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
- Functionsmalate synthase activity / metal ion bindingProcessesglyoxylate catabolic process / glyoxylate cycle / tricarboxylic acid cycleComponentscytosol
- 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
- Malate_synthase (PF01274)
- 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
Resource Link UniProtKB ID P37330 UniProtKB Entry Name MASZ_ECOLI GenBank Protein ID 517247 GenBank Gene ID X74547 - General References
- 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]
- 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]
- 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]
- Ornston LN, Ornston MK: Regulation of glyoxylate metabolism in Escherichia coli K-12. J Bacteriol. 1969 Jun;98(3):1098-108. [Article]
- FALMAGNE P, VANDERWINKEL E, WIAME JM: [DEMONSTRATION OF 2 MALATE SYNTHASES IN ESCHERICHIA COLI]. Biochim Biophys Acta. 1965 May 18;99:246-58. [Article]
- 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]
- 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]
- 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]
- 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]
- 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]