Rv1837c - malate synthase G glcB

Expression: Most Significant Conditions for Rv1837c

Protein Domains

Gene Information
Locus	Rv1837c
Symbol	glcB
Gene Name	malate synthase G glcB
Location	2084756 - 2086981 (-)
Species	Mycobacterium tuberculosis H37Rv complete genome.
Length	Gene:2226 bp Protein:742 aa
External Links	Tuberculist Target Gene Information String Protein-Protein Interactions STITCH Chemical-Protein Interactions Search Google Scholar
Orthologs
Orthogroup Number	13899
Related Genes	CE2231 cg2559 jk1932 MAP1549c MAV_2880 Mkms_2861 ML2069 Mmcs_2817 MSMEG_3640 MT1885 MUL_3055 Mvan_3097 nfa25030 SAV2000
Transcriptional Regulation
Operons	View gene in operon browser
Regulatory Network	Search for regulators of Rv1837c
Expression Correlation	Genes with Correlated Expression Scatterplot of Gene Expression

Sequence

Proteins

>Rv1837c Transcript 1
MTDRVSVGNLRIARVLYDFVNNEALPGTDIDPDSFWAGVDKVVADLTPQNQALLNARDEL
QAQIDKWHRRRVIEPIDMDAYRQFLTEIGYLLPEPDDFTITTSGVDAEITTTAGPQLVVP
VLNARFALNAANARWGSLYDALYGTDVIPETDGAEKGPTYNKVRGDKVIAYARKFLDDSV
PLSSGSFGDATGFTVQDGQLVVALPDKSTGLANPGQFAGYTGAAESPTSVLLINHGLHIE
ILIDPESQVGTTDRAGVKDVILESAITTIMDFEDSVAAVDAADKVLGYRNWLGLNKGDLA
AAVDKDGTAFLRVLNRDRNYTAPGGGQFTLPGRSLMFVRNVGHLMTNDAIVDTDGSEVFE
GIMDALFTGLIAIHGLKASDVNGPLINSRTGSIYIVKPKMHGPAEVAFTCELFSRVEDVL
GLPQNTMKIGIMDEERRTTVNLKACIKAAADRVVFINTGFLDRTGDEIHTSMEAGPMVRK
GTMKSQPWILAYEDHNVDAGLAAGFSGRAQVGKGMWTMTELMADMVETKIAQPRAGASTA
WVPSPTAATLHALHYHQVDVAAVQQGLAGKRRATIEQLLTIPLAKELAWAPDEIREEVDN
NCQSILGYVVRWVDQGVGCSKVPDIHDVALMEDRATLRISSQLLANWLRHGVITSADVRA
SLERMAPLVDRQNAGDVAYRPMAPNFDDSIAFLAAQELILSGAQQPNGYTEPILHRRRRE
FKARAAEKPAPSDRAGDDAAR*

Genomic Sequence

>Rv1837c
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

Community Annotations Pending Curatorial Review

Field	Value	Status	Creator	Date
Term	TBRXN:MALS malate synthase - ISS	active	njamshidi	2012-10-05
	see PMID: 12393860 CV. Smith, CC. Huang et al. Biochemical and structural studies of malate synthase from Mycobacterium tuberculosis. J. Biol. Chem. 2003
Term	EC:4.1.3.2 Transferred entry: 2.3.3.9. - ISS	active	njamshidi	2012-10-05
	see PMID: 12393860 CV. Smith, CC. Huang et al. Biochemical and structural studies of malate synthase from Mycobacterium tuberculosis. J. Biol. Chem. 2003
Term	TBRXN:MALS malate synthase - IDA	active	njamshidi	2012-10-05
	see PMID: 12393860 CV. Smith, CC. Huang et al. Biochemical and structural studies of malate synthase from Mycobacterium tuberculosis. J. Biol. Chem. 2003
Term	EC:4.1.3.2 Transferred entry: 2.3.3.9. - IDA	active	njamshidi	2012-10-05
	see PMID: 12393860 CV. Smith, CC. Huang et al. Biochemical and structural studies of malate synthase from Mycobacterium tuberculosis. J. Biol. Chem. 2003
Term	EC:2.3.3.9 Malate synthase. - NR	active	extern:JZUCKER	2012-03-06
	Inferred from mutant phenotype CV. Smith, CC. Huang et al. Biochemical and structural studies of malate synthase from Mycobacterium tuberculosis. J. Biol. Chem. 2003
Term	EC:2.3.3.9 Malate synthase. - NR	active	extern:JZUCKER	2012-03-06
	Traceable author statement to experimental support authors,KY. Rhee,LP. de Carvalho,R. Bryk,S. Ehrt,J. Marrero,SW. Park,D. Schnappinger,A. Venugopal,C. Nathan Central carbon metabolism in Mycobacterium tuberculosis: an unexpected frontier. Trends Microbiol. 2011