1EGH,1B93,1IK4


Conserved Protein Domain Family
MGS

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cd01422: MGS 
Click on image for an interactive view with Cn3D
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.
Statistics
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PSSM-Id: 238710
Aligned: 21 rows
Threshold Bit Score: 152.78
Created: 10-Jan-2006
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
active sitecatalyticdimer
Conserved site includes 9 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Structure:1B93_B binds phosphate and formic acid
  • Structure:1EGH_C binds 2-phosphoglycolic acid, a dihydroxyacetone phosphate analog
  • Structure:1IK4_A binds phosphoglycolohydroxamic acid, a dihydroxyacetone phosphate analog

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1           #     #                     # ##                          ##    #           
1EGH_C       13 HIALVAHDhcKQMLMSWVERHQPLLeqHVLYATGTTGNLISra-------tGMNVNAm---LSGPMGGDQQVGALISegK 82  Escherichia coli
1B93_B       13 HIALVAHDhcKQMLMSWVERHQPLLeqHVLYATGTTGNLISra-------tGMNVNAm---LSGPMGGDQQVGALISegK 82  Escherichia coli
ZP_00015530  12 TIGLVAHDgqKRAMGQWVAANATVLghHALVATGTTARVLKe---------QNPTFDitglKSGPFGGDQQLGALIAegH 82  Rhodospirillum r...
ZP_00073465   7 TIALLAYDskKDNLVEFVKKHKIVLsrYQLVATESTAQYILqe-------vDIEINSv---LAGPLGGDAQLAVEVTtgN 76  Trichodesmium er...
ZP_00074983 154 YLALIAHNemKSSLVEFVKEHIKLItkFPLVATGTTGLLLHq---------ATGVVLsrkvKSGPLGGDQAIGSMIStdN 224 Trichodesmium er...
NP_811063     8 GIGLVAHDamKKDLIEWVLWNSELLmgNKFYCTGTTGTLILealkekhpevEWDFTIl---KSGPLGGDQQMGSRIVdgQ 84  Bacteroides thet...
Q8XLN2        2 KIALIAHDkkKEEMIELAKDFEDKLskHILVATGTTGLKIMqn-------tSLEVKRc---KSGPLGGDQEIGAMVAnhD 71  Clostridium perf...
P42980        2 KIALIAHDkkKQDMVQFTTAYRDILknHDLYATGTTGLKIHea-------tGLQIERf---QSGPLGGDQQIGALIAanA 71  Bacillus subtilis
O51339        4 KIALIAHDkkKEDLVNFVKQNYLFLskFKLIATGTTGSKIQqa-------tDLTIFKy---KSGPMGGDQQIGAEVAegN 73  Lyme disease spi...
Q8XXD0        6 RIALIAHDhkKDDMIAFAQTHKAFLmrCDLLATGTTGGRLQde-------vGLSVQRm---LSGPWGGDLQIGAQLAegR 75  Ralstonia solana...
Feature 1                      #                             
1EGH_C       83 IDVLIFFWDPLNAVPHDPDVKALLRLATVWNIPVATNVATADFII 127 Escherichia coli
1B93_B       83 IDVLIFFWDPLNAVPHDPDVKALLRLATVWNIPVATNVATADFII 127 Escherichia coli
ZP_00015530  83 LDCLIFFVDPMEPQPHDVDVKALIRLAQVHEIPAACNRATADLMI 127 Rhodospirillum rubrum
ZP_00073465  77 VVAVICLVDYLFSQSYEPDIKLLLRLCQVHNVPIAINIATAEIII 121 Trichodesmium erythraeum IMS101
ZP_00074983 225 ICGVLFFRDPLSSHPHHADIEALSRLCDVYQVPLATNPSTAKAIL 269 Trichodesmium erythraeum IMS101
NP_811063    85 IDYLFFFTDPMTLQPHDTDVKALTRLAGVENIVFCCNRSTADHII 129 Bacteroides thetaiotaomicron VPI-5482
Q8XLN2       72 VDMVIFLRDPLTAQPHEPDISALLRLCDVYKVPLATNTESAKLIM 116 Clostridium perfringens
P42980       72 LDLVIFLRDPLTAQPHEPDVSALIRLCDVYSIPLATNMGTAEILV 116 Bacillus subtilis
O51339       74 ILAIFFFRDPLTSQPHEPDVSALIRLCDVHKIPLATNVKTAEILI 118 Lyme disease spirochete
Q8XXD0       76 VDAVIFLRDPMTPQPHEPDINALVRACDVHNIPCATNLATADLVM 120 Ralstonia solanacearum

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