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Conserved domains on  [gi|1139890557|gb|ONI48032|]
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methylglyoxal synthase [Epulopiscium sp. SCG-C06WGA-EpuloA1]

Protein Classification

methylglyoxal synthase( domain architecture ID 10788044)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MgsA COG1803
Methylglyoxal synthase [Carbohydrate transport and metabolism];
1-122 1.19e-67

Methylglyoxal synthase [Carbohydrate transport and metabolism];


:

Pssm-ID: 441408  Cd Length: 122  Bit Score: 199.94  E-value: 1.19e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139890557   1 MNIGLVAHDAKKKLMENLAIAYRHILAKHTLYATATTGRLVEESTNLTIYKYLAGHLGGLQQLGSQIAHNQLDMVIFLRD 80
Cdd:COG1803     1 MTIALIAHDNKKDDLVEFAKAHKDILSKHELVATGTTGKLIEEATGLEVTRLLSGPLGGDQQIGALIAEGEIDAVIFFRD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1139890557  81 PLTQKPHEPELGTLERLCDIHNIPIATNLATAELLIKALERG 122
Cdd:COG1803    81 PLTAQPHEPDVKALLRLCDVHNIPLATNLATAELLITSLLRG 122
 
Name Accession Description Interval E-value
MgsA COG1803
Methylglyoxal synthase [Carbohydrate transport and metabolism];
1-122 1.19e-67

Methylglyoxal synthase [Carbohydrate transport and metabolism];


Pssm-ID: 441408  Cd Length: 122  Bit Score: 199.94  E-value: 1.19e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139890557   1 MNIGLVAHDAKKKLMENLAIAYRHILAKHTLYATATTGRLVEESTNLTIYKYLAGHLGGLQQLGSQIAHNQLDMVIFLRD 80
Cdd:COG1803     1 MTIALIAHDNKKDDLVEFAKAHKDILSKHELVATGTTGKLIEEATGLEVTRLLSGPLGGDQQIGALIAEGEIDAVIFFRD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1139890557  81 PLTQKPHEPELGTLERLCDIHNIPIATNLATAELLIKALERG 122
Cdd:COG1803    81 PLTAQPHEPDVKALLRLCDVHNIPLATNLATAELLITSLLRG 122
mgsA PRK05234
methylglyoxal synthase; Validated
 1-130 2.25e-60

methylglyoxal synthase; Validated


Pssm-ID: 179969 [Multi-domain]  Cd Length: 142  Bit Score: 181.95  E-value: 2.25e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139890557   1 MNIGLVAHDAKKKLMENLAIAYRHILAKHTLYATATTGRLVEESTNLTIYKYLAGHLGGLQQLGSQIAHNQLDMVIFLRD 80
Cdd:PRK05234    5 KRIALIAHDHKKDDLVAWVKAHKDLLEQHELYATGTTGGLIQEATGLDVTRLLSGPLGGDQQIGALIAEGKIDMLIFFRD 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1139890557  81 PLTQKPHEPELGTLERLCDIHNIPIATNLATAELLIKALERgDLSWREIV 130
Cdd:PRK05234   85 PLTAQPHDPDVKALLRLADVWNIPVATNRATADFLISSLLF-DDEVEILI 133
MGSA TIGR00160
methylglyoxal synthase; Methylglyoxal synthase (MGS) generates methylglyoxal (MG), a toxic ...
 1-123 6.40e-49

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: 153.41  E-value: 6.40e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139890557   1 MNIGLVAHDAKKKLMENLAIAYRHILAKHTLYATATTGRLVEESTNLTIYKYLAGHLGGLQQLGSQIAHNQLDMVIFLRD 80
Cdd:TIGR00160   3 KHIALIAHDKKKQDLVNFVQQHKPLLSQHDLYATGTTGNLISRATGLNINAMLSGPMGGDQQIGALIAEGKIDAVIFFWD 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1139890557  81 PLTQKPHEPELGTLERLCDIHNIPIATNLATAELLIKALERGD 123
Cdd:TIGR00160  83 PLNAQPHEPDVKALLRLCTVWNIPLATNVATADFLIKSPHFND 125
MGS cd01422
Methylglyoxal synthase catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to ...
 2-116 5.85e-48

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: 149.70  E-value: 5.85e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139890557   2 NIGLVAHDAKKKLMENLAIAYRHILAKHTLYATATTGRLVEESTNLTIYKYLAGHLGGLQQLGSQIAHNQLDMVIFLRDP 81
Cdd:cd01422     1 RIALIAHDNKKEDLVEFVKQHQELLSRHRLVATGTTGLLIQEATGLTVNRMKSGPLGGDQQIGALIAEGEIDAVIFFRDP 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1139890557  82 LTQKPHEPELGTLERLCDIHNIPIATNLATAELLI 116
Cdd:cd01422    81 LTAQPHEPDVKALLRLCDVYNIPLATNRSTADAII 115
MGS pfam02142
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 18-107 4.65e-13

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: 60.20  E-value: 4.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139890557  18 LAIAYRHILAKHTLYATATTGRLVEE---STNLTIYKYLAGHLGGLQQLGSQIAHNQLDMVIFLRDPLTQKPHEPelGTL 94
Cdd:pfam02142   3 VELAKALVELGFELLATGGTAKFLREagiPVTEVVEKTGEGRPGGRVQIGDLIKNGEIDLVINTLYPFKATVHDG--YAI 80

                          90
                  ....*....|...
gi 1139890557  95 ERLCDIHNIPIAT 107
Cdd:pfam02142  81 RRAAENIDIPGPT 93
 
Name Accession Description Interval E-value
MgsA COG1803
Methylglyoxal synthase [Carbohydrate transport and metabolism];
1-122 1.19e-67

Methylglyoxal synthase [Carbohydrate transport and metabolism];


Pssm-ID: 441408  Cd Length: 122  Bit Score: 199.94  E-value: 1.19e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139890557   1 MNIGLVAHDAKKKLMENLAIAYRHILAKHTLYATATTGRLVEESTNLTIYKYLAGHLGGLQQLGSQIAHNQLDMVIFLRD 80
Cdd:COG1803     1 MTIALIAHDNKKDDLVEFAKAHKDILSKHELVATGTTGKLIEEATGLEVTRLLSGPLGGDQQIGALIAEGEIDAVIFFRD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1139890557  81 PLTQKPHEPELGTLERLCDIHNIPIATNLATAELLIKALERG 122
Cdd:COG1803    81 PLTAQPHEPDVKALLRLCDVHNIPLATNLATAELLITSLLRG 122
mgsA PRK05234
methylglyoxal synthase; Validated
 1-130 2.25e-60

methylglyoxal synthase; Validated


Pssm-ID: 179969 [Multi-domain]  Cd Length: 142  Bit Score: 181.95  E-value: 2.25e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139890557   1 MNIGLVAHDAKKKLMENLAIAYRHILAKHTLYATATTGRLVEESTNLTIYKYLAGHLGGLQQLGSQIAHNQLDMVIFLRD 80
Cdd:PRK05234    5 KRIALIAHDHKKDDLVAWVKAHKDLLEQHELYATGTTGGLIQEATGLDVTRLLSGPLGGDQQIGALIAEGKIDMLIFFRD 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1139890557  81 PLTQKPHEPELGTLERLCDIHNIPIATNLATAELLIKALERgDLSWREIV 130
Cdd:PRK05234   85 PLTAQPHDPDVKALLRLADVWNIPVATNRATADFLISSLLF-DDEVEILI 133
MGSA TIGR00160
methylglyoxal synthase; Methylglyoxal synthase (MGS) generates methylglyoxal (MG), a toxic ...
 1-123 6.40e-49

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: 153.41  E-value: 6.40e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139890557   1 MNIGLVAHDAKKKLMENLAIAYRHILAKHTLYATATTGRLVEESTNLTIYKYLAGHLGGLQQLGSQIAHNQLDMVIFLRD 80
Cdd:TIGR00160   3 KHIALIAHDKKKQDLVNFVQQHKPLLSQHDLYATGTTGNLISRATGLNINAMLSGPMGGDQQIGALIAEGKIDAVIFFWD 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1139890557  81 PLTQKPHEPELGTLERLCDIHNIPIATNLATAELLIKALERGD 123
Cdd:TIGR00160  83 PLNAQPHEPDVKALLRLCTVWNIPLATNVATADFLIKSPHFND 125
MGS cd01422
Methylglyoxal synthase catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to ...
 2-116 5.85e-48

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: 149.70  E-value: 5.85e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139890557   2 NIGLVAHDAKKKLMENLAIAYRHILAKHTLYATATTGRLVEESTNLTIYKYLAGHLGGLQQLGSQIAHNQLDMVIFLRDP 81
Cdd:cd01422     1 RIALIAHDNKKEDLVEFVKQHQELLSRHRLVATGTTGLLIQEATGLTVNRMKSGPLGGDQQIGALIAEGEIDAVIFFRDP 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1139890557  82 LTQKPHEPELGTLERLCDIHNIPIATNLATAELLI 116
Cdd:cd01422    81 LTAQPHEPDVKALLRLCDVYNIPLATNRSTADAII 115
MGS pfam02142
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
 18-107 4.65e-13

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: 60.20  E-value: 4.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139890557  18 LAIAYRHILAKHTLYATATTGRLVEE---STNLTIYKYLAGHLGGLQQLGSQIAHNQLDMVIFLRDPLTQKPHEPelGTL 94
Cdd:pfam02142   3 VELAKALVELGFELLATGGTAKFLREagiPVTEVVEKTGEGRPGGRVQIGDLIKNGEIDLVINTLYPFKATVHDG--YAI 80

                          90
                  ....*....|...
gi 1139890557  95 ERLCDIHNIPIAT 107
Cdd:pfam02142  81 RRAAENIDIPGPT 93
MGS-like cd00532
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ...
 5-112 4.74e-12

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: 58.29  E-value: 4.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1139890557   5 LVAHDAKKKLMENLAiaYRHILAKHTLYATATTGRLVEEsTNLTIYKYLAGHLGGLQQLGSQIA-HNQLDMVIFLRDPLT 83
Cdd:cd00532     4 LSVSDHVKAMLVDLA--PKLSSDGFPLFATGGTSRVLAD-AGIPVRAVSKRHEDGEPTVDAAIAeKGKFDVVINLRDPRR 80

                          90       100
                  ....*....|....*....|....*....
gi 1139890557  84 QKPHEPELGTLERLCDIHNIPIATNLATA 112
Cdd:cd00532    81 DRCTDEDGTALLRLARLYKIPVTTPNATA 109
 
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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