Malate synthase G

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	None
Molecular Weight	80487.88
Theoretical pI	6.09
GO Classification	Functions malate synthase activity metal ion binding Processes tricarboxylic acid cycle glyoxylate cycle glyoxylate catabolic process 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.
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	P37330
UniProtKB Entry Name
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
GenBank Gene ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	None
Locus	None
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. [7925370 ] 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. [9278503 ] 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. [16738553 ] Ornston LN, Ornston MK: Regulation of glyoxylate metabolism in Escherichia coli K-12. J Bacteriol. 1969 Jun;98(3):1098-108. [4892366 ] FALMAGNE P, VANDERWINKEL E, WIAME JM: [DEMONSTRATION OF 2 MALATE SYNTHASES IN ESCHERICHIA COLI]. Biochim Biophys Acta. 1965 May 18;99:246-58. [14336062 ] 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. [9880556 ] 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. [10715138 ] 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. [12930982 ] 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. [15637152 ] 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. [18008171 ]

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