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Conserved domains on  [gi|525964238|ref|WP_020831077|]
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methylglyoxal synthase [Mannheimia haemolytica]

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 4.69e-89

methylglyoxal synthase; Validated


:

Pssm-ID: 179969 [Multi-domain]  Cd Length: 142  Bit Score: 255.53  E-value: 4.69e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525964238   8 IAKQKQIALVAHDSCKQDLIRWTQTHQAQLASHKLYATGTTGHLLARETGLEITSLLSGPMGGDQQLGGLIAEKKIDLLV 87
Cdd:PRK05234   1 MPARKRIALIAHDHKKDDLVAWVKAHKDLLEQHELYATGTTGGLIQEATGLDVTRLLSGPLGGDQQIGALIAEGKIDMLI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525964238  88 FFWDPMNAAPHDPDVKALMRIATVWNIPVAINETTANFLLNADLFHQEVSVNVPDYDGYLAE 149
Cdd:PRK05234  81 FFRDPLTAQPHDPDVKALLRLADVWNIPVATNRATADFLISSLLFDDEVEILIPDYQRYLAE 142
 
Name Accession Description Interval E-value
mgsA PRK05234
methylglyoxal synthase; Validated
 8-149 4.69e-89

methylglyoxal synthase; Validated


Pssm-ID: 179969 [Multi-domain]  Cd Length: 142  Bit Score: 255.53  E-value: 4.69e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525964238   8 IAKQKQIALVAHDSCKQDLIRWTQTHQAQLASHKLYATGTTGHLLARETGLEITSLLSGPMGGDQQLGGLIAEKKIDLLV 87
Cdd:PRK05234   1 MPARKRIALIAHDHKKDDLVAWVKAHKDLLEQHELYATGTTGGLIQEATGLDVTRLLSGPLGGDQQIGALIAEGKIDMLI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525964238  88 FFWDPMNAAPHDPDVKALMRIATVWNIPVAINETTANFLLNADLFHQEVSVNVPDYDGYLAE 149
Cdd:PRK05234  81 FFRDPLTAQPHDPDVKALLRLADVWNIPVATNRATADFLISSLLFDDEVEILIPDYQRYLAE 142
MGSA TIGR00160
methylglyoxal synthase; Methylglyoxal synthase (MGS) generates methylglyoxal (MG), a toxic ...
 11-151 2.58e-75

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: 220.82  E-value: 2.58e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525964238   11 QKQIALVAHDSCKQDLIRWTQTHQAQLASHKLYATGTTGHLLARETGLEITSLLSGPMGGDQQLGGLIAEKKIDLLVFFW 90
Cdd:TIGR00160   2 RKHIALIAHDKKKQDLVNFVQQHKPLLSQHDLYATGTTGNLISRATGLNINAMLSGPMGGDQQIGALIAEGKIDAVIFFW 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525964238   91 DPMNAAPHDPDVKALMRIATVWNIPVAINETTANFLLNADLFHQEVSVNVPDYDGYLAERL 151
Cdd:TIGR00160  82 DPLNAQPHEPDVKALLRLCTVWNIPLATNVATADFLIKSPHFNDAVDILIPDYQGYLADRL 142
MgsA COG1803
Methylglyoxal synthase [Carbohydrate transport and metabolism];
12-133 1.50e-69

Methylglyoxal synthase [Carbohydrate transport and metabolism];


Pssm-ID: 441408  Cd Length: 122  Bit Score: 205.33  E-value: 1.50e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525964238  12 KQIALVAHDSCKQDLIRWTQTHQAQLASHKLYATGTTGHLLARETGLEITSLLSGPMGGDQQLGGLIAEKKIDLLVFFWD 91
Cdd:COG1803    1 MTIALIAHDNKKDDLVEFAKAHKDILSKHELVATGTTGKLIEEATGLEVTRLLSGPLGGDQQIGALIAEGEIDAVIFFRD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 525964238  92 PMNAAPHDPDVKALMRIATVWNIPVAINETTANFLLNADLFH 133
Cdd:COG1803   81 PLTAQPHEPDVKALLRLCDVHNIPLATNLATAELLITSLLRG 122
MGS cd01422
Methylglyoxal synthase catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to ...
 14-127 2.44e-58

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: 177.05  E-value: 2.44e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525964238  14 IALVAHDSCKQDLIRWTQTHQAQLASHKLYATGTTGHLLARETGLEITSLLSGPMGGDQQLGGLIAEKKIDLLVFFWDPM 93
Cdd:cd01422    2 IALIAHDNKKEDLVEFVKQHQELLSRHRLVATGTTGLLIQEATGLTVNRMKSGPLGGDQQIGALIAEGEIDAVIFFRDPL 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 525964238  94 NAAPHDPDVKALMRIATVWNIPVAINETTANFLL 127
Cdd:cd01422   82 TAQPHEPDVKALLRLCDVYNIPLATNRSTADAII 115
MGS pfam02142
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 25-117 2.61e-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: 2.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525964238   25 DLIRWTQTHQAQLasHKLYATGTTGHLLaRETGLEITSL----LSGPMGGDQQLGGLIAEKKIDLLVFFWDPMNAAPHdp 100
Cdd:pfam02142   1 GLVELAKALVELG--FELLATGGTAKFL-REAGIPVTEVvektGEGRPGGRVQIGDLIKNGEIDLVINTLYPFKATVH-- 75

                          90
                  ....*....|....*..
gi 525964238  101 DVKALMRIATVWNIPVA 117
Cdd:pfam02142  76 DGYAIRRAAENIDIPGP 92
MGS smart00851
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 40-117 2.73e-19

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: 76.74  E-value: 2.73e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525964238    40 HKLYATGTTGHLLaRETGLEITSLLSGPMGGDQ-QLGGLIAEKKIDLLVFFWDPMNAAPHDpDVKALMRIATVWNIPVA 117
Cdd:smart00851  14 FELLATGGTAKFL-REAGLPVVKTLHPKVHGGIpQILDLIKNGEIDLVINTLYPFEAQAHE-DGYSIRRAAENIDIPGP 90
 
Name Accession Description Interval E-value
mgsA PRK05234
methylglyoxal synthase; Validated
 8-149 4.69e-89

methylglyoxal synthase; Validated


Pssm-ID: 179969 [Multi-domain]  Cd Length: 142  Bit Score: 255.53  E-value: 4.69e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525964238   8 IAKQKQIALVAHDSCKQDLIRWTQTHQAQLASHKLYATGTTGHLLARETGLEITSLLSGPMGGDQQLGGLIAEKKIDLLV 87
Cdd:PRK05234   1 MPARKRIALIAHDHKKDDLVAWVKAHKDLLEQHELYATGTTGGLIQEATGLDVTRLLSGPLGGDQQIGALIAEGKIDMLI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525964238  88 FFWDPMNAAPHDPDVKALMRIATVWNIPVAINETTANFLLNADLFHQEVSVNVPDYDGYLAE 149
Cdd:PRK05234  81 FFRDPLTAQPHDPDVKALLRLADVWNIPVATNRATADFLISSLLFDDEVEILIPDYQRYLAE 142
MGSA TIGR00160
methylglyoxal synthase; Methylglyoxal synthase (MGS) generates methylglyoxal (MG), a toxic ...
 11-151 2.58e-75

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: 220.82  E-value: 2.58e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525964238   11 QKQIALVAHDSCKQDLIRWTQTHQAQLASHKLYATGTTGHLLARETGLEITSLLSGPMGGDQQLGGLIAEKKIDLLVFFW 90
Cdd:TIGR00160   2 RKHIALIAHDKKKQDLVNFVQQHKPLLSQHDLYATGTTGNLISRATGLNINAMLSGPMGGDQQIGALIAEGKIDAVIFFW 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525964238   91 DPMNAAPHDPDVKALMRIATVWNIPVAINETTANFLLNADLFHQEVSVNVPDYDGYLAERL 151
Cdd:TIGR00160  82 DPLNAQPHEPDVKALLRLCTVWNIPLATNVATADFLIKSPHFNDAVDILIPDYQGYLADRL 142
MgsA COG1803
Methylglyoxal synthase [Carbohydrate transport and metabolism];
12-133 1.50e-69

Methylglyoxal synthase [Carbohydrate transport and metabolism];


Pssm-ID: 441408  Cd Length: 122  Bit Score: 205.33  E-value: 1.50e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525964238  12 KQIALVAHDSCKQDLIRWTQTHQAQLASHKLYATGTTGHLLARETGLEITSLLSGPMGGDQQLGGLIAEKKIDLLVFFWD 91
Cdd:COG1803    1 MTIALIAHDNKKDDLVEFAKAHKDILSKHELVATGTTGKLIEEATGLEVTRLLSGPLGGDQQIGALIAEGEIDAVIFFRD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 525964238  92 PMNAAPHDPDVKALMRIATVWNIPVAINETTANFLLNADLFH 133
Cdd:COG1803   81 PLTAQPHEPDVKALLRLCDVHNIPLATNLATAELLITSLLRG 122
MGS cd01422
Methylglyoxal synthase catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to ...
 14-127 2.44e-58

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: 177.05  E-value: 2.44e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525964238  14 IALVAHDSCKQDLIRWTQTHQAQLASHKLYATGTTGHLLARETGLEITSLLSGPMGGDQQLGGLIAEKKIDLLVFFWDPM 93
Cdd:cd01422    2 IALIAHDNKKEDLVEFVKQHQELLSRHRLVATGTTGLLIQEATGLTVNRMKSGPLGGDQQIGALIAEGEIDAVIFFRDPL 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 525964238  94 NAAPHDPDVKALMRIATVWNIPVAINETTANFLL 127
Cdd:cd01422   82 TAQPHEPDVKALLRLCDVYNIPLATNRSTADAII 115
MGS-like cd00532
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ...
 14-125 1.02e-31

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: 109.52  E-value: 1.02e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525964238  14 IALVAHDSCKQDLIRWTQTHQAQlaSHKLYATGTTGHLLaRETGLEITSLLSGPMGGDQQLGGLIAEK-KIDLLVFFWDP 92
Cdd:cd00532    2 VFLSVSDHVKAMLVDLAPKLSSD--GFPLFATGGTSRVL-ADAGIPVRAVSKRHEDGEPTVDAAIAEKgKFDVVINLRDP 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 525964238  93 MNAAPHDPDVKALMRIATVWNIPVAINETTANF 125
Cdd:cd00532   79 RRDRCTDEDGTALLRLARLYKIPVTTPNATAMF 111
MGS pfam02142
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 25-117 2.61e-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: 2.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525964238   25 DLIRWTQTHQAQLasHKLYATGTTGHLLaRETGLEITSL----LSGPMGGDQQLGGLIAEKKIDLLVFFWDPMNAAPHdp 100
Cdd:pfam02142   1 GLVELAKALVELG--FELLATGGTAKFL-REAGIPVTEVvektGEGRPGGRVQIGDLIKNGEIDLVINTLYPFKATVH-- 75

                          90
                  ....*....|....*..
gi 525964238  101 DVKALMRIATVWNIPVA 117
Cdd:pfam02142  76 DGYAIRRAAENIDIPGP 92
MGS smart00851
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 40-117 2.73e-19

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: 76.74  E-value: 2.73e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525964238    40 HKLYATGTTGHLLaRETGLEITSLLSGPMGGDQ-QLGGLIAEKKIDLLVFFWDPMNAAPHDpDVKALMRIATVWNIPVA 117
Cdd:smart00851  14 FELLATGGTAKFL-REAGLPVVKTLHPKVHGGIpQILDLIKNGEIDLVINTLYPFEAQAHE-DGYSIRRAAENIDIPGP 90
 
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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