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Conserved domains on  [gi|895953806|ref|WP_049038672|]
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MULTISPECIES: methylmalonyl-CoA epimerase [Elizabethkingia]

Protein Classification

VOC family protein( domain architecture ID 10163523)

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

CATH:  3.10.180.10
PubMed:  21820381

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 5-131 8.64e-48

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: 150.03  E-value: 8.64e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806   5 IEHLGIAVKSLETSDSLFAKLIGREAYKMEEVEREGVKTSFYQIGESKIELLESTREDSPISKFIEKKGEGVHHIAFGVD 84
Cdd:cd07249    1 LDHIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELGNTQIELLEPLGEDSPIAKFLDKKGGGLHHIAFEVD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 895953806  85 DIYAEIERLKKEGFEFISEEPKDGADNKIVVFLHPKSTNGVLIELCQ 131
Cdd:cd07249   81 DIDAAVEELKAQGVRLLSEGPRIGAHGKRVAFLHPKDTGGVLIELVE 127
 
Name Accession Description Interval E-value
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 5-131 8.64e-48

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: 150.03  E-value: 8.64e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806   5 IEHLGIAVKSLETSDSLFAKLIGREAYKMEEVEREGVKTSFYQIGESKIELLESTREDSPISKFIEKKGEGVHHIAFGVD 84
Cdd:cd07249    1 LDHIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELGNTQIELLEPLGEDSPIAKFLDKKGGGLHHIAFEVD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 895953806  85 DIYAEIERLKKEGFEFISEEPKDGADNKIVVFLHPKSTNGVLIELCQ 131
Cdd:cd07249   81 DIDAAVEELKAQGVRLLSEGPRIGAHGKRVAFLHPKDTGGVLIELVE 127
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
 4-131 3.76e-47

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: 148.24  E-value: 3.76e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806    4 KIEHLGIAVKSLETSDSLFAKLIGREAYKMEEVEREGVKTSFYQIGESKIELLESTREDSPISKFIEKKGEGVHHIAFGV 83
Cdd:TIGR03081   1 RIDHVGIAVPDLEEAAKFYEDVLGAQVSEIEELPEQGVKVVFIALGNTKVELLEPLGEDSPIAKFLEKNGGGIHHIAIEV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 895953806   84 DDIYAEIERLKKEGFEFISEEPKDGADNKIVVFLHPKSTNGVLIELCQ 131
Cdd:TIGR03081  81 DDIEAALETLKEKGVRLIDEEPRIGAHGKPVAFLHPKSTGGVLIELEQ 128
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 1-129 1.09e-40

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: 138.10  E-value: 1.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806   1 MLDKIEHLGIAVK--SLETSDSLFAKLIGREAYKMEEVE--REGVKTSFYQI--GESKIELLESTREDSPISKFIEKK-G 73
Cdd:COG3185  143 GLTRIDHIGIAVPrgDLDEWVLFYEDVLGFEEIREEDIEdpYQGVRSAVLQSpdGKVRIPLNEPTSPDSQIAEFLEKYrG 222

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806  74 EGVHHIAFGVDDIYAEIERLKKEGFEFISE--------EPKDGADNKIVVFLHPK------STNGVLIEL 129
Cdd:COG3185  223 EGIQHIAFATDDIEATVAALRARGVRFLDIpdnyyddlEPRVGAHGEDVAFLHPKgilvdrDTGGVLLQI 292
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-116 8.83e-22

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 83.10  E-value: 8.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806    7 HLGIAVKSLETSDSLFAKLIGREAYKMEEVEREGVKTSFYQIGES--KIELLESTREDSPIskfiEKKGEGVHHIAFGVD 84
Cdd:pfam13669   2 HVGIAVPDLDRALALWGALLGLGPEGDYRSEPQNVDLAFALLGDGpvEVELIQPLDGDSPL----ARHGPGLHHLAYWVD 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 895953806   85 DIYAEIERLKKEGFEFISEEPKDGADNKIVVF 116
Cdd:pfam13669  78 DLDAAVARLLDQGYRVAPKGPRAGAAGRRVAF 109
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 75-134 4.33e-04

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 38.26  E-value: 4.33e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806  75 GVHHIAFGVDDIYAEIERLKKEGFEFIsEEPKDGAdNKIVVFLhpKSTNGVLIELCQEKR 134
Cdd:PLN03042 121 GFGHIGITVDDVYKACERFEKLGVEFV-KKPDDGK-MKGLAFI--KDPDGYWIEIFDLKR 176
 
Name Accession Description Interval E-value
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 5-131 8.64e-48

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: 150.03  E-value: 8.64e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806   5 IEHLGIAVKSLETSDSLFAKLIGREAYKMEEVEREGVKTSFYQIGESKIELLESTREDSPISKFIEKKGEGVHHIAFGVD 84
Cdd:cd07249    1 LDHIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELGNTQIELLEPLGEDSPIAKFLDKKGGGLHHIAFEVD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 895953806  85 DIYAEIERLKKEGFEFISEEPKDGADNKIVVFLHPKSTNGVLIELCQ 131
Cdd:cd07249   81 DIDAAVEELKAQGVRLLSEGPRIGAHGKRVAFLHPKDTGGVLIELVE 127
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
 4-131 3.76e-47

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: 148.24  E-value: 3.76e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806    4 KIEHLGIAVKSLETSDSLFAKLIGREAYKMEEVEREGVKTSFYQIGESKIELLESTREDSPISKFIEKKGEGVHHIAFGV 83
Cdd:TIGR03081   1 RIDHVGIAVPDLEEAAKFYEDVLGAQVSEIEELPEQGVKVVFIALGNTKVELLEPLGEDSPIAKFLEKNGGGIHHIAIEV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 895953806   84 DDIYAEIERLKKEGFEFISEEPKDGADNKIVVFLHPKSTNGVLIELCQ 131
Cdd:TIGR03081  81 DDIEAALETLKEKGVRLIDEEPRIGAHGKPVAFLHPKSTGGVLIELEQ 128
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 1-129 1.09e-40

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: 138.10  E-value: 1.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806   1 MLDKIEHLGIAVK--SLETSDSLFAKLIGREAYKMEEVE--REGVKTSFYQI--GESKIELLESTREDSPISKFIEKK-G 73
Cdd:COG3185  143 GLTRIDHIGIAVPrgDLDEWVLFYEDVLGFEEIREEDIEdpYQGVRSAVLQSpdGKVRIPLNEPTSPDSQIAEFLEKYrG 222

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806  74 EGVHHIAFGVDDIYAEIERLKKEGFEFISE--------EPKDGADNKIVVFLHPK------STNGVLIEL 129
Cdd:COG3185  223 EGIQHIAFATDDIEATVAALRARGVRFLDIpdnyyddlEPRVGAHGEDVAFLHPKgilvdrDTGGVLLQI 292
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-116 8.83e-22

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 83.10  E-value: 8.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806    7 HLGIAVKSLETSDSLFAKLIGREAYKMEEVEREGVKTSFYQIGES--KIELLESTREDSPIskfiEKKGEGVHHIAFGVD 84
Cdd:pfam13669   2 HVGIAVPDLDRALALWGALLGLGPEGDYRSEPQNVDLAFALLGDGpvEVELIQPLDGDSPL----ARHGPGLHHLAYWVD 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 895953806   85 DIYAEIERLKKEGFEFISEEPKDGADNKIVVF 116
Cdd:pfam13669  78 DLDAAVARLLDQGYRVAPKGPRAGAAGRRVAF 109
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 4-134 1.38e-20

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: 80.81  E-value: 1.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806   4 KIEHLGIAVKSLETSDSLFAKLIGREAYKMEEVEREGVKTSFYQIGE-SKIELLESTREDSPiskfieKKGEGVHHIAFG 82
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDgTELELFEAPGAAPA------PGGGGLHHLAFR 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 895953806  83 VDDIYAEIERLKKEGFEFIsEEPKDGADNKIVVFLhpKSTNGVLIELCQEKR 134
Cdd:COG0346   76 VDDLDAAYARLRAAGVEIE-GEPRDRAYGYRSAYF--RDPDGNLIELVEPPP 124
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
4-129 1.68e-14

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 64.78  E-value: 1.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806    4 KIEHLGIAVKSLETSDSLFAKLIG-REAYKMEEVEREGVKTSFYQIGESKIELLESTREDSPISKFiekKGEGVHHIAFG 82
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGfKLVEETDAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGF---GGHHIAFIAFS 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 895953806   83 VDDIYAEIERLKKEGFEFISEEPKDGADNKIVVFLHPkstNGVLIEL 129
Cdd:pfam00903  78 VDDVDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDP---DGNLIEL 121
Glyoxalase_3 pfam13468
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 5-110 9.97e-09

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


Pssm-ID: 433233  Cd Length: 175  Bit Score: 50.80  E-value: 9.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806    5 IEHLGIAVKSLETSDSLFAKLIGREAYKMEEVEREGVKTSFYQIGESKIELL----ESTREDSPISKFIE--KKGEGVHH 78
Cdd:pfam13468   1 LDHVVLAVPDLDEAAARFARALGFTVTPGGRHPGMGTANALIMFGDGYLELLavdpEAPAPPRGRWFGLDrlADGEGLLG 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 895953806   79 IAFGVDDIYAEIERLKKEGFEFISEEPKDGAD 110
Cdd:pfam13468  81 WALRTDDIDAVAARLRAAGVEPGRRVRPDGGD 112
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 7-129 4.67e-08

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


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 47.90  E-value: 4.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806   7 HLGIAVKSLETSDSLFAKLIGreaykMEEVER-EGVKTSFYQIGE-SKIELLESTREDSPiskfiekKGEGVHHIAFGVD 84
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLG-----FEVVSRnEGGGFAFLRLGPgLRLALLEGPEPERP-------GGGGLFHLAFEVD 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 895953806  85 DIYAEIERLKKEGFEF--ISEEPKDGADNKIVVFLHPkstNGVLIEL 129
Cdd:cd06587   69 DVDEVDERLREAGAEGelVAPPVDDPWGGRSFYFRDP---DGNLIEF 112
VOC_like cd08353
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 4-103 1.11e-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: 319941  Cd Length: 142  Bit Score: 47.57  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806   4 KIEHLGIAVKSLETSDSLFAKL----IGREAYKMEEVER----EGVKTSFYQI----GESKIELLE----STREDSPISK 67
Cdd:cd08353    3 RMDHVGIVVEDLDAAIAFFTELglelEGRMTVEGEWADRvvglDGVRVEIAMLrtpdGHGRLELSKfltpAAIPGHRPAP 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 895953806  68 FIEKkgeGVHHIAFGVDDIYAEIERLKKEGFEFISE 103
Cdd:cd08353   83 ANAL---GLRHVAFAVDDIDAVVARLRKHGAELVGE 115
HPPD_C_like cd07250
C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate synthase ...
 63-102 1.31e-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: 45.24  E-value: 1.31e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 895953806  63 SPISKFIEK-KGEGVHHIAFGVDDIYAEIERLKKEGFEFIS 102
Cdd:cd07250   73 SQIQEFLDYhGGAGVQHIALNTDDIFATVRALRARGVEFLP 113
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
4-133 1.41e-06

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 44.56  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806   4 KIEHLGIAVKSLETSDSLFAKLIGreaykMEEVEREGvKTSFYQIGESKIEL-LESTREDSPiskfiEKKGEGVHHIAFG 82
Cdd:COG2514    3 RLGHVTLRVRDLERSAAFYTDVLG-----LEVVEREG-GRVYLRADGGEHLLvLEEAPGAPP-----RPGAAGLDHVAFR 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 895953806  83 VD---DIYAEIERLKKEGFEFisEEPKDGADNKIVVFLHPkstNGVLIELCQEK 133
Cdd:COG2514   72 VPsraDLDAALARLAAAGVPV--EGAVDHGVGESLYFRDP---DGNLIELYTDR 120
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 2-103 1.54e-06

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: 45.65  E-value: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806   2 LDKIEHLGIAVKSLETSDSLFAKL----IGREAYKMEEVEREGvktsfyqigesKIELLESTREDSPISKFIEKKGEGVH 77
Cdd:COG3185    1 LDGIEFVEFAVGDAEQLAFLLEALgftlVARHRSKAVTLYRQG-----------DINFVLNAEPDSFAARFAREHGPGVC 69

                         90       100
                 ....*....|....*....|....*.
gi 895953806  78 HIAFGVDDIYAEIERLKKEGFEFISE 103
Cdd:COG3185   70 AIAFRVDDAAAAYERALALGAEPFEG 95
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-108 3.26e-06

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


Pssm-ID: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 43.08  E-value: 3.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806   5 IEHLGIAVKSLETSDSLFAKLIGreaykMEEVER------EGVktsFYQIGES-KIELLESTREDSPISKFIEKKGegvH 77
Cdd:cd07245    1 LDHVALACPDLERARRFYTDVLG-----LEEVPRppflkfGGA---WLYLGGGqQIHLVVEQNPSELPRPEHPGRD---R 69

                         90       100       110
                 ....*....|....*....|....*....|.
gi 895953806  78 HIAFGVDDIYAEIERLKKEGFEFISEEPKDG 108
Cdd:cd07245   70 HPSFSVPDLDALKQRLKEAGIPYTESTSPGG 100
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 73-133 1.36e-05

lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and glyoxalase I. Glyoxylase I is a homodimer in many species. In some eukaryotes, including yeasts and plants, the orthologous protein carries a tandem duplication, is twice as long, and hits this model twice. [Central intermediary metabolism, Amino sugars, Energy metabolism, Other]


Pssm-ID: 272886  Cd Length: 150  Bit Score: 42.10  E-value: 1.36e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 895953806   73 GEGVHHIAFGVDDIYAEIERLKKEGFEFISEEPKDGADNKIVVFLhpKSTNGVLIELCQEK 133
Cdd:TIGR00068  84 GNGFGHIAIGVDDVYKACERVRALGGNVVREPGPVKGGTTVIAFV--EDPDGYKIELIQRK 142
HPPD_N_like cd08342
N-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate Synthase ...
 5-116 1.58e-05

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: 41.81  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806   5 IEHLGIAVKSLETSDSLFAKLIGREAYKMEEVEREGVKTSFYQIGESKIELLESTREDSPISKFIEKKGEGVHHIAFGVD 84
Cdd:cd08342    1 FDHVEFYVGNAKQAASYYSTGLGFEPVAYHGLETREKASHVLRQGDIRFVFTSPLSSDAPAADFLAKHGDGVKDVAFRVE 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 895953806  85 DIYAEIERLKKEGFEFISEEPKDGADNKIVVF 116
Cdd:cd08342   81 DADAAYERAVARGAKPVAEPVELSDEGGEVVI 112
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 65-134 3.20e-05

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 40.39  E-value: 3.20e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 895953806  65 ISKFIEKKGEGVHHIAFGVDDIYAEIERLKKEGFEFIsEEPKDGADN-KIVVFLHPkstNGVLIELCQEKR 134
Cdd:COG3324   53 LMPGAEEPGGPGWLLYFAVDDLDAAVARVEAAGGTVL-RPPTDIPPWgRFAVFRDP---EGNRFGLWQPAA 119
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 70-129 1.95e-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: 38.85  E-value: 1.95e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806  70 EKKGEGvhHIAFGVDDIYAEIERLKKEGFEFIsEEPKDGADNKIVVFLHPkstNGVLIEL 129
Cdd:cd07233   88 DPRGFG--HIGIAVDDVYAACERFEELGVKFK-KKPDDGKMKGIAFIKDP---DGYWIEI 141
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 75-134 4.33e-04

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 38.26  E-value: 4.33e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806  75 GVHHIAFGVDDIYAEIERLKKEGFEFIsEEPKDGAdNKIVVFLhpKSTNGVLIELCQEKR 134
Cdd:PLN03042 121 GFGHIGITVDDVYKACERFEKLGVEFV-KKPDDGK-MKGLAFI--KDPDGYWIEIFDLKR 176
PLN02367 PLN02367
lactoylglutathione lyase
 70-134 7.80e-04

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 37.67  E-value: 7.80e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 895953806  70 EKKGEGvhHIAFGVDDIYAEIERLKKEGFEFIsEEPKDGaDNKIVVFLhpKSTNGVLIELCQEKR 134
Cdd:PLN02367 166 EPRGFG--HIGITVDDVYKACERFEELGVEFV-KKPNDG-KMKGIAFI--KDPDGYWIEIFDLKT 224
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 71-129 1.27e-03

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: 36.22  E-value: 1.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806  71 KKGEGVHHIAFGVDDIYAEIERLKKEGFEFISE-EPKDGADNKIVVFLHPkstNGVLIEL 129
Cdd:cd16358   65 DLGTAYGHIAIGVEDVYETCERIRKKGGKVTREpGPMKGGTTVIAFVEDP---DGYKIEL 121
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-103 2.75e-03

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


Pssm-ID: 319917 [Multi-domain]  Cd Length: 120  Bit Score: 35.52  E-value: 2.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806   7 HLGIAVKSLETSDSLFAKLIGREAYKmeeveregVKTSF--YQIGESKIELLESTREdspiskfiEKKGEGVHHIAFGVD 84
Cdd:cd07254    4 HLSLNVTDLERSIRFYSDLFGAEPAK--------RKADYakFMLEDPPLNLALLVND--------RKEPYGLNHLGIQVD 67

                         90       100
                 ....*....|....*....|..
gi 895953806  85 D---IYAEIERLKKEGFEFISE 103
Cdd:cd07254   68 SkeeVAALKARAEAAGLPVRKE 89
PcpA_C_like cd08347
C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 10-129 6.22e-03

C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins; The C-terminal domain of Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins. PcpA is a key enzyme in the pentachlorophenol (PCP) degradation pathway, catalyzing the conversion of 2,6-dichloro-p-hydroquinone to 2-chloromaleylacetate. This domain belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases.


Pssm-ID: 319935  Cd Length: 157  Bit Score: 34.91  E-value: 6.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 895953806  10 IAVKSLETSDSLFakligREAYKMEEVEREGVKTSFYQIGE---SKIELLESTREDSpiskfiEKKGEG-VHHIAFGVDD 85
Cdd:cd08347    7 LTVREPEETDAFL-----TNVFGFTEVGEEGDLVRLFAGGNgsgGVVDVLDDPDLPS------AQQGYGtVHHVAFRVAD 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 895953806  86 IYAE---IERLKKEGFEFisEEPKDGADNKIVVFLHPkstNGVLIEL 129
Cdd:cd08347   76 DEEQaawKERLEELGFDN--SGIVDRFYFESLYFREP---GGVLFEI 117
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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