Malate synthase G
Details
- Name
- Malate synthase G
- Synonyms
- 2.3.3.9
- Gene Name
- glcB
- Organism
- Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
- Amino acid sequence
>lcl|BSEQ0051251|Malate synthase G MTDRVSVGNLRIARVLYDFVNNEALPGTDIDPDSFWAGVDKVVADLTPQNQALLNARDEL QAQIDKWHRRRVIEPIDMDAYRQFLTEIGYLLPEPDDFTITTSGVDAEITTTAGPQLVVP VLNARFALNAANARWGSLYDALYGTDVIPETDGAEKGPTYNKVRGDKVIAYARKFLDDSV PLSSGSFGDATGFTVQDGQLVVALPDKSTGLANPGQFAGYTGAAESPTSVLLINHGLHIE ILIDPESQVGTTDRAGVKDVILESAITTIMDFEDSVAAVDAADKVLGYRNWLGLNKGDLA AAVDKDGTAFLRVLNRDRNYTAPGGGQFTLPGRSLMFVRNVGHLMTNDAIVDTDGSEVFE GIMDALFTGLIAIHGLKASDVNGPLINSRTGSIYIVKPKMHGPAEVAFTCELFSRVEDVL GLPQNTMKIGIMDEERRTTVNLKACIKAAADRVVFINTGFLDRTGDEIHTSMEAGPMVRK GTMKSQPWILAYEDHNVDAGLAAGFSGRAQVGKGMWTMTELMADMVETKIAQPRAGASTA WVPSPTAATLHALHYHQVDVAAVQQGLAGKRRATIEQLLTIPLAKELAWAPDEIREEVDN NCQSILGYVVRWVDQGVGCSKVPDIHDVALMEDRATLRISSQLLANWLRHGVITSADVRA SLERMAPLVDRQNAGDVAYRPMAPNFDDSIAFLAAQELILSGAQQPNGYTEPILHRRRRE FKARAAEKPAPSDRAGDDAAR
- Number of residues
- 741
- Molecular Weight
- 80402.24
- Theoretical pI
- Not Available
- GO Classification
- Functionscoenzyme binding / fibronectin binding / host cell extracellular matrix binding / laminin binding / magnesium ion binding / malate synthase activity / protein homodimerization activityProcessesadhesion of symbiont to host / coenzyme A metabolic process / glyoxylate catabolic process / glyoxylate cycle / tricarboxylic acid cycleComponentscapsule / cell surface / cell wall / cytoplasm / cytosol / extracellular region / plasma membrane
- General 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.
- Specific Function
- Coenzyme binding
- Pfam Domain Function
- Malate_synthase (PF01274)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0051252|Malate synthase G (glcB) ATGACAGATCGCGTGTCGGTGGGCAACTTGCGCATCGCTCGGGTGCTCTACGACTTCGTG AACAATGAAGCCCTGCCTGGCACCGATATCGACCCGGACAGCTTCTGGGCGGGCGTCGAC AAGGTCGTCGCCGACCTGACCCCGCAGAACCAAGCTCTGTTGAACGCCCGCGACGAGCTG CAGGCGCAGATCGACAAGTGGCACCGGCGTCGGGTGATCGAGCCCATCGACATGGATGCC TACCGCCAGTTCCTCACCGAGATCGGCTACCTGCTTCCCGAACCTGATGACTTCACCATC ACCACGTCCGGTGTCGACGCTGAGATCACCACGACCGCCGGCCCCCAGCTGGTGGTGCCG GTGCTCAACGCGCGGTTTGCTCTGAACGCGGCCAACGCTCGCTGGGGCTCCCTCTACGAC GCCTTGTATGGCACCGATGTCATCCCCGAGACCGACGGCGCCGAAAAAGGCCCCACGTAC AACAAGGTTCGTGGCGACAAGGTGATCGCGTATGCCCGCAAGTTCCTCGACGACAGTGTT CCGCTGTCGTCGGGTTCCTTTGGCGACGCCACCGGTTTCACAGTGCAGGATGGCCAGCTC GTGGTTGCCTTGCCGGATAAGTCCACCGGCCTGGCCAACCCCGGCCAGTTCGCCGGCTAC ACCGGCGCAGCCGAGTCGCCGACATCGGTGCTGCTAATCAATCACGGTTTGCACATCGAG ATCCTGATCGATCCGGAGTCGCAGGTCGGCACCACCGACCGGGCCGGCGTCAAGGACGTG ATCCTGGAATCCGCGATCACCACGATCATGGACTTCGAGGACTCGGTGGCCGCCGTGGAC GCCGCCGACAAGGTGCTGGGTTATCGGAACTGGCTCGGCCTGAACAAGGGCGACCTGGCA GCAGCGGTAGACAAGGACGGCACCGCTTTCCTGCGGGTGCTCAATAGGGACCGGAACTAC ACCGCACCCGGCGGTGGCCAGTTCACGCTGCCTGGACGCAGCCTCATGTTCGTCCGCAAC GTCGGTCACTTGATGACGAATGACGCCATCGTCGACACTGACGGCAGCGAGGTGTTCGAA GGCATCATGGATGCCCTATTCACCGGCCTGATCGCCATCCACGGGCTAAAGGCCAGCGAC GTCAACGGGCCGCTGATCAACAGCCGCACCGGCTCCATCTACATCGTCAAGCCGAAGATG CACGGTCCGGCCGAGGTGGCGTTTACCTGCGAACTGTTCAGCCGGGTTGAAGATGTGCTG GGGTTGCCGCAAAACACCATGAAGATCGGCATCATGGACGAGGAACGCCGGACCACGGTC AACCTCAAGGCGTGCATCAAAGCTGCCGCGGACCGCGTGGTGTTCATCAACACCGGGTTC CTGGACCGCACCGGCGATGAAATCCACACCTCGATGGAGGCCGGCCCGATGGTGCGCAAG GGCACCATGAAGAGCCAGCCGTGGATCTTGGCCTACGAGGACCACAACGTCGATGCCGGC CTGGCCGCCGGGTTCAGCGGCCGAGCCCAGGTCGGCAAGGGCATGTGGACAATGACCGAG CTGATGGCCGACATGGTCGAGACAAAAATCGCCCAGCCGCGCGCCGGGGCCAGCACCGCC TGGGTTCCCTCTCCCACTGCGGCCACCCTGCATGCGCTGCACTACCACCAGGTCGACGTC GCCGCGGTGCAACAAGGACTGGCGGGGAAGCGTCGCGCCACCATCGAACAATTGCTGACC ATTCCGCTGGCCAAGGAATTGGCCTGGGCTCCCGACGAGATCCGCGAAGAGGTCGACAAC AACTGTCAATCCATCCTCGGCTACGTGGTTCGCTGGGTTGATCAAGGTGTCGGCTGCTCG AAGGTGCCCGACATCCACGACGTCGCGCTCATGGAGGACCGGGCCACGCTGCGAATCTCC AGCCAATTGTTGGCCAACTGGCTGCGCCACGGTGTGATCACCAGCGCGGATGTGCGGGCC AGCTTGGAGCGGATGGCGCCGTTGGTCGATCGACAAAACGCGGGCGACGTGGCATACCGA CCGATGGCACCCAACTTCGACGACAGTATCGCCTTCCTGGCCGCGCAGGAGCTGATCTTG TCCGGGGCCCAGCAGCCCAACGGCTACACCGAGCCGATCCTGCACCGACGTCGTCGGGAG TTTAAGGCCCGGGCCGCTGAGAAGCCGGCCCCATCGGACAGGGCCGGTGACGATGCGGCC CGCTAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P9WK17 UniProtKB Entry Name MASZ_MYCTU - General References
- Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [Article]
- Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3. [Article]
- Anstrom DM, Remington SJ: The product complex of M. tuberculosis malate synthase revisited. Protein Sci. 2006 Aug;15(8):2002-7. [Article]
- Krieger IV, Freundlich JS, Gawandi VB, Roberts JP, Gawandi VB, Sun Q, Owen JL, Fraile MT, Huss SI, Lavandera JL, Ioerger TR, Sacchettini JC: Structure-guided discovery of phenyl-diketo acids as potent inhibitors of M. tuberculosis malate synthase. Chem Biol. 2012 Dec 21;19(12):1556-67. doi: 10.1016/j.chembiol.2012.09.018. [Article]