in bacteria, archaea, and as a mitochondrial protein in animals. It is closely related to lactoylglutathione lyase (TIGR00068), which is also called glyoxylase I, and is also a homodimer.


:

Pssm-ID: 213772 [Multi-domain]  Cd Length: 128  Bit Score: 222.59  E-value: 7.73e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928   47 RLNHVAIAVPDLEKAAAFYKNILGAQVSEAVPLPEHGVSVVFVNLGNTKMELLHPLGRDSPIAGFLQKNkAGGMHHICIE 126
Cdd:TIGR03081   1 RIDHVGIAVPDLEEAAKFYEDVLGAQVSEIEELPEQGVKVVFIALGNTKVELLEPLGEDSPIAKFLEKN-GGGIHHIAIE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 188035928  127 VDNINAAVMDLKKKKIRSLSEEVKIGAHGKPVIFLHPKDCGGVLVELEQ 175
Cdd:TIGR03081  80 VDDIEAALETLKEKGVRLIDEEPRIGAHGKPVAFLHPKSTGGVLIELEQ 128
 
Name Accession Description Interval E-value
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
 47-175 7.73e-76

methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA epimerase (EC 5.1.99.1), also called methylmalonyl-CoA racemase. This enzyme converts (2R)-methylmalonyl-CoA to (2S)-methylmalonyl-CoA, which is then a substrate for methylmalonyl-CoA mutase (TIGR00642). It is known in bacteria, archaea, and as a mitochondrial protein in animals. It is closely related to lactoylglutathione lyase (TIGR00068), which is also called glyoxylase I, and is also a homodimer.


Pssm-ID: 213772 [Multi-domain]  Cd Length: 128  Bit Score: 222.59  E-value: 7.73e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928   47 RLNHVAIAVPDLEKAAAFYKNILGAQVSEAVPLPEHGVSVVFVNLGNTKMELLHPLGRDSPIAGFLQKNkAGGMHHICIE 126
Cdd:TIGR03081   1 RIDHVGIAVPDLEEAAKFYEDVLGAQVSEIEELPEQGVKVVFIALGNTKVELLEPLGEDSPIAKFLEKN-GGGIHHIAIE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 188035928  127 VDNINAAVMDLKKKKIRSLSEEVKIGAHGKPVIFLHPKDCGGVLVELEQ 175
Cdd:TIGR03081  80 VDDIEAALETLKEKGVRLIDEEPRIGAHGKPVAFLHPKSTGGVLIELEQ 128
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 48-175 3.10e-66

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: 198.18  E-value: 3.10e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  48 LNHVAIAVPDLEKAAAFYKNILGAQVSEAVPLPEHGVSVVFVNLGNTKMELLHPLGRDSPIAGFLqKNKAGGMHHICIEV 127
Cdd:cd07249    1 LDHIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELGNTQIELLEPLGEDSPIAKFL-DKKGGGLHHIAFEV 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 188035928 128 DNINAAVMDLKKKKIRSLSEEVKIGAHGKPVIFLHPKDCGGVLVELEQ 175
Cdd:cd07249   80 DDIDAAVEELKAQGVRLLSEGPRIGAHGKRVAFLHPKDTGGVLIELVE 127
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 45-173 3.06e-34

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: 122.69  E-value: 3.06e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  45 LGRLNHVAIAVP--DLEKAAAFYKNILGAQV--SEAVPLPEHGV-SVVFVNL-GNTKMELLHPLGRDSPIAGFLQKNKAG 118
Cdd:COG3185  144 LTRIDHIGIAVPrgDLDEWVLFYEDVLGFEEirEEDIEDPYQGVrSAVLQSPdGKVRIPLNEPTSPDSQIAEFLEKYRGE 223

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 188035928 119 GMHHICIEVDNINAAVMDLKKKKIRSLSE--------EVKIGAHGKPVIFLHPK------DCGGVLVEL 173
Cdd:COG3185  224 GIQHIAFATDDIEATVAALRARGVRFLDIpdnyyddlEPRVGAHGEDVAFLHPKgilvdrDTGGVLLQI 292
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
49-160 2.63e-25

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 93.88  E-value: 2.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928   49 NHVAIAVPDLEKAAAFYKNILGAQVSEAVPLPEHGVSVVFVNLGNTKM--ELLHPLGRDSPIAgflqkNKAGGMHHICIE 126
Cdd:pfam13669   1 HHVGIAVPDLDRALALWGALLGLGPEGDYRSEPQNVDLAFALLGDGPVevELIQPLDGDSPLA-----RHGPGLHHLAYW 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 188035928  127 VDNINAAVMDLKKKKIRSLSEEVKIGAHGKPVIF 160
Cdd:pfam13669  76 VDDLDAAVARLLDQGYRVAPKGPRAGAAGRRVAF 109
PLN02875 PLN02875
4-hydroxyphenylpyruvate dioxygenase
 28-140 1.54e-05

4-hydroxyphenylpyruvate dioxygenase


Pssm-ID: 215472 [Multi-domain]  Cd Length: 398  Bit Score: 43.90  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  28 ASSTSQPLDqvtgsvWNLGRLNHVAIAVPDLEKAAAFYKNILG----AQVS-EAVPLPEHGV-SVVFVNlgNTKMELL-- 99
Cdd:PLN02875 167 ESSSSFPLD------YGLRRLDHAVGNVPNLLPAVNYIAGFTGfhefAEFTaEDVGTVDSGLnSMVLAS--NNEMVLLpl 238

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 188035928 100 ----HPLGRDSPIAGFLQKNKAGGMHHICIEVDNINAAVMDLKKK 140
Cdd:PLN02875 239 neptFGTKRKSQIQTYLEHNEGPGLQHLALKSDDIFGTLREMRAR 283
 
Name Accession Description Interval E-value
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
 47-175 7.73e-76

methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA epimerase (EC 5.1.99.1), also called methylmalonyl-CoA racemase. This enzyme converts (2R)-methylmalonyl-CoA to (2S)-methylmalonyl-CoA, which is then a substrate for methylmalonyl-CoA mutase (TIGR00642). It is known in bacteria, archaea, and as a mitochondrial protein in animals. It is closely related to lactoylglutathione lyase (TIGR00068), which is also called glyoxylase I, and is also a homodimer.


Pssm-ID: 213772 [Multi-domain]  Cd Length: 128  Bit Score: 222.59  E-value: 7.73e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928   47 RLNHVAIAVPDLEKAAAFYKNILGAQVSEAVPLPEHGVSVVFVNLGNTKMELLHPLGRDSPIAGFLQKNkAGGMHHICIE 126
Cdd:TIGR03081   1 RIDHVGIAVPDLEEAAKFYEDVLGAQVSEIEELPEQGVKVVFIALGNTKVELLEPLGEDSPIAKFLEKN-GGGIHHIAIE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 188035928  127 VDNINAAVMDLKKKKIRSLSEEVKIGAHGKPVIFLHPKDCGGVLVELEQ 175
Cdd:TIGR03081  80 VDDIEAALETLKEKGVRLIDEEPRIGAHGKPVAFLHPKSTGGVLIELEQ 128
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 48-175 3.10e-66

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: 198.18  E-value: 3.10e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  48 LNHVAIAVPDLEKAAAFYKNILGAQVSEAVPLPEHGVSVVFVNLGNTKMELLHPLGRDSPIAGFLqKNKAGGMHHICIEV 127
Cdd:cd07249    1 LDHIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELGNTQIELLEPLGEDSPIAKFL-DKKGGGLHHIAFEV 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 188035928 128 DNINAAVMDLKKKKIRSLSEEVKIGAHGKPVIFLHPKDCGGVLVELEQ 175
Cdd:cd07249   80 DDIDAAVEELKAQGVRLLSEGPRIGAHGKRVAFLHPKDTGGVLIELVE 127
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 45-173 3.06e-34

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: 122.69  E-value: 3.06e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  45 LGRLNHVAIAVP--DLEKAAAFYKNILGAQV--SEAVPLPEHGV-SVVFVNL-GNTKMELLHPLGRDSPIAGFLQKNKAG 118
Cdd:COG3185  144 LTRIDHIGIAVPrgDLDEWVLFYEDVLGFEEirEEDIEDPYQGVrSAVLQSPdGKVRIPLNEPTSPDSQIAEFLEKYRGE 223

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 188035928 119 GMHHICIEVDNINAAVMDLKKKKIRSLSE--------EVKIGAHGKPVIFLHPK------DCGGVLVEL 173
Cdd:COG3185  224 GIQHIAFATDDIEATVAALRARGVRFLDIpdnyyddlEPRVGAHGEDVAFLHPKgilvdrDTGGVLLQI 292
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 47-173 4.02e-28

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: 101.61  E-value: 4.02e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  47 RLNHVAIAVPDLEKAAAFYKNILGAQVSEAVPLPEHGVSVVFVNLGN-TKMELLHPLGrDSPIAGflqknkAGGMHHICI 125
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDgTELELFEAPG-AAPAPG------GGGLHHLAF 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 188035928 126 EVDNINAAVMDLKKKKIRsLSEEVKIGAHGKPVIFLhpKDCGGVLVEL 173
Cdd:COG0346   75 RVDDLDAAYARLRAAGVE-IEGEPRDRAYGYRSAYF--RDPDGNLIEL 119
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
49-160 2.63e-25

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 93.88  E-value: 2.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928   49 NHVAIAVPDLEKAAAFYKNILGAQVSEAVPLPEHGVSVVFVNLGNTKM--ELLHPLGRDSPIAgflqkNKAGGMHHICIE 126
Cdd:pfam13669   1 HHVGIAVPDLDRALALWGALLGLGPEGDYRSEPQNVDLAFALLGDGPVevELIQPLDGDSPLA-----RHGPGLHHLAYW 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 188035928  127 VDNINAAVMDLKKKKIRSLSEEVKIGAHGKPVIF 160
Cdd:pfam13669  76 VDDLDAAVARLLDQGYRVAPKGPRAGAAGRRVAF 109
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
47-173 6.50e-19

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 77.87  E-value: 6.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928   47 RLNHVAIAVPDLEKAAAFYKNILGAQVSEAVPLPEH-GVSVVFVNLGNTKMELLHPLGRDSPIAGFlqknKAGGMHHICI 125
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEgGLRSAFFLAGGRVLELLLNETPPPAAAGF----GGHHIAFIAF 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 188035928  126 EVDNINAAVMDLKKKKIRSLSEevkIGAHGKPVIFLHPKDCGGVLVEL 173
Cdd:pfam00903  77 SVDDVDAAYDRLKAAGVEIVRE---PGRHGWGGRYSYFRDPDGNLIEL 121
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 50-173 1.02e-13

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: 64.08  E-value: 1.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  50 HVAIAVPDLEKAAAFYKNILGAQVseaVPLPEHGVSVVFVNLGNTKMELLHPLGRdspiagflQKNKAGGMHHICIEVDN 129
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEV---VSRNEGGGFAFLRLGPGLRLALLEGPEP--------ERPGGGGLFHLAFEVDD 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 188035928 130 INAAVMDLKKKKIR-SLSEEVKIGAHGKPVIFLHpkDCGGVLVEL 173
Cdd:cd06587   70 VDEVDERLREAGAEgELVAPPVDDPWGGRSFYFR--DPDGNLIEF 112
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 48-173 4.16e-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: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 59.64  E-value: 4.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  48 LNHVAIAVPDLEKAAAFYKNILGAqvsEAVPLPEHGV-SVVFVNLGNTKMelLHpLGRDSPIAGFLQKNKAGGMHHICIE 126
Cdd:cd07245    1 LDHVALACPDLERARRFYTDVLGL---EEVPRPPFLKfGGAWLYLGGGQQ--IH-LVVEQNPSELPRPEHPGRDRHPSFS 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 188035928 127 VDNINAAVMDLKKKKI---RSLSEEVKIGAhgkpvIFLHpkDCGGVLVEL 173
Cdd:cd07245   75 VPDLDALKQRLKEAGIpytESTSPGGGVTQ-----LFFR--DPDGNRLEF 117
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 46-173 2.20e-10

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 55.41  E-value: 2.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  46 GRLNHVAIAVPDLEKAAAFYKNILGAQVSEAVPLPEHgvsVVFVNLGNTKMELLHPLGRDSPIAGFlqknkaggmhHICI 125
Cdd:COG3324    3 GTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPGGD---YAEFDTDGGQVGGLMPGAEEPGGPGW----------LLYF 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 188035928 126 EVDNINAAVMDLKKKKIRSLSEEVKIGAHGKPVIFlhpKDCGGVLVEL 173
Cdd:COG3324   70 AVDDLDAAVARVEAAGGTVLRPPTDIPPWGRFAVF---RDPEGNRFGL 114
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
47-132 1.49e-09

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 53.42  E-value: 1.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  47 RLNHVAIAVPDLEKAAAFYKNILGAQVSEavplpEHGVSVVFVNLGNTKMELLHPLGRDSPIAGflqknkAGGMHHICIE 126
Cdd:COG2514    3 RLGHVTLRVRDLERSAAFYTDVLGLEVVE-----REGGRVYLRADGGEHLLVLEEAPGAPPRPG------AAGLDHVAFR 71


                 ....*.
gi 188035928 127 VDNINA 132
Cdd:COG2514   72 VPSRAD 77
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 47-173 2.37e-09

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


Pssm-ID: 319940 [Multi-domain]  Cd Length: 123  Bit Score: 52.55  E-value: 2.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  47 RLNHVAIAVPDLEKAAAFYKNILGAQVSEAVPLPEHGVSVVFVNLGNTKMELlhplgrdspiagFLQKN--------KAG 118
Cdd:cd08352    2 KIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDIKLDLALGGYQLEL------------FIKPDaparpsypEAL 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 188035928 119 GMHHICIEVDNINAAVMDLKKKKIRslSEEVKIGAH-GKPVIFLhpKDCGGVLVEL 173
Cdd:cd08352   70 GLRHLAFKVEDVEATVAELKSLGIE--TEPIRVDDFtGKKFTFF--FDPDGLPLEL 121
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 47-174 1.17e-08

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: 50.69  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  47 RLNHVAIAVPDLEKAAAFYKNILGAQVSEAVPLPEHgvsvvfVNLGNTKMElLHPLGRDspiagFLQKNKAG--GMHHIC 124
Cdd:cd07253    3 RLDHLVLTVKDIERTIDFYTKVLGMTVVTFKEGRKA------LRFGNQKIN-LHQKGKE-----FEPKASAPtpGSADLC 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 188035928 125 IEVD-NINAAVMDLKKKKIRSLSEEVK-IGAHGkPVIFLHPKDCGGVLVELE 174
Cdd:cd07253   71 FITEtPIDEVLEHLEACGVTIEEGPVKrTGALG-PILSIYFRDPDGNLIELS 121
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 47-134 1.51e-08

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: 51.18  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  47 RLNHVAIAVPDLEKAAAFYKNILGAQV---SEAVPLPEHGVSV----VFVN-----------LGN-TKMELLHPLGRDSP 107
Cdd:cd16361    1 GVNHVGITVPDLDAAVEFYTDVLGAEVvyrSTPLAEGDRGGGEmraaGFVPgfarariamlrLGPgPGIELFEYKGPEQR 80

                         90       100
                 ....*....|....*....|....*..
gi 188035928 108 IAGFlqKNKAGGMHHICIEVDNINAAV 134
Cdd:cd16361   81 APVP--RNSDVGIFHFALQVDDVEAAA 105
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 50-173 2.13e-08

Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other prokaryotic glyoxalase I that uses nickel as cofactor. Glyoxalase I (also known as lactoylglutathione lyase; EC 4.4.1.5) is part of the glyoxalase system, a two-step system for detoxifying methylglyoxal, a side product of glycolysis. This system is responsible for the conversion of reactive, acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids and involves 2 enzymes, glyoxalase I and II. Glyoxalase I catalyses an intramolecular redox reaction of the hemithioacetal (formed from methylglyoxal and glutathione) to form the thioester, S-D-lactoylglutathione. This reaction involves the transfer of two hydrogen atoms from C1 to C2 of the methylglyoxal, and proceeds via an ene-diol intermediate. Glyoxalase I has a requirement for bound metal ions for catalysis. Eukaryotic glyoxalase I prefers the divalent cation zinc as cofactor, whereas Escherichia coil and other prokaryotic glyoxalase I uses nickel. However, eukaryotic Trypanosomatid parasites also use nickel as a cofactor, which could possibly be explained by acquiring their GLOI gene by horizontal gene transfer. Human glyoxalase I is a two-domain enzyme and it has the structure of a domain-swapped dimer with two active sites located at the dimer interface. In yeast, in various plants, insects and Plasmodia, glyoxalase I is four-domain, possibly the result of a further gene duplication and an additional gene fusing event.


Pssm-ID: 319965 [Multi-domain]  Cd Length: 122  Bit Score: 50.09  E-value: 2.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  50 HVAIAVPDLEKAAAFYKNILGAQVSEAVPLPEHGVSVVFVNLG----NTKMELLHPLGRDSpiagflqKNKAGGMHHICI 125
Cdd:cd16358    3 HTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYGdedeNTVLELTYNWGVDK-------YDLGTAYGHIAI 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 188035928 126 EVDNINAAVMDLKKK--KIRSLSEEVKigaHGKPVI-FLHPKDcgGVLVEL 173
Cdd:cd16358   76 GVEDVYETCERIRKKggKVTREPGPMK---GGTTVIaFVEDPD--GYKIEL 121
BphC1-RGP6_C_like cd07237
C-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase; This subfamily contains the ...
 38-131 9.66e-08

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


Pssm-ID: 319902  Cd Length: 153  Bit Score: 48.81  E-value: 9.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  38 VTGsvwNLGrLNHVAIAVPDLEKAAAFYKNILGAQVSEAV---PLPEHGVSVVFvnlgntkmelLHPLGRDSPIAgFLQK 114
Cdd:cd07237    4 VTG---DQG-LGHVVLIVPDVDEALAFYTDVLGFRLSDEIripLPPGVTARLHF----------LHCNGRHHSLA-FGAG 68

                         90
                 ....*....|....*..
gi 188035928 115 NKAGGMHHICIEVDNIN 131
Cdd:cd07237   69 PGPKRLHHLMLEVTSLD 85
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 50-173 3.40e-07

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: 46.93  E-value: 3.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  50 HVAIAVPDLEKAAAFYKNILGAQVSEAVPLPEHGVsVVFVNLGNTkmELLHPLgrdspiagFLQKNKAGGMHHICIEVDN 129
Cdd:cd08343    2 HVVLCSPDVEASRDFYTDVLGFRVSDRIVDPGVDG-GAFLHCDRG--TDHHTV--------ALAGGPHPGLHHVAFEVHD 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 188035928 130 INAAVMD---LKKKKIRSlseEVKIGAHGKPV-IFLHPKDCGGVLVEL 173
Cdd:cd08343   71 LDDVGRGhdrLREKGYKI---EWGPGRHGLGSqVFDYWFDPSGNRVEY 115
Glyoxalase_3 pfam13468
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 48-139 4.08e-07

Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.


Pssm-ID: 433233  Cd Length: 175  Bit Score: 47.72  E-value: 4.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928   48 LNHVAIAVPDLEKAAAFYKNILGAQVSEAVPLPEHGVSVVFVNLGNTKMELLHP----LGRDSPIAGFLQK-NKAGGMHH 122
Cdd:pfam13468   1 LDHVVLAVPDLDEAAARFARALGFTVTPGGRHPGMGTANALIMFGDGYLELLAVdpeaPAPPRGRWFGLDRlADGEGLLG 80

                          90
                  ....*....|....*..
gi 188035928  123 ICIEVDNINAAVMDLKK 139
Cdd:pfam13468  81 WALRTDDIDAVAARLRA 97
HPPD_C_like cd07250
C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate synthase ...
 45-139 6.18e-06

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: 44.47  E-value: 6.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  45 LGRLNHVAIAVPD--LEKAAAFYKNILG----AQVSEAVPLPEHGV--SVVFVN-LGNTKMELLHPL--GRDSPIAGFLQ 113
Cdd:cd07250    1 LTRIDHVVGNVPDgeMDPAVEWYEKCLGfhrfWEFDDEDIGTEYSGlrSIVLANpNETIKLPLNEPApgKRKSQIQEFLD 80

                         90       100
                 ....*....|....*....|....*.
gi 188035928 114 KNKAGGMHHICIEVDNINAAVMDLKK 139
Cdd:cd07250   81 YHGGAGVQHIALNTDDIFATVRALRA 106
VOC_like cd08353
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 47-149 8.85e-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: 319941  Cd Length: 142  Bit Score: 43.33  E-value: 8.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  47 RLNHVAIAVPDLEKAAAFYK----------NILGAQVSEAVPLPEHGVSVVFVNL--GNTKMEL---LHPlgrdSPIAGF 111
Cdd:cd08353    3 RMDHVGIVVEDLDAAIAFFTelglelegrmTVEGEWADRVVGLDGVRVEIAMLRTpdGHGRLELskfLTP----AAIPGH 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 188035928 112 LQ-KNKAGGMHHICIEVDNINAAVMDLKKKKIRSLSEEV 149
Cdd:cd08353   79 RPaPANALGLRHVAFAVDDIDAVVARLRKHGAELVGEVV 117
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
53-133 1.29e-05

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 42.54  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  53 IAVPDLEKAAAFYKNILGAQVSEAVPLPEHGVSVVFVNLGNTKMELLHPLGrDSPiagflqkNKAGGMHHICIEVDNINA 132
Cdd:COG2764    6 LVVDDAEEALEFYEDVFGFEVVFRMTDPDGKIMHAELRIGGSVLMLSDAPP-DSP-------AAEGNGVSLSLYVDDVDA 77


                 .
gi 188035928 133 A 133
Cdd:COG2764   78 L 78
PLN02875 PLN02875
4-hydroxyphenylpyruvate dioxygenase
 28-140 1.54e-05

4-hydroxyphenylpyruvate dioxygenase


Pssm-ID: 215472 [Multi-domain]  Cd Length: 398  Bit Score: 43.90  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  28 ASSTSQPLDqvtgsvWNLGRLNHVAIAVPDLEKAAAFYKNILG----AQVS-EAVPLPEHGV-SVVFVNlgNTKMELL-- 99
Cdd:PLN02875 167 ESSSSFPLD------YGLRRLDHAVGNVPNLLPAVNYIAGFTGfhefAEFTaEDVGTVDSGLnSMVLAS--NNEMVLLpl 238

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 188035928 100 ----HPLGRDSPIAGFLQKNKAGGMHHICIEVDNINAAVMDLKKK 140
Cdd:PLN02875 239 neptFGTKRKSQIQTYLEHNEGPGLQHLALKSDDIFGTLREMRAR 283
VOC_like cd07246
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 54-134 1.85e-05

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


Pssm-ID: 319910 [Multi-domain]  Cd Length: 124  Bit Score: 42.28  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  54 AVPDLEKAAAFYKNILGAQVSEAVPLPEHGVSVVFVNLGNTKMELLHPlgrdSPIAGFLQKNKAGGMH-HICIEVDNINA 132
Cdd:cd07246    8 VVEDAAAAIAFYKKAFGAEELGRTTQEDGRVGHAELRIGGTVVMVADE----NPERGALSPTKLGGTPvIFHLYVEDVDA 83


                 ..
gi 188035928 133 AV 134
Cdd:cd07246   84 TF 85
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 50-176 2.08e-05

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


Pssm-ID: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 41.93  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  50 HVAIAVPDLEKAAAFYKNILGAQVSEAVPLPEHGVsvvfVNLGNTKMELL------HPLGRDSPIAGFLqknkaggmhhI 123
Cdd:cd07264    3 YIVLYVDDFAASLRFYRDVLGLPPRFLHEEGEYAE----FDTGETKLALFsrkemaRSGGPDRRGSAFE----------L 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 188035928 124 CIEVDNINAAVMDLKKKKIRSLsEEVKIGAHGKPVIFLhpKDCGGVLVELEQA 176
Cdd:cd07264   69 GFEVDDVEATVEELVERGAEFV-REPANKPWGQTVAYV--RDPDGNLIEICEP 118
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 50-140 5.98e-05

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


Pssm-ID: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 40.74  E-value: 5.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  50 HVAIAVPDLEKAAAFYKNILGAQVSEAVPLPEHGVsVVFVNLGNTKMELLhpLGRDSPIAGFLQK-NKAGGMHHICIEVD 128
Cdd:cd07263    1 QVMLYVDDQDKALDFYVEKLGFEVVEDVPMGGMRW-VTVAPPGSPGTSLL--LEPKAHPAQMPQSpEAAGGTPGILLATD 77

                         90
                 ....*....|..
gi 188035928 129 NINAAVMDLKKK 140
Cdd:cd07263   78 DIDATYERLTAA 89
MhqB_like_C cd08360
C-terminal domain of Burkholderia sp. NF100 MhqB and similar proteins; This subfamily contains ...
 47-131 1.66e-04

C-terminal domain of Burkholderia sp. NF100 MhqB and similar proteins; This subfamily contains the C-terminal, catalytic, domain of Burkholderia sp. NF100 MhqB and similar proteins. MhqB is a type I extradiol dioxygenase involved in the catabolism of methylhydroquinone, an intermediate in the degradation of fenitrothion. The purified enzyme has shown extradiol ring cleavage activity toward 3-methylcatechol. Fe2+ was suggested as a cofactor, the same as most other enzymes in the family. Burkholderia sp. NF100 MhqB is encoded on the plasmid pNF1. 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: 319948  Cd Length: 134  Bit Score: 39.80  E-value: 1.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  47 RLNHVAIAVPDLEKAAAFYKNILGAQVSEAVplpehgvsvvfvnlgNTKMELLH-PLGRDSPIAGFlQKNKAGGMHHICI 125
Cdd:cd08360    3 RLGHVLLFSPDVDRSVDFYRDLLGLKVSDRS---------------FDIIAFMRgAAGSDHHLIAF-AKSSATGLHHMSW 66


                 ....*.
gi 188035928 126 EVDNIN 131
Cdd:cd08360   67 DVSDVN 72
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 48-70 3.64e-04

fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin resistant protein. FosA is a Mn(II) and K(+)-dependent glutathione transferase. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosA, catalyzes the addition of glutathione to the antibiotic fosfomycin, (1R,2S)-epoxypropylphosphonic acid, making it inactive. FosA is a Mn(II) dependent enzyme. It is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319908 [Multi-domain]  Cd Length: 121  Bit Score: 38.42  E-value: 3.64e-04
                         10        20
                 ....*....|....*....|...
gi 188035928  48 LNHVAIAVPDLEKAAAFYKNILG 70
Cdd:cd07244    2 INHITLAVSDLERSLAFYVDLLG 24
HPCD_N_class_II cd07266
N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 44-76 6.94e-04

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: 6.94e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 188035928  44 NLGRLNHVAIAVPDLEKAAAFYKNILGAQVSEA 76
Cdd:cd07266    1 DIIRLAHAELVVTDLAASREFYVDTLGLHVTDE 33
PRK10291 PRK10291
glyoxalase I; Provisional
 55-133 2.32e-03

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 36.54  E-value: 2.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 188035928  55 VPDLEKAAAFYKNILGAQVSEAVPLPEHGVSVVFVNLGNTKMELLHPLGRDSPIAGFLQKNKAGgmhHICIEVDNINAA 133
Cdd:PRK10291   4 VGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYG---HIALSVDNAAEA 79
HPPD_N_like cd08342
N-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate Synthase ...
 50-160 2.72e-03

N-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 HPP 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_N_like domain represents the N-terminal domain.


Pssm-ID: 319930  Cd Length: 141  Bit Score: 36.42  E-value: 2.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  50 HVAIAVPDLEKAAAFYKNILGAQ-VSEAVPLPEHGVSVVFVNlGNTKMELLHPLGRDSPIAGFLQKnkaggmhH------ 122
Cdd:cd08342    3 HVEFYVGNAKQAASYYSTGLGFEpVAYHGLETREKASHVLRQ-GDIRFVFTSPLSSDAPAADFLAK-------Hgdgvkd 74

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 188035928 123 ICIEVDNINAAVMDLKKKKIRSLSEEVKIGAHGKPVIF 160
Cdd:cd08342   75 VAFRVEDADAAYERAVARGAKPVAEPVELSDEGGEVVI 112
THT_oxygenase_C cd07257
The C-terminal domain of 2,4,5-trihydroxytoluene (THT) oxygenase; This subfamily contains the ...
 47-135 3.52e-03

The C-terminal domain of 2,4,5-trihydroxytoluene (THT) oxygenase; This subfamily contains the C-terminal, catalytic, domain of THT oxygenase. THT oxygenase is an extradiol dioxygenase in the 2,4-dinitrotoluene (DNT) degradation pathway. It catalyzes the conversion of 2,4,5-trihydroxytoluene to an unstable ring fission product, 2,4-dihydroxy-5-methyl-6-oxo-2,4-hexadienoic acid. The native protein was determined to be a dimer by gel filtration. The enzyme belongs to the type I family of extradiol dioxygenases which contains two structurally homologous barrel-shaped domains at the N- and C-terminus of each monomer. The active-site metal is located in the C-terminal barrel. Fe(II) is required for its catalytic activity.


Pssm-ID: 319920  Cd Length: 152  Bit Score: 36.16  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188035928  47 RLNHVAIAVPDLEKAAAFYKNILGAQVSEAVPLPEhgvsvvfvnlGNTKMELLHPLGRDSPI---AGFLQKNKAGGMHHI 123
Cdd:cd07257    1 KLGHVGLEVNDFEATFDWYTKTFGLKPSDVIYLPD----------GKTVGSFLHLDRGSEYVdhhSFFFAQGPRPKVHHA 70

                         90
                 ....*....|..
gi 188035928 124 CIEVDNINAAVM 135
Cdd:cd07257   71 AFEVHDFDSQVL 82
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 47-75 5.66e-03

N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC superfamily contains Bacillus subtilis CatE and similar proteins. CatE is proposed to function as Catechol-2,3-dioxygenase. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319918  Cd Length: 124  Bit Score: 35.37  E-value: 5.66e-03
                         10        20
                 ....*....|....*....|....*....
gi 188035928  47 RLNHVAIAVPDLEKAAAFYKNILGAQVSE 75
Cdd:cd07255    2 RIGRVTLKVADLERQSAFYQNVIGLSVLK 30
 
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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