NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1894710860|ref|XP_035755431|]
View 

methylmalonyl-CoA epimerase, mitochondrial isoform X2 [Egretta garzetta]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 44-172 9.45e-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: 222.20  E-value: 9.45e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  44 RLNHVAIAVPDLEKAQSLYKDVLGAQVSETVALPEHGVYTVFVELGNTKLELLHPLGEKSPIASFLQKNKtGGMHHICIE 123
Cdd:TIGR03081   1 RIDHVGIAVPDLEEAAKFYEDVLGAQVSEIEELPEQGVKVVFIALGNTKVELLEPLGEDSPIAKFLEKNG-GGIHHIAIE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1894710860 124 VDDIKAAMTELKKKKIRILSEEPKIGAHGKPVIFLHPKDCHGVLVELEQ 172
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 ...
 44-172 9.45e-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: 222.20  E-value: 9.45e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  44 RLNHVAIAVPDLEKAQSLYKDVLGAQVSETVALPEHGVYTVFVELGNTKLELLHPLGEKSPIASFLQKNKtGGMHHICIE 123
Cdd:TIGR03081   1 RIDHVGIAVPDLEEAAKFYEDVLGAQVSEIEELPEQGVKVVFIALGNTKVELLEPLGEDSPIAKFLEKNG-GGIHHIAIE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1894710860 124 VDDIKAAMTELKKKKIRILSEEPKIGAHGKPVIFLHPKDCHGVLVELEQ 172
Cdd:TIGR03081  80 VDDIEAALETLKEKGVRLIDEEPRIGAHGKPVAFLHPKSTGGVLIELEQ 128
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 45-172 5.41e-67

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: 200.11  E-value: 5.41e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  45 LNHVAIAVPDLEKAQSLYKDVLGAQVSETVALPEHGVYTVFVELGNTKLELLHPLGEKSPIASFLqKNKTGGMHHICIEV 124
Cdd:cd07249     1 LDHIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELGNTQIELLEPLGEDSPIAKFL-DKKGGGLHHIAFEV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1894710860 125 DDIKAAMTELKKKKIRILSEEPKIGAHGKPVIFLHPKDCHGVLVELEQ 172
Cdd:cd07249    80 DDIDAAVEELKAQGVRLLSEGPRIGAHGKRVAFLHPKDTGGVLIELVE 127
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 41-170 2.43e-38

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: 133.48  E-value: 2.43e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  41 KLGRLNHVAIAVP--DLEKAQSLYKDVLGAQV--SETVALPEHGVYTVFVEL--GNTKLELLHPLGEKSPIASFLQKNKT 114
Cdd:COG3185   143 GLTRIDHIGIAVPrgDLDEWVLFYEDVLGFEEirEEDIEDPYQGVRSAVLQSpdGKVRIPLNEPTSPDSQIAEFLEKYRG 222

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860 115 GGMHHICIEVDDIKAAMTELKKKKIRILSE--------EPKIGAHGKPVIFLHPK------DCHGVLVEL 170
Cdd:COG3185   223 EGIQHIAFATDDIEATVAALRARGVRFLDIpdnyyddlEPRVGAHGEDVAFLHPKgilvdrDTGGVLLQI 292
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
46-157 2.01e-28

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 101.59  E-value: 2.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  46 NHVAIAVPDLEKAQSLYKDVLGAQVSETVALPEHGVYTVFVELGNT--KLELLHPLGEKSPIAsflqkNKTGGMHHICIE 123
Cdd:pfam13669   1 HHVGIAVPDLDRALALWGALLGLGPEGDYRSEPQNVDLAFALLGDGpvEVELIQPLDGDSPLA-----RHGPGLHHLAYW 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1894710860 124 VDDIKAAMTELKKKKIRILSEEPKIGAHGKPVIF 157
Cdd:pfam13669  76 VDDLDAAVARLLDQGYRVAPKGPRAGAAGRRVAF 109
PLN02875 PLN02875
4-hydroxyphenylpyruvate dioxygenase
 42-137 1.92e-04

4-hydroxyphenylpyruvate dioxygenase


Pssm-ID: 215472 [Multi-domain]  Cd Length: 398  Bit Score: 40.81  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  42 LGRLNHVAIAVPDLEKAQSLYKDVLG----AQVS-ETVALPEHGVYTVFveLGNTKLELLHPLGE-------KSPIASFL 109
Cdd:PLN02875  178 LRRLDHAVGNVPNLLPAVNYIAGFTGfhefAEFTaEDVGTVDSGLNSMV--LASNNEMVLLPLNEptfgtkrKSQIQTYL 255

                          90       100
                  ....*....|....*....|....*...
gi 1894710860 110 QKNKTGGMHHICIEVDDIKAAMTELKKK 137
Cdd:PLN02875  256 EHNEGPGLQHLALKSDDIFGTLREMRAR 283
 
Name Accession Description Interval E-value
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
 44-172 9.45e-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: 222.20  E-value: 9.45e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  44 RLNHVAIAVPDLEKAQSLYKDVLGAQVSETVALPEHGVYTVFVELGNTKLELLHPLGEKSPIASFLQKNKtGGMHHICIE 123
Cdd:TIGR03081   1 RIDHVGIAVPDLEEAAKFYEDVLGAQVSEIEELPEQGVKVVFIALGNTKVELLEPLGEDSPIAKFLEKNG-GGIHHIAIE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1894710860 124 VDDIKAAMTELKKKKIRILSEEPKIGAHGKPVIFLHPKDCHGVLVELEQ 172
Cdd:TIGR03081  80 VDDIEAALETLKEKGVRLIDEEPRIGAHGKPVAFLHPKSTGGVLIELEQ 128
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 45-172 5.41e-67

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: 200.11  E-value: 5.41e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  45 LNHVAIAVPDLEKAQSLYKDVLGAQVSETVALPEHGVYTVFVELGNTKLELLHPLGEKSPIASFLqKNKTGGMHHICIEV 124
Cdd:cd07249     1 LDHIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELGNTQIELLEPLGEDSPIAKFL-DKKGGGLHHIAFEV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1894710860 125 DDIKAAMTELKKKKIRILSEEPKIGAHGKPVIFLHPKDCHGVLVELEQ 172
Cdd:cd07249    80 DDIDAAVEELKAQGVRLLSEGPRIGAHGKRVAFLHPKDTGGVLIELVE 127
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 41-170 2.43e-38

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: 133.48  E-value: 2.43e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  41 KLGRLNHVAIAVP--DLEKAQSLYKDVLGAQV--SETVALPEHGVYTVFVEL--GNTKLELLHPLGEKSPIASFLQKNKT 114
Cdd:COG3185   143 GLTRIDHIGIAVPrgDLDEWVLFYEDVLGFEEirEEDIEDPYQGVRSAVLQSpdGKVRIPLNEPTSPDSQIAEFLEKYRG 222

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860 115 GGMHHICIEVDDIKAAMTELKKKKIRILSE--------EPKIGAHGKPVIFLHPK------DCHGVLVEL 170
Cdd:COG3185   223 EGIQHIAFATDDIEATVAALRARGVRFLDIpdnyyddlEPRVGAHGEDVAFLHPKgilvdrDTGGVLLQI 292
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 44-170 2.03e-30

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: 107.39  E-value: 2.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  44 RLNHVAIAVPDLEKAQSLYKDVLGAQVSETVALPEHGVYTVFVELGN-TKLELLHPLGEKspiasflQKNKTGGMHHICI 122
Cdd:COG0346     2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDgTELELFEAPGAA-------PAPGGGGLHHLAF 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1894710860 123 EVDDIKAAMTELKKKKIRILsEEPKIGAHGKPVIFLhpKDCHGVLVEL 170
Cdd:COG0346    75 RVDDLDAAYARLRAAGVEIE-GEPRDRAYGYRSAYF--RDPDGNLIEL 119
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
46-157 2.01e-28

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 101.59  E-value: 2.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  46 NHVAIAVPDLEKAQSLYKDVLGAQVSETVALPEHGVYTVFVELGNT--KLELLHPLGEKSPIAsflqkNKTGGMHHICIE 123
Cdd:pfam13669   1 HHVGIAVPDLDRALALWGALLGLGPEGDYRSEPQNVDLAFALLGDGpvEVELIQPLDGDSPLA-----RHGPGLHHLAYW 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1894710860 124 VDDIKAAMTELKKKKIRILSEEPKIGAHGKPVIF 157
Cdd:pfam13669  76 VDDLDAAVARLLDQGYRVAPKGPRAGAAGRRVAF 109
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
44-170 3.81e-19

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 78.26  E-value: 3.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  44 RLNHVAIAVPDLEKAQSLYKDVLGAQVSETVALPEHGVYTVFVEL-GNTKLELLHPLGEKSPIASFlqknKTGGMHHICI 122
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLaGGRVLELLLNETPPPAAAGF----GGHHIAFIAF 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1894710860 123 EVDDIKAAMTELKKKKIRILSEEPKIGAHGkpvIFLHPKDCHGVLVEL 170
Cdd:pfam00903  77 SVDDVDAAYDRLKAAGVEIVREPGRHGWGG---RYSYFRDPDGNLIEL 121
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 47-170 1.16e-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: 63.70  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  47 HVAIAVPDLEKAQSLYKDVLGAQVSETvalPEHGVYTVFVELGNTKLELLHPLGEKSPIAsflqknktGGMHHICIEVDD 126
Cdd:cd06587     1 HVALRVPDLDASVAFYEEVLGFEVVSR---NEGGGFAFLRLGPGLRLALLEGPEPERPGG--------GGLFHLAFEVDD 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1894710860 127 IKAAMTELKKKKIRILSEEPKIGAH-GKPVIFLHPKDchGVLVEL 170
Cdd:cd06587    70 VDEVDERLREAGAEGELVAPPVDDPwGGRSFYFRDPD--GNLIEF 112
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 44-134 2.33e-11

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: 58.50  E-value: 2.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  44 RLNHVAIAVPDLEKAQSLYKDVLGAQV---SETVALPEHGV----YTVFVE-----------LGN-TKLELLHPLGEKSP 104
Cdd:cd16361     1 GVNHVGITVPDLDAAVEFYTDVLGAEVvyrSTPLAEGDRGGgemrAAGFVPgfarariamlrLGPgPGIELFEYKGPEQR 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1894710860 105 IASFlQKNKTGGmHHICIEVDDIKAAMTEL 134
Cdd:cd16361    81 APVP-RNSDVGI-FHFALQVDDVEAAAERL 108
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 45-170 1.65e-10

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: 55.40  E-value: 1.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  45 LNHVAIAVPDLEKAQSLYKDVLGAqvsETVALPEHGVYTVfVELGNTKLELLHpLGEKSPIASFLQKNKTGGMHHICIEV 124
Cdd:cd07245     1 LDHVALACPDLERARRFYTDVLGL---EEVPRPPFLKFGG-AWLYLGGGQQIH-LVVEQNPSELPRPEHPGRDRHPSFSV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1894710860 125 DDIKAAMTELKKKKIRILSEEPKIGahGKPVIFLHpkDCHGVLVEL 170
Cdd:cd07245    76 PDLDALKQRLKEAGIPYTESTSPGG--GVTQLFFR--DPDGNRLEF 117
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 43-170 1.02e-09

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 53.49  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  43 GRLNHVAIAVPDLEKAQSLYKDVLGAQVSETValPEHGVYTVFvELGNTKLELLHPLGEKSPIASFlqknktggmhHICI 122
Cdd:COG3324     3 GTIVWVELPVDDLERAKAFYEEVFGWTFEDDA--GPGGDYAEF-DTDGGQVGGLMPGAEEPGGPGW----------LLYF 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1894710860 123 EVDDIKAAMTELKKKKIRILSEEPKIGAHGKPVIFlhpKDCHGVLVEL 170
Cdd:COG3324    70 AVDDLDAAVARVEAAGGTVLRPPTDIPPWGRFAVF---RDPEGNRFGL 114
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
44-141 1.41e-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: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  44 RLNHVAIAVPDLEKAQSLYKDVLGAQVSETvalpEHGVYTVFVELGNTKLELlhplgEKSPIASFLQknKTGGMHHICIE 123
Cdd:COG2514     3 RLGHVTLRVRDLERSAAFYTDVLGLEVVER----EGGRVYLRADGGEHLLVL-----EEAPGAPPRP--GAAGLDHVAFR 71

                          90       100
                  ....*....|....*....|.
gi 1894710860 124 VDDIK---AAMTELKKKKIRI 141
Cdd:COG2514    72 VPSRAdldAALARLAAAGVPV 92
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 44-171 4.69e-09

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: 51.84  E-value: 4.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  44 RLNHVAIAVPDLEKAQSLYKDVLGAQVSEtvalPEHGVYTvfVELGNTKLElLHPLGEKspiasFLQK--NKTGGMHHIC 121
Cdd:cd07253     3 RLDHLVLTVKDIERTIDFYTKVLGMTVVT----FKEGRKA--LRFGNQKIN-LHQKGKE-----FEPKasAPTPGSADLC 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1894710860 122 IEVD-DIKAAMTELKKKKIRI-LSEEPKIGAHGkPVIFLHPKDCHGVLVELE 171
Cdd:cd07253    71 FITEtPIDEVLEHLEACGVTIeEGPVKRTGALG-PILSIYFRDPDGNLIELS 121
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 47-170 2.12e-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: 2.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  47 HVAIAVPDLEKAQSLYKDVLGAQVSETVALPEhGVYT-VFV----ELGNTKLELLHPLGekspIASFLQKNKTGgmhHIC 121
Cdd:cd16358     3 HTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPE-GKYTlAFVgygdEDENTVLELTYNWG----VDKYDLGTAYG---HIA 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1894710860 122 IEVDDIKAAMTELKKKKIRILsEEPKIGAHGKPVI-FLHPKDchGVLVEL 170
Cdd:cd16358    75 IGVEDVYETCERIRKKGGKVT-REPGPMKGGTTVIaFVEDPD--GYKIEL 121
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 44-140 2.35e-08

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: 49.85  E-value: 2.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  44 RLNHVAIAVPDLEKAQSLYKDVLGAQVSETVALPEHGVYTVFVELGNTKLELlhplgekspiasFLQKN--------KTG 115
Cdd:cd08352     2 KIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDIKLDLALGGYQLEL------------FIKPDaparpsypEAL 69

                          90       100
                  ....*....|....*....|....*
gi 1894710860 116 GMHHICIEVDDIKAAMTELKKKKIR 140
Cdd:cd08352    70 GLRHLAFKVEDVEATVAELKSLGIE 94
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 47-173 2.99e-07

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: 46.94  E-value: 2.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  47 HVAIAVPDLEKAQSLYKDVLGAQVSetvALPEHGVYTVFvELGNTKLELL------HPLGEKSPIASFLqknktggmhhI 120
Cdd:cd07264     3 YIVLYVDDFAASLRFYRDVLGLPPR---FLHEEGEYAEF-DTGETKLALFsrkemaRSGGPDRRGSAFE----------L 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1894710860 121 CIEVDDIKAAMTELKKKKIRILsEEPKIGAHGKPVIFLHPKDchGVLVELEQA 173
Cdd:cd07264    69 GFEVDDVEATVEELVERGAEFV-REPANKPWGQTVAYVRDPD--GNLIEICEP 118
Glyoxalase_3 pfam13468
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 45-136 3.44e-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: 3.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  45 LNHVAIAVPDLEKAQSLYKDVLGAQVSETVALPEHGVYTVFVELGNTKLELLHPLGEK----SPIASFLQKNKTG-GMHH 119
Cdd:pfam13468   1 LDHVVLAVPDLDEAAARFARALGFTVTPGGRHPGMGTANALIMFGDGYLELLAVDPEApappRGRWFGLDRLADGeGLLG 80

                          90
                  ....*....|....*..
gi 1894710860 120 ICIEVDDIKAAMTELKK 136
Cdd:pfam13468  81 WALRTDDIDAVAARLRA 97
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 47-170 6.60e-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: 46.16  E-value: 6.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  47 HVAIAVPDLEKAQSLYKDVLGAQVSETVALPEHGVyTVFVELGNtkLELLHPLgekspiasFLQKNKTGGMHHICIEV-- 124
Cdd:cd08343     2 HVVLCSPDVEASRDFYTDVLGFRVSDRIVDPGVDG-GAFLHCDR--GTDHHTV--------ALAGGPHPGLHHVAFEVhd 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1894710860 125 -DDIKAAMTELKKKKIRIlseEPKIGAHGKPV-IFLHPKDCHGVLVEL 170
Cdd:cd08343    71 lDDVGRGHDRLREKGYKI---EWGPGRHGLGSqVFDYWFDPSGNRVEY 115
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 47-146 7.60e-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: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 43.05  E-value: 7.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  47 HVAIAVPDLEKAQSLYKDVLGAQVSETVALPEHGVYTVFVELGNTKLELLHPlgeKSPIASFLQK-NKTGGMHHICIEVD 125
Cdd:cd07263     1 QVMLYVDDQDKALDFYVEKLGFEVVEDVPMGGMRWVTVAPPGSPGTSLLLEP---KAHPAQMPQSpEAAGGTPGILLATD 77

                          90       100
                  ....*....|....*....|.
gi 1894710860 126 DIKAAMTELKKKKIRILsEEP 146
Cdd:cd07263    78 DIDATYERLTAAGVTFV-QEP 97
VOC_like cd08353
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 44-144 8.12e-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: 8.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  44 RLNHVAIAVPDLEKAQSLYKD----------VLGAQVSETVALpeHGVYTVFVEL----GNTKLEL---LHPLGEKSPIA 106
Cdd:cd08353     3 RMDHVGIVVEDLDAAIAFFTElglelegrmtVEGEWADRVVGL--DGVRVEIAMLrtpdGHGRLELskfLTPAAIPGHRP 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1894710860 107 SFLQknkTGGMHHICIEVDDIKAAMTELKKKKIRILSE 144
Cdd:cd08353    81 APAN---ALGLRHVAFAVDDIDAVVARLRKHGAELVGE 115
BphC1-RGP6_C_like cd07237
C-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase; This subfamily contains the ...
 45-151 1.95e-05

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: 42.65  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  45 LNHVAIAVPDLEKAQSLYKDVLGAQVSETVAL---PEHGVYTVFvelgntklelLHPLGEKSPIAsFLQKNKTGGMHHIC 121
Cdd:cd07237    10 LGHVVLIVPDVDEALAFYTDVLGFRLSDEIRIplpPGVTARLHF----------LHCNGRHHSLA-FGAGPGPKRLHHLM 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1894710860 122 IEVDDIKA---AMTELKKKKIRILSEepkIGAH 151
Cdd:cd07237    79 LEVTSLDDvgrAYDRVRKRGIPIAMT---LGRH 108
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
50-144 2.64e-05

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 41.38  E-value: 2.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  50 IAVPDLEKAQSLYKDVLGAQVSETVALPEHGVYTVFVELGNTKLELLHPLGEkspiasflQKNKTGGMHHICIEVDDIKA 129
Cdd:COG2764     6 LVVDDAEEALEFYEDVFGFEVVFRMTDPDGKIMHAELRIGGSVLMLSDAPPD--------SPAAEGNGVSLSLYVDDVDA 77

                          90
                  ....*....|....*
gi 1894710860 130 AMTELKKKKIRILSE 144
Cdd:COG2764    78 LFARLVAAGATVVMP 92
HPPD_C_like cd07250
C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate synthase ...
 42-136 1.40e-04

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: 40.62  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  42 LGRLNHVAIAVPD--LEKAQSLYKDVLGAQ-----VSETVALPEHGVYTVFVELGNTKLELlhPLGE------KSPIASF 108
Cdd:cd07250     1 LTRIDHVVGNVPDgeMDPAVEWYEKCLGFHrfwefDDEDIGTEYSGLRSIVLANPNETIKL--PLNEpapgkrKSQIQEF 78

                          90       100
                  ....*....|....*....|....*...
gi 1894710860 109 LQKNKTGGMHHICIEVDDIKAAMTELKK 136
Cdd:cd07250    79 LDYHGGAGVQHIALNTDDIFATVRALRA 106
HPPD_N_like cd08342
N-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate Synthase ...
 47-157 1.87e-04

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: 39.50  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  47 HVAIAVPDLEKAQSLYKDVLGAQVSETVALPEHGVYTVFVELGNTKLELLHPLGEKSPIASFLQKnktggmhH------I 120
Cdd:cd08342     3 HVEFYVGNAKQAASYYSTGLGFEPVAYHGLETREKASHVLRQGDIRFVFTSPLSSDAPAADFLAK-------HgdgvkdV 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1894710860 121 CIEVDDIKAAMTELKKKKIRILSEEPKIGAHGKPVIF 157
Cdd:cd08342    76 AFRVEDADAAYERAVARGAKPVAEPVELSDEGGEVVI 112
PLN02875 PLN02875
4-hydroxyphenylpyruvate dioxygenase
 42-137 1.92e-04

4-hydroxyphenylpyruvate dioxygenase


Pssm-ID: 215472 [Multi-domain]  Cd Length: 398  Bit Score: 40.81  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  42 LGRLNHVAIAVPDLEKAQSLYKDVLG----AQVS-ETVALPEHGVYTVFveLGNTKLELLHPLGE-------KSPIASFL 109
Cdd:PLN02875  178 LRRLDHAVGNVPNLLPAVNYIAGFTGfhefAEFTaEDVGTVDSGLNSMV--LASNNEMVLLPLNEptfgtkrKSQIQTYL 255

                          90       100
                  ....*....|....*....|....*...
gi 1894710860 110 QKNKTGGMHHICIEVDDIKAAMTELKKK 137
Cdd:PLN02875  256 EHNEGPGLQHLALKSDDIFGTLREMRAR 283
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 45-139 2.40e-04

Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that prefers the divalent cation zinc 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: 319900 [Multi-domain]  Cd Length: 142  Bit Score: 39.23  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  45 LNHVAIAVPDLEKAQSLYKDVLGAQV-----------------SETVALPEHGVYTVFVELGNTKLELLHPLG-EKSPIA 106
Cdd:cd07233     1 FNHTMLRVKDPKKSLKFYTEVLGMKLlrkkdfpemkfslyflgYEDPKDIPKDPRTAWVFSREGTLELTHNWGtENDEDP 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1894710860 107 SFLQKNKTG-GMHHICIEVDDIKAAMTELKKKKI 139
Cdd:cd07233    81 VYHNGNSDPrGFGHIGIAVDDVYAACERFEELGV 114
THT_oxygenase_C cd07257
The C-terminal domain of 2,4,5-trihydroxytoluene (THT) oxygenase; This subfamily contains the ...
 44-129 3.67e-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: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  44 RLNHVAIAVPDLEKAQSLYKDVLGAQVSETVALPEHGVYTVFvelgntklelLHPLGEKSPI---ASFLQKNKTGGMHHI 120
Cdd:cd07257     1 KLGHVGLEVNDFEATFDWYTKTFGLKPSDVIYLPDGKTVGSF----------LHLDRGSEYVdhhSFFFAQGPRPKVHHA 70


                  ....*....
gi 1894710860 121 CIEVDDIKA 129
Cdd:cd07257    71 AFEVHDFDS 79
HPCD_N_class_II cd07266
N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 44-72 3.77e-03

N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily contains the N-terminal, non-catalytic, domain of HPCD. HPCD catalyses the second step in the degradation of 4-hydroxyphenylacetate to succinate and pyruvate. The aromatic ring of 4-hydroxyphenylacetate is opened by this dioxygenase to yield the 3,4-diol product, 2-hydroxy-5-carboxymethylmuconate semialdehyde. HPCD is a homotetramer and each monomer contains two structurally homologous barrel-shaped domains at the N- and C-terminus. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism. Most extradiol dioxygenases contain Fe(II) in their active site, but HPCD can be activated by either Mn(II) or Fe(II). These enzymes belong to the type I class II family of extradiol dioxygenases. The class III 3,4-dihydroxyphenylacetate 2,3-dioxygenases belong to a different superfamily.


Pssm-ID: 319927  Cd Length: 118  Bit Score: 35.46  E-value: 3.77e-03
                          10        20
                  ....*....|....*....|....*....
gi 1894710860  44 RLNHVAIAVPDLEKAQSLYKDVLGAQVSE 72
Cdd:cd07266     4 RLAHAELVVTDLAASREFYVDTLGLHVTD 32
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 44-152 3.81e-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: 35.75  E-value: 3.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  44 RLNHVAIAVPDLEKAQSLYKDVLGAQVSETVAlpehGVYTVFVELGNTKLELlhplgEKSPIASFLQKNKTgGMHHICIE 123
Cdd:cd07255     2 RIGRVTLKVADLERQSAFYQNVIGLSVLKQNA----SRAYLGVDGKQVLLVL-----EAIPDAVLAPRSTT-GLYHFAIL 71

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1894710860 124 VDDIKAAMTELKkkkiRILSEEPKIGA--HG 152
Cdd:cd07255    72 LPDRKALGRALA----HLAEHGPLIGAadHG 98
PLN02300 PLN02300
lactoylglutathione lyase
 44-172 5.56e-03

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 36.30  E-value: 5.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894710860  44 RLNHVAIAVPDLEKAQSLYKDVLGAQVSETVALPEHGVYTVFVELG----NTKLELLHPLG-EKSPIASflqknktgGMH 118
Cdd:PLN02300   24 RMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYGpedsNFVVELTYNYGvDKYDIGT--------GFG 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1894710860 119 HICIEVDDIkAAMTELKKKKIRILSEEPKIGAHGKPVI-FLhpKDCHGVLVELEQ 172
Cdd:PLN02300   96 HFGIAVEDV-AKTVELVKAKGGKVTREPGPVKGGKSVIaFV--KDPDGYKFELIQ 147
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH