Malate synthase G

Details

Name
Malate synthase G
Synonyms
  • 2.3.3.9
  • glc
  • MSG
Gene Name
glcB
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0016351|Malate synthase G
MSQTITQSRLRIDANFKRFVDEEVLPGTGLDAAAFWRNFDEIVHDLAPENRQLLAERDRI
QAALDEWHRSNPGPVKDKAAYKSFLRELGYLVPQPERVTVETTGIDSEITSQAGPQLVVP
AMNARYALNAANARWGSLYDALYGSDIIPQEGAMVSGYDPQRGEQVIAWVRRFLDESLPL
ENGSYQDVVAFKVVDKQLRIQLKNGKETTLRTPAQFVGYRGDAAAPTCILLKNNGLHIEL
QIDANGRIGKDDPAHINDVIVEAAISTILDCEDSVAAVDAEDKILLYRNLLGLMQGTLQE
KMEKNGRQIVRKLNDDRHYTAADGSEISLHGRSLLFIRNVGHLMTIPVIWDSEGNEIPEG
ILDGVMTGAIALYDLKVQKNSRTGSVYIVKPKMHGPQEVAFANKLFTRIETMLGMAPNTL
KMGIMDEERRTSLNLRSCIAQARNRVAFINTGFLDRTGDEMHSVMEAGPMLRKNQMKSTP
WIKAYERNNVLSGLFCGLRGKAQIGKGMWAMPDLMADMYSQKGDQLRAGANTAWVPSPTA
ATLHALHYHQTNVQSVQANIAQTEFNAEFEPLLDDLLTIPVAENANWSAQEIQQELDNNV
QGILGYVVRWVEQGIGCSKVPDIHNVALMEDRATLRISSQHIANWLRHGILTKEQVQASL
ENMAKVVDQQNAGDPAYRPMAGNFANSCAFKAASDLIFLGVKQPNGYTEPLLHAWRLREK
ESH
Number of residues
723
Molecular Weight
80487.88
Theoretical pI
6.09
GO Classification
Functions
malate synthase activity / metal ion binding
Processes
glyoxylate catabolic process / glyoxylate cycle / tricarboxylic acid cycle
Components
cytosol
General Function
Metal ion binding
Specific Function
Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0016352|Malate synthase G (glcB)
ATGAGTCAAACCATAACCCAGAGCCGTTTACGCATTGACGCCAATTTTAAACGTTTTGTG
GATGAAGAAGTTTTACCGGGAACAGGGCTGGACGCTGCGGCGTTCTGGCGCAATTTTGAT
GAGATCGTTCATGATCTGGCACCAGAAAATCGTCAGTTGCTGGCAGAACGCGATCGCATT
CAGGCAGCGCTTGATGAGTGGCATCGCAGCAATCCGGGGCCGGTAAAAGATAAAGCGGCC
TATAAATCTTTCCTGCGTGAACTGGGCTACCTGGTGCCGCAACCGGAGCGCGTGACGGTG
GAAACCACGGGCATTGACAGCGAAATCACCAGCCAGGCGGGGCCGCAGCTGGTGGTTCCG
GCAATGAACGCCCGCTACGCGCTGAACGCGGCGAACGCTCGCTGGGGCTCACTGTACGAT
GCGTTATACGGCAGCGACATCATCCCGCAGGAAGGGGCGATGGTCAGCGGCTACGATCCG
CAACGCGGTGAGCAGGTTATCGCCTGGGTTCGGCGTTTCCTCGATGAATCTCTACCGCTG
GAAAACGGCAGCTATCAGGATGTGGTGGCGTTTAAGGTGGTTGATAAACAATTACGCATC
CAGTTGAAAAATGGTAAAGAAACCACGTTACGTACTCCAGCACAGTTTGTCGGTTACCGT
GGCGATGCCGCTGCGCCGACCTGCATTTTGCTGAAAAATAACGGCCTGCATATTGAGCTG
CAAATCGATGCCAATGGGCGGATTGGCAAAGACGATCCGGCGCACATCAACGATGTTATC
GTCGAAGCTGCTATCAGTACCATTCTCGACTGCGAAGATTCGGTCGCGGCGGTTGATGCG
GAAGATAAAATCCTGCTGTACCGCAACCTGCTGGGCCTGATGCAGGGGACTCTGCAAGAG
AAAATGGAGAAAAACGGTCGGCAAATCGTGCGTAAACTGAATGACGATCGTCATTACACC
GCCGCCGATGGCTCTGAAATTTCTCTGCACGGACGCTCGCTGCTGTTTATCCGCAACGTG
GGTCATTTGATGACCATTCCTGTGATTTGGGACAGCGAAGGCAATGAAATCCCGGAAGGC
ATTCTTGATGGCGTCATGACTGGCGCGATTGCCCTCTATGATTTAAAAGTGCAGAAAAAC
TCGCGCACTGGCAGCGTCTATATTGTGAAACCGAAAATGCACGGTCCGCAGGAAGTGGCG
TTCGCCAACAAACTGTTTACCCGCATTGAGACAATGCTCGGTATGGCACCGAATACCCTG
AAAATGGGCATTATGGATGAAGAACGTCGGACCTCGCTGAACTTGCGTAGCTGTATCGCT
CAGGCGCGCAACCGCGTGGCGTTCATCAATACCGGTTTCCTCGACCGTACCGGCGATGAA
ATGCATTCGGTGATGGAAGCTGGCCCGATGCTGCGTAAAAATCAGATGAAATCGACGCCT
TGGATCAAAGCCTACGAGCGTAATAACGTGCTTTCCGGTCTGTTCTGTGGGCTGCGCGGT
AAAGCGCAAATTGGTAAAGGCATGTGGGCAATGCCGGACCTGATGGCAGACATGTACAGC
CAGAAGGGCGACCAACTGCGTGCCGGGGCAAACACAGCCTGGGTTCCGTCACCAACCGCT
GCTACGCTCCATGCGCTGCACTACCACCAAACCAACGTACAGAGCGTACAAGCCAACATT
GCCCAGACCGAGTTCAATGCTGAATTTGAACCGCTGCTGGACGATCTGCTGACTATTCCG
GTTGCTGAAAACGCTAACTGGTCGGCGCAAGAGATCCAACAAGAGCTGGATAACAACGTG
CAGGGGATTCTGGGGTACGTGGTGCGCTGGGTGGAGCAGGGGATTGGTTGTTCAAAAGTG
CCGGATATTCACAATGTGGCGTTGATGGAAGACCGCGCAACGCTGCGTATCTCCAGCCAG
CATATCGCCAACTGGTTACGTCACGGTATTCTGACCAAAGAACAGGTGCAGGCGTCGCTG
GAGAATATGGCGAAAGTGGTTGATCAGCAAAACGCTGGCGATCCGGCTTATCGTCCGATG
GCGGGGAATTTCGCTAACTCGTGTGCTTTTAAAGCTGCCAGCGATTTAATCTTCCTCGGC
GTGAAACAGCCAAACGGCTATACCGAACCGTTATTACACGCCTGGCGTTTACGCGAAAAA
GAAAGTCATTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP37330
UniProtKB Entry NameMASZ_ECOLI
GenBank Protein ID517247
GenBank Gene IDX74547
General References
  1. Molina I, Pellicer MT, Badia J, Aguilar J, Baldoma L: Molecular characterization of Escherichia coli malate synthase G. Differentiation with the malate synthase A isoenzyme. Eur J Biochem. 1994 Sep 1;224(2):541-8. [Article]
  2. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  3. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  4. Ornston LN, Ornston MK: Regulation of glyoxylate metabolism in Escherichia coli K-12. J Bacteriol. 1969 Jun;98(3):1098-108. [Article]
  5. FALMAGNE P, VANDERWINKEL E, WIAME JM: [DEMONSTRATION OF 2 MALATE SYNTHASES IN ESCHERICHIA COLI]. Biochim Biophys Acta. 1965 May 18;99:246-58. [Article]
  6. Pellicer MT, Fernandez C, Badia J, Aguilar J, Lin EC, Baldom L: Cross-induction of glc and ace operons of Escherichia coli attributable to pathway intersection. Characterization of the glc promoter. J Biol Chem. 1999 Jan 15;274(3):1745-52. [Article]
  7. Howard BR, Endrizzi JA, Remington SJ: Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 A resolution: mechanistic implications. Biochemistry. 2000 Mar 21;39(11):3156-68. [Article]
  8. Anstrom DM, Kallio K, Remington SJ: Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution. Protein Sci. 2003 Sep;12(9):1822-32. [Article]
  9. Tugarinov V, Choy WY, Orekhov VY, Kay LE: Solution NMR-derived global fold of a monomeric 82-kDa enzyme. Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):622-7. Epub 2005 Jan 6. [Article]
  10. Grishaev A, Tugarinov V, Kay LE, Trewhella J, Bax A: Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints. J Biomol NMR. 2008 Feb;40(2):95-106. Epub 2007 Nov 16. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04343Glyoxylic acidexperimentalunknownDetails