Rv0534c - 1,4-dihydroxy-2-naphthoate octaprenyltransferase menA


Protein Domains

Gene Information
LocusRv0534c
SymbolmenA
Gene Name1,4-dihydroxy-2-naphthoate octaprenyltransferase menA
Location625562 - 626440 (-)
SpeciesMycobacterium tuberculosis H37Rv complete genome.
LengthGene:879 bp
Protein:293 aa
External LinksTuberculist
Target Gene Information
String Protein-Protein Interactions
STITCH Chemical-Protein Interactions
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Orthologs
Orthogroup Number18777
Related GenesAcel_0150 BL1655 CE0469 cg0531 DIP0418 jk1877 MAP4029c MAV_4611 Mkms_0716 ML2406 Mmcs_0702 MSMEG_0988 MT0558 MUL_0633 Mvan_0880 nfa51470 PPA1945
Transcriptional Regulation
Operons View gene in operon browser
Regulatory Network
Search for regulators of Rv0534c
Expression Correlation Genes with Correlated Expression
Scatterplot of Gene Expression

Sequence
Proteins
Genomic Sequence
Community Annotations Pending Curatorial Review
FieldValueStatusCreatorDate
TermTBRXN:DHNAOT 1,4-dihydroxy-2-naphthoate octaprenyltransferase - IPIactivenjamshidi2012-10-05
see PMID: 16131752, 12909628
JJ. Truglio, K. Theis et al. Crystal structure of Mycobacterium tuberculosis MenB, a key enzyme in vitamin K2 biosynthesis. J. Biol. Chem. 2003
TermTBRXN:DHNAOT 1,4-dihydroxy-2-naphthoate octaprenyltransferase - IPIactivenjamshidi2012-10-05
see PMID: 16131752, 12909628
JM. Johnston, VL. Arcus et al. Structure of naphthoate synthase (MenB) from Mycobacterium tuberculosis in both native and product-bound forms. Acta Crystallogr. D Biol. Crystallogr. 2005
TermTBRXN:DHNAOT 1,4-dihydroxy-2-naphthoate octaprenyltransferase - ISSactivenjamshidi2012-10-05
see PMID: 16131752, 12909628
JJ. Truglio, K. Theis et al. Crystal structure of Mycobacterium tuberculosis MenB, a key enzyme in vitamin K2 biosynthesis. J. Biol. Chem. 2003
TermTBRXN:DHNAOT 1,4-dihydroxy-2-naphthoate octaprenyltransferase - ISSactivenjamshidi2012-10-05
see PMID: 16131752, 12909628
JM. Johnston, VL. Arcus et al. Structure of naphthoate synthase (MenB) from Mycobacterium tuberculosis in both native and product-bound forms. Acta Crystallogr. D Biol. Crystallogr. 2005