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Conserved domains on  [gi|446346332|ref|WP_000424187|]
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MULTISPECIES: methylglyoxal synthase [Salmonella]

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
 8-149 4.63e-98

methylglyoxal synthase; Validated


:

Pssm-ID: 179969 [Multi-domain]  Cd Length: 142  Bit Score: 278.25  E-value: 4.63e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346332   8 LPTRKHIALVAHDHCKQMLMNWVERHQPLLEKHVLYATGTTGNLIQRATGMDVNAMLSGPMGGDQQVGALISEGKIDVLI 87
Cdd:PRK05234   1 MPARKRIALIAHDHKKDDLVAWVKAHKDLLEQHELYATGTTGGLIQEATGLDVTRLLSGPLGGDQQIGALIAEGKIDMLI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446346332  88 FFWDPLNAVPHDPDVKALLRLATVWNIPVATNVSTADFIIQSPHFNDAVDILIPDYARYLAE 149
Cdd:PRK05234  81 FFRDPLTAQPHDPDVKALLRLADVWNIPVATNRATADFLISSLLFDDEVEILIPDYQRYLAE 142
 
Name Accession Description Interval E-value
mgsA PRK05234
methylglyoxal synthase; Validated
 8-149 4.63e-98

methylglyoxal synthase; Validated


Pssm-ID: 179969 [Multi-domain]  Cd Length: 142  Bit Score: 278.25  E-value: 4.63e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346332   8 LPTRKHIALVAHDHCKQMLMNWVERHQPLLEKHVLYATGTTGNLIQRATGMDVNAMLSGPMGGDQQVGALISEGKIDVLI 87
Cdd:PRK05234   1 MPARKRIALIAHDHKKDDLVAWVKAHKDLLEQHELYATGTTGGLIQEATGLDVTRLLSGPLGGDQQIGALIAEGKIDMLI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446346332  88 FFWDPLNAVPHDPDVKALLRLATVWNIPVATNVSTADFIIQSPHFNDAVDILIPDYARYLAE 149
Cdd:PRK05234  81 FFRDPLTAQPHDPDVKALLRLADVWNIPVATNRATADFLISSLLFDDEVEILIPDYQRYLAE 142
MGSA TIGR00160
methylglyoxal synthase; Methylglyoxal synthase (MGS) generates methylglyoxal (MG), a toxic ...
 11-152 8.65e-93

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: 265.12  E-value: 8.65e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346332   11 RKHIALVAHDHCKQMLMNWVERHQPLLEKHVLYATGTTGNLIQRATGMDVNAMLSGPMGGDQQVGALISEGKIDVLIFFW 90
Cdd:TIGR00160   2 RKHIALIAHDKKKQDLVNFVQQHKPLLSQHDLYATGTTGNLISRATGLNINAMLSGPMGGDQQIGALIAEGKIDAVIFFW 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446346332   91 DPLNAVPHDPDVKALLRLATVWNIPVATNVSTADFIIQSPHFNDAVDILIPDYARYLAERLK 152
Cdd:TIGR00160  82 DPLNAQPHEPDVKALLRLCTVWNIPLATNVATADFLIKSPHFNDAVDILIPDYQGYLADRLK 143
MgsA COG1803
Methylglyoxal synthase [Carbohydrate transport and metabolism];
12-133 1.28e-76

Methylglyoxal synthase [Carbohydrate transport and metabolism];


Pssm-ID: 441408  Cd Length: 122  Bit Score: 223.44  E-value: 1.28e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346332  12 KHIALVAHDHCKQMLMNWVERHQPLLEKHVLYATGTTGNLIQRATGMDVNAMLSGPMGGDQQVGALISEGKIDVLIFFWD 91
Cdd:COG1803    1 MTIALIAHDNKKDDLVEFAKAHKDILSKHELVATGTTGKLIEEATGLEVTRLLSGPLGGDQQIGALIAEGEIDAVIFFRD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446346332  92 PLNAVPHDPDVKALLRLATVWNIPVATNVSTADFIIQSPHFN 133
Cdd:COG1803   81 PLTAQPHEPDVKALLRLCDVHNIPLATNLATAELLITSLLRG 122
MGS cd01422
Methylglyoxal synthase catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to ...
 13-127 6.40e-70

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: 206.32  E-value: 6.40e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346332  13 HIALVAHDHCKQMLMNWVERHQPLLEKHVLYATGTTGNLIQRATGMDVNAMLSGPMGGDQQVGALISEGKIDVLIFFWDP 92
Cdd:cd01422    1 RIALIAHDNKKEDLVEFVKQHQELLSRHRLVATGTTGLLIQEATGLTVNRMKSGPLGGDQQIGALIAEGEIDAVIFFRDP 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446346332  93 LNAVPHDPDVKALLRLATVWNIPVATNVSTADFII 127
Cdd:cd01422   81 LTAQPHEPDVKALLRLCDVYNIPLATNRSTADAII 115
MGS pfam02142
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 26-118 2.10e-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: 84.85  E-value: 2.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346332   26 LMNWVERHQPLLekHVLYATGTTGNLIQrATGMDV----NAMLSGPMGGDQQVGALISEGKIDVLIFFWDPLNAVPHdpD 101
Cdd:pfam02142   2 LVELAKALVELG--FELLATGGTAKFLR-EAGIPVtevvEKTGEGRPGGRVQIGDLIKNGEIDLVINTLYPFKATVH--D 76

                          90
                  ....*....|....*..
gi 446346332  102 VKALLRLATVWNIPVAT 118
Cdd:pfam02142  77 GYAIRRAAENIDIPGPT 93
MGS smart00851
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 26-118 1.25e-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: 80.21  E-value: 1.25e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346332    26 LMNWVERHQPLleKHVLYATGTTGNLIqRATGMDVNAMLSGPMGGDQ-QVGALISEGKIDVLIFFWDPLNAVPHDpDVKA 104
Cdd:smart00851   2 LVEFAKRLAEL--GFELLATGGTAKFL-REAGLPVVKTLHPKVHGGIpQILDLIKNGEIDLVINTLYPFEAQAHE-DGYS 77

                           90
                   ....*....|....
gi 446346332   105 LLRLATVWNIPVAT 118
Cdd:smart00851  78 IRRAAENIDIPGPT 91
 
Name Accession Description Interval E-value
mgsA PRK05234
methylglyoxal synthase; Validated
 8-149 4.63e-98

methylglyoxal synthase; Validated


Pssm-ID: 179969 [Multi-domain]  Cd Length: 142  Bit Score: 278.25  E-value: 4.63e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346332   8 LPTRKHIALVAHDHCKQMLMNWVERHQPLLEKHVLYATGTTGNLIQRATGMDVNAMLSGPMGGDQQVGALISEGKIDVLI 87
Cdd:PRK05234   1 MPARKRIALIAHDHKKDDLVAWVKAHKDLLEQHELYATGTTGGLIQEATGLDVTRLLSGPLGGDQQIGALIAEGKIDMLI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446346332  88 FFWDPLNAVPHDPDVKALLRLATVWNIPVATNVSTADFIIQSPHFNDAVDILIPDYARYLAE 149
Cdd:PRK05234  81 FFRDPLTAQPHDPDVKALLRLADVWNIPVATNRATADFLISSLLFDDEVEILIPDYQRYLAE 142
MGSA TIGR00160
methylglyoxal synthase; Methylglyoxal synthase (MGS) generates methylglyoxal (MG), a toxic ...
 11-152 8.65e-93

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: 265.12  E-value: 8.65e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346332   11 RKHIALVAHDHCKQMLMNWVERHQPLLEKHVLYATGTTGNLIQRATGMDVNAMLSGPMGGDQQVGALISEGKIDVLIFFW 90
Cdd:TIGR00160   2 RKHIALIAHDKKKQDLVNFVQQHKPLLSQHDLYATGTTGNLISRATGLNINAMLSGPMGGDQQIGALIAEGKIDAVIFFW 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446346332   91 DPLNAVPHDPDVKALLRLATVWNIPVATNVSTADFIIQSPHFNDAVDILIPDYARYLAERLK 152
Cdd:TIGR00160  82 DPLNAQPHEPDVKALLRLCTVWNIPLATNVATADFLIKSPHFNDAVDILIPDYQGYLADRLK 143
MgsA COG1803
Methylglyoxal synthase [Carbohydrate transport and metabolism];
12-133 1.28e-76

Methylglyoxal synthase [Carbohydrate transport and metabolism];


Pssm-ID: 441408  Cd Length: 122  Bit Score: 223.44  E-value: 1.28e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346332  12 KHIALVAHDHCKQMLMNWVERHQPLLEKHVLYATGTTGNLIQRATGMDVNAMLSGPMGGDQQVGALISEGKIDVLIFFWD 91
Cdd:COG1803    1 MTIALIAHDNKKDDLVEFAKAHKDILSKHELVATGTTGKLIEEATGLEVTRLLSGPLGGDQQIGALIAEGEIDAVIFFRD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446346332  92 PLNAVPHDPDVKALLRLATVWNIPVATNVSTADFIIQSPHFN 133
Cdd:COG1803   81 PLTAQPHEPDVKALLRLCDVHNIPLATNLATAELLITSLLRG 122
MGS cd01422
Methylglyoxal synthase catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to ...
 13-127 6.40e-70

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: 206.32  E-value: 6.40e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346332  13 HIALVAHDHCKQMLMNWVERHQPLLEKHVLYATGTTGNLIQRATGMDVNAMLSGPMGGDQQVGALISEGKIDVLIFFWDP 92
Cdd:cd01422    1 RIALIAHDNKKEDLVEFVKQHQELLSRHRLVATGTTGLLIQEATGLTVNRMKSGPLGGDQQIGALIAEGEIDAVIFFRDP 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446346332  93 LNAVPHDPDVKALLRLATVWNIPVATNVSTADFII 127
Cdd:cd01422   81 LTAQPHEPDVKALLRLCDVYNIPLATNRSTADAII 115
MGS-like cd00532
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ...
 13-126 1.27e-43

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: 139.57  E-value: 1.27e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346332  13 HIALVAHDHCKQMLMNWVERHQplLEKHVLYATGTTGNLIQRAtGMDVNAMLSGPMGGDQQVGALISE-GKIDVLIFFWD 91
Cdd:cd00532    1 GVFLSVSDHVKAMLVDLAPKLS--SDGFPLFATGGTSRVLADA-GIPVRAVSKRHEDGEPTVDAAIAEkGKFDVVINLRD 77

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446346332  92 PLNAVPHDPDVKALLRLATVWNIPVATNVSTADFI 126
Cdd:cd00532   78 PRRDRCTDEDGTALLRLARLYKIPVTTPNATAMFV 112
MGS pfam02142
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 26-118 2.10e-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: 84.85  E-value: 2.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346332   26 LMNWVERHQPLLekHVLYATGTTGNLIQrATGMDV----NAMLSGPMGGDQQVGALISEGKIDVLIFFWDPLNAVPHdpD 101
Cdd:pfam02142   2 LVELAKALVELG--FELLATGGTAKFLR-EAGIPVtevvEKTGEGRPGGRVQIGDLIKNGEIDLVINTLYPFKATVH--D 76

                          90
                  ....*....|....*..
gi 446346332  102 VKALLRLATVWNIPVAT 118
Cdd:pfam02142  77 GYAIRRAAENIDIPGPT 93
MGS smart00851
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 26-118 1.25e-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: 80.21  E-value: 1.25e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346332    26 LMNWVERHQPLleKHVLYATGTTGNLIqRATGMDVNAMLSGPMGGDQ-QVGALISEGKIDVLIFFWDPLNAVPHDpDVKA 104
Cdd:smart00851   2 LVEFAKRLAEL--GFELLATGGTAKFL-REAGLPVVKTLHPKVHGGIpQILDLIKNGEIDLVINTLYPFEAQAHE-DGYS 77

                           90
                   ....*....|....
gi 446346332   105 LLRLATVWNIPVAT 118
Cdd:smart00851  78 IRRAAENIDIPGPT 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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