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Conserved domains on  [gi|822525302|ref|WP_046955216|]
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MULTISPECIES: methylglyoxal synthase [Bacillus]

Protein Classification

methylglyoxal synthase( domain architecture ID 10012278)

methylglyoxal synthase catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to produce methylglyoxal

CATH:  3.40.50.1380
EC:  4.2.3.3
Gene Ontology:  GO:0008929|GO:0019242
PubMed:  15049687
SCOP:  4003765

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
mgsA PRK05234
methylglyoxal synthase; Validated
 1-128 1.08e-82

methylglyoxal synthase; Validated


:

Pssm-ID: 179969 [Multi-domain]  Cd Length: 142  Bit Score: 238.58  E-value: 1.08e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525302   1 MKIALIAHDKKKDDMVSFAYAYKPIFEQHELFATGTTGLRIMEATGLVVTRFQSGPLGGDQEIGAMIAKNDMDMVIFFRD 80
Cdd:PRK05234   5 KRIALIAHDHKKDDLVAWVKAHKDLLEQHELYATGTTGGLIQEATGLDVTRLLSGPLGGDQQIGALIAEGKIDMLIFFRD 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 822525302  81 PLTAQPHEPDVNALLRLCDVYAIPLATNMASAEMLMHALERgDLDYRK 128
Cdd:PRK05234  85 PLTAQPHDPDVKALLRLADVWNIPVATNRATADFLISSLLF-DDEVEI 131
 
Name Accession Description Interval E-value
mgsA PRK05234
methylglyoxal synthase; Validated
 1-128 1.08e-82

methylglyoxal synthase; Validated


Pssm-ID: 179969 [Multi-domain]  Cd Length: 142  Bit Score: 238.58  E-value: 1.08e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525302   1 MKIALIAHDKKKDDMVSFAYAYKPIFEQHELFATGTTGLRIMEATGLVVTRFQSGPLGGDQEIGAMIAKNDMDMVIFFRD 80
Cdd:PRK05234   5 KRIALIAHDHKKDDLVAWVKAHKDLLEQHELYATGTTGGLIQEATGLDVTRLLSGPLGGDQQIGALIAEGKIDMLIFFRD 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 822525302  81 PLTAQPHEPDVNALLRLCDVYAIPLATNMASAEMLMHALERgDLDYRK 128
Cdd:PRK05234  85 PLTAQPHDPDVKALLRLADVWNIPVATNRATADFLISSLLF-DDEVEI 131
MgsA COG1803
Methylglyoxal synthase [Carbohydrate transport and metabolism];
1-122 5.47e-82

Methylglyoxal synthase [Carbohydrate transport and metabolism];


Pssm-ID: 441408  Cd Length: 122  Bit Score: 236.15  E-value: 5.47e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525302   1 MKIALIAHDKKKDDMVSFAYAYKPIFEQHELFATGTTGLRIMEATGLVVTRFQSGPLGGDQEIGAMIAKNDMDMVIFFRD 80
Cdd:COG1803    1 MTIALIAHDNKKDDLVEFAKAHKDILSKHELVATGTTGKLIEEATGLEVTRLLSGPLGGDQQIGALIAEGEIDAVIFFRD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 822525302  81 PLTAQPHEPDVNALLRLCDVYAIPLATNMASAEMLMHALERG 122
Cdd:COG1803   81 PLTAQPHEPDVKALLRLCDVHNIPLATNLATAELLITSLLRG 122
MGS cd01422
Methylglyoxal synthase catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to ...
 2-116 4.87e-66

Methylglyoxal synthase catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to produce methylglyoxal. The first part of the catalytic mechanism is believed to be similar to TIM (triosephosphate isomerase) in that both enzymes utilize DHAP to form an ene-diolate phosphate intermediate. In MGS, the second catalytic step is characterized by the elimination of phosphate and collapse of the enediolate to form methylglyoxal instead of reprotonation to form the isomer glyceraldehyde 3-phosphate, as in TIM. This is the first reaction in the methylglyoxal bypass of the Embden-Myerhoff glycolytic pathway and is believed to provide physiological benefits under non-ideal growth conditions in bacteria.


Pssm-ID: 238710  Cd Length: 115  Bit Score: 195.54  E-value: 4.87e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525302   2 KIALIAHDKKKDDMVSFAYAYKPIFEQHELFATGTTGLRIMEATGLVVTRFQSGPLGGDQEIGAMIAKNDMDMVIFFRDP 81
Cdd:cd01422    1 RIALIAHDNKKEDLVEFVKQHQELLSRHRLVATGTTGLLIQEATGLTVNRMKSGPLGGDQQIGALIAEGEIDAVIFFRDP 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 822525302  82 LTAQPHEPDVNALLRLCDVYAIPLATNMASAEMLM 116
Cdd:cd01422   81 LTAQPHEPDVKALLRLCDVYNIPLATNRSTADAII 115
MGSA TIGR00160
methylglyoxal synthase; Methylglyoxal synthase (MGS) generates methylglyoxal (MG), a toxic ...
 1-130 3.36e-65

methylglyoxal synthase; Methylglyoxal synthase (MGS) generates methylglyoxal (MG), a toxic metabolite (that may also be a regulatory metabolite and) that is detoxified, prinicipally, through a pathway involving glutathione and glyoxylase I. Totemeyer et al. propose that, during a loss of control over carbon flux, with accumulation of phosphorylated sugars and depletion of phosphate, as might happen during a rapid shift to a richer medium, MGS aids the cell by converting some dihydroxyacetone phosphate (DHAP) to MG and phosphate. This is therefore an alternative to triosephosphate isomerase and the remainder of the glycolytic pathway for the disposal of DHAP during the stress of a sudden increase in available sugars. [Energy metabolism, Other]


Pssm-ID: 272935  Cd Length: 143  Bit Score: 194.24  E-value: 3.36e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525302    1 MKIALIAHDKKKDDMVSFAYAYKPIFEQHELFATGTTGLRIMEATGLVVTRFQSGPLGGDQEIGAMIAKNDMDMVIFFRD 80
Cdd:TIGR00160   3 KHIALIAHDKKKQDLVNFVQQHKPLLSQHDLYATGTTGNLISRATGLNINAMLSGPMGGDQQIGALIAEGKIDAVIFFWD 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 822525302   81 PLTAQPHEPDVNALLRLCDVYAIPLATNMASAEMLM---HALERGDLDYRKFR 130
Cdd:TIGR00160  83 PLNAQPHEPDVKALLRLCTVWNIPLATNVATADFLIkspHFNDAVDILIPDYQ 135
MGS pfam02142
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 14-107 3.18e-22

MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.


Pssm-ID: 460462 [Multi-domain]  Cd Length: 93  Bit Score: 83.69  E-value: 3.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525302   14 DMVSFAYAYKPIFeqHELFATGTTGLRIMEAtGL----VVTRFQSGPLGGDQEIGAMIAKNDMDMVIFFRDPLTAQPHep 89
Cdd:pfam02142   1 GLVELAKALVELG--FELLATGGTAKFLREA-GIpvteVVEKTGEGRPGGRVQIGDLIKNGEIDLVINTLYPFKATVH-- 75

                          90
                  ....*....|....*...
gi 822525302   90 DVNALLRLCDVYAIPLAT 107
Cdd:pfam02142  76 DGYAIRRAAENIDIPGPT 93
MGS smart00851
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 14-107 1.31e-20

MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.


Pssm-ID: 214855 [Multi-domain]  Cd Length: 91  Bit Score: 79.44  E-value: 1.31e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525302    14 DMVSFAYAYKPIfeQHELFATGTTGlRIMEATGLVVTRFQSGPLGGDQE-IGAMIAKNDMDMVIFFRDPLTAQPHEpDVN 92
Cdd:smart00851   1 GLVEFAKRLAEL--GFELLATGGTA-KFLREAGLPVVKTLHPKVHGGIPqILDLIKNGEIDLVINTLYPFEAQAHE-DGY 76

                           90
                   ....*....|....*
gi 822525302    93 ALLRLCDVYAIPLAT 107
Cdd:smart00851  77 SIRRAAENIDIPGPT 91
 
Name Accession Description Interval E-value
mgsA PRK05234
methylglyoxal synthase; Validated
 1-128 1.08e-82

methylglyoxal synthase; Validated


Pssm-ID: 179969 [Multi-domain]  Cd Length: 142  Bit Score: 238.58  E-value: 1.08e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525302   1 MKIALIAHDKKKDDMVSFAYAYKPIFEQHELFATGTTGLRIMEATGLVVTRFQSGPLGGDQEIGAMIAKNDMDMVIFFRD 80
Cdd:PRK05234   5 KRIALIAHDHKKDDLVAWVKAHKDLLEQHELYATGTTGGLIQEATGLDVTRLLSGPLGGDQQIGALIAEGKIDMLIFFRD 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 822525302  81 PLTAQPHEPDVNALLRLCDVYAIPLATNMASAEMLMHALERgDLDYRK 128
Cdd:PRK05234  85 PLTAQPHDPDVKALLRLADVWNIPVATNRATADFLISSLLF-DDEVEI 131
MgsA COG1803
Methylglyoxal synthase [Carbohydrate transport and metabolism];
1-122 5.47e-82

Methylglyoxal synthase [Carbohydrate transport and metabolism];


Pssm-ID: 441408  Cd Length: 122  Bit Score: 236.15  E-value: 5.47e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525302   1 MKIALIAHDKKKDDMVSFAYAYKPIFEQHELFATGTTGLRIMEATGLVVTRFQSGPLGGDQEIGAMIAKNDMDMVIFFRD 80
Cdd:COG1803    1 MTIALIAHDNKKDDLVEFAKAHKDILSKHELVATGTTGKLIEEATGLEVTRLLSGPLGGDQQIGALIAEGEIDAVIFFRD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 822525302  81 PLTAQPHEPDVNALLRLCDVYAIPLATNMASAEMLMHALERG 122
Cdd:COG1803   81 PLTAQPHEPDVKALLRLCDVHNIPLATNLATAELLITSLLRG 122
MGS cd01422
Methylglyoxal synthase catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to ...
 2-116 4.87e-66

Methylglyoxal synthase catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to produce methylglyoxal. The first part of the catalytic mechanism is believed to be similar to TIM (triosephosphate isomerase) in that both enzymes utilize DHAP to form an ene-diolate phosphate intermediate. In MGS, the second catalytic step is characterized by the elimination of phosphate and collapse of the enediolate to form methylglyoxal instead of reprotonation to form the isomer glyceraldehyde 3-phosphate, as in TIM. This is the first reaction in the methylglyoxal bypass of the Embden-Myerhoff glycolytic pathway and is believed to provide physiological benefits under non-ideal growth conditions in bacteria.


Pssm-ID: 238710  Cd Length: 115  Bit Score: 195.54  E-value: 4.87e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525302   2 KIALIAHDKKKDDMVSFAYAYKPIFEQHELFATGTTGLRIMEATGLVVTRFQSGPLGGDQEIGAMIAKNDMDMVIFFRDP 81
Cdd:cd01422    1 RIALIAHDNKKEDLVEFVKQHQELLSRHRLVATGTTGLLIQEATGLTVNRMKSGPLGGDQQIGALIAEGEIDAVIFFRDP 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 822525302  82 LTAQPHEPDVNALLRLCDVYAIPLATNMASAEMLM 116
Cdd:cd01422   81 LTAQPHEPDVKALLRLCDVYNIPLATNRSTADAII 115
MGSA TIGR00160
methylglyoxal synthase; Methylglyoxal synthase (MGS) generates methylglyoxal (MG), a toxic ...
 1-130 3.36e-65

methylglyoxal synthase; Methylglyoxal synthase (MGS) generates methylglyoxal (MG), a toxic metabolite (that may also be a regulatory metabolite and) that is detoxified, prinicipally, through a pathway involving glutathione and glyoxylase I. Totemeyer et al. propose that, during a loss of control over carbon flux, with accumulation of phosphorylated sugars and depletion of phosphate, as might happen during a rapid shift to a richer medium, MGS aids the cell by converting some dihydroxyacetone phosphate (DHAP) to MG and phosphate. This is therefore an alternative to triosephosphate isomerase and the remainder of the glycolytic pathway for the disposal of DHAP during the stress of a sudden increase in available sugars. [Energy metabolism, Other]


Pssm-ID: 272935  Cd Length: 143  Bit Score: 194.24  E-value: 3.36e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525302    1 MKIALIAHDKKKDDMVSFAYAYKPIFEQHELFATGTTGLRIMEATGLVVTRFQSGPLGGDQEIGAMIAKNDMDMVIFFRD 80
Cdd:TIGR00160   3 KHIALIAHDKKKQDLVNFVQQHKPLLSQHDLYATGTTGNLISRATGLNINAMLSGPMGGDQQIGALIAEGKIDAVIFFWD 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 822525302   81 PLTAQPHEPDVNALLRLCDVYAIPLATNMASAEMLM---HALERGDLDYRKFR 130
Cdd:TIGR00160  83 PLNAQPHEPDVKALLRLCTVWNIPLATNVATADFLIkspHFNDAVDILIPDYQ 135
MGS pfam02142
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 14-107 3.18e-22

MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.


Pssm-ID: 460462 [Multi-domain]  Cd Length: 93  Bit Score: 83.69  E-value: 3.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525302   14 DMVSFAYAYKPIFeqHELFATGTTGLRIMEAtGL----VVTRFQSGPLGGDQEIGAMIAKNDMDMVIFFRDPLTAQPHep 89
Cdd:pfam02142   1 GLVELAKALVELG--FELLATGGTAKFLREA-GIpvteVVEKTGEGRPGGRVQIGDLIKNGEIDLVINTLYPFKATVH-- 75

                          90
                  ....*....|....*...
gi 822525302   90 DVNALLRLCDVYAIPLAT 107
Cdd:pfam02142  76 DGYAIRRAAENIDIPGPT 93
MGS-like cd00532
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ...
 3-112 1.77e-21

MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to produce methylglyoxal. The family also includes the C-terminal domain in carbamoyl phosphate synthetase (CPS) where it catalyzes the last phosphorylation of a coaboxyphosphate intermediate to form the product carbamoyl phosphate and may also play a regulatory role. This family also includes inosine monophosphate cyclohydrolase. The known structures in this family show a common phosphate binding site.


Pssm-ID: 238297 [Multi-domain]  Cd Length: 112  Bit Score: 82.56  E-value: 1.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525302   3 IALIAHDKKKDDMVSFAYAYKPifEQHELFATGTTGlRIMEATGLVVTRFQSGPLGGDQEIGAMIA-KNDMDMVIFFRDP 81
Cdd:cd00532    2 VFLSVSDHVKAMLVDLAPKLSS--DGFPLFATGGTS-RVLADAGIPVRAVSKRHEDGEPTVDAAIAeKGKFDVVINLRDP 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 822525302  82 LTAQPHEPDVNALLRLCDVYAIPLATNMASA 112
Cdd:cd00532   79 RRDRCTDEDGTALLRLARLYKIPVTTPNATA 109
MGS smart00851
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 14-107 1.31e-20

MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.


Pssm-ID: 214855 [Multi-domain]  Cd Length: 91  Bit Score: 79.44  E-value: 1.31e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822525302    14 DMVSFAYAYKPIfeQHELFATGTTGlRIMEATGLVVTRFQSGPLGGDQE-IGAMIAKNDMDMVIFFRDPLTAQPHEpDVN 92
Cdd:smart00851   1 GLVEFAKRLAEL--GFELLATGGTA-KFLREAGLPVVKTLHPKVHGGIPqILDLIKNGEIDLVINTLYPFEAQAHE-DGY 76

                           90
                   ....*....|....*
gi 822525302    93 ALLRLCDVYAIPLAT 107
Cdd:smart00851  77 SIRRAAENIDIPGPT 91
 
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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