Rv2962c
- Type
- protein_coding
- Name
- Rv2962c
- Locus Name
-
Rv2962c
- Product
-
Possible glycosyl transferase
- Functional Category
-
Intermediary metabolism and respiration
- Location
- 3313773..3315122 (- strand)
- Gene Length
- 1349 bp
- Nucleotides
-
GTGCGCGTGTCGTGCGTGTACGCTACGGCGTCGAGGTGGGGCGGGCCACCGGTTGCTAGCGAGGTGAGAGGGGACGCGGCCATCAGCACGACACCGGACGCCGCACCTGGGCTTGCCGCACGCAGGCGCCGGATCCTTTTCGTCGCGGAAGCAGTGACCCTGGCTCACGTCGTCCGGCCATTCGCGCTTGCGCAGTCGCTGGACCCTAGTCGTTATGAAGTGCACTTCGCCTGCGACCCGCGCTACAACCAGCTTCTAGGTCCGCTCCCTTTCCGTCACCATGCGATTCACACCATCCCCAGCGAGCGGTTTTTCGGCAATCTGACTCAGGGTCGTTTCTATGCCATGCGGACGCTGCGGAAGTACGTTGAGGCGGACCTGCGGGTCCTGGATGAGATCGCGCCGGACCTCGTCGTCGGTGACCTTCGCATTTCACTGTCGGTCAGCGCCCGACTGGCCGGCATTCCTTACATCGCGATCGCGAATGCCTACTGGAGTCCGTACGCGCAGCGGCGTTTTCCGCTGCCCGACGTGATATGGACCCGCTTGTTCGGCGTCAGGTTGGTCAAGCTCCTCTACCGCCTGGAACGCCCTTTGCTCTTCGCCCTGCAGTGCATGCCGCTCAACTGGGTCCGCCGCAGGCACGGGCTGTCGAGTCTGGGGTGGAACCTGTGCCGCATTTTCACCGACGGGGACCACACCCTGTATGCTGACGTGCCCGAGCTGATGCCCACCTACGACTTGCCGGCCAACCACGAGTACCTTGGCCCGGTCCTGTGGTCGCCCGCCGGGAAGCCGCCGACATGGTGGGATTCGCTGCCAACCGACCGGCCGATCGTGTACGCAACCCTGGGCACGTCCGGCGGGAGAAATCTGTTGCAACTGGTGTTGAACGCGTTGGCTGAGTTGCCGGTGACGGTGATCGCGGCCACCGCGGGCCGCAGTGACCTGAAGACCGTGCCGGCCAACGCCTTCGTGGCGGACTACCTGCCGGGTGAGGCCGCTGCGGCTCGCTCGGCCGTGGTGGTCTGCAATGGCGGGAGTTTGACGACCCAGCAGGCCTTGGTGGCCGGGGTGCCGGTGATCGGGGTCGCGGGCAATCTCGATCAGCACTTGAATATGGAGGCCGTTGAGCGGGCCGGGGCGGGCGTGCTGCTGCGAACTGAGCGGCTGAAGAGTCAGCGGGTGGCAGGGGCCGTGATGCAGGTGATCAGTCGGTCCGAGTACCGACAAGCCGCCGCGCGACTCGCCGATGCCTTCGGACGAGACCGCGTTGGATTCCCGCAGCATGTGGAGAATGCTCTGCGCCTCATGCCGGAGAACCGGCCCCGGACATGGTTGGCCAGCTA
- Drug Resistance
- Mutations
- Function
- Catalyzes the transfer of the first rhamnosyl residue on p-hydroxybenzoic acid or phenolphthiocerol derivatives to form, after O-methylation at position 2 of the sugar unit, mono-O-methyl-glycosyl-p-hydroxybenzoic acid derivative (p-HBAD I) and 2-O-methyl-rhamnosyl-phenolphthiocerol dimycocerosate (also called mycoside B) during p-hydroxybenzoic acid derivatives (p-HBAD) and glycosylated phenolphthiocerol dimycocerosates (PGL) biosynthesis. {ECO:0000269|PubMed:15292272}.
- Family
-
Glycosyltransferase 28 family
- GO
-
- evasion or tolerance of host immune response GO:0020012 biological_process
- glycolipid biosynthetic process GO:0009247 biological_process
- intracellular membrane-bounded organelle GO:0043231 cellular_component
- plasma membrane GO:0005886 cellular_component
- UDP-glycosyltransferase activity GO:0008194 molecular_function
- transferase activity, transferring hexosyl groups GO:0016758 molecular_function
- InterPro
Summary
- Name
- PGL/p-HBAD biosynthesis rhamnosyltransferase (EC 2.4.1.-)
- Family
- Glycosyltransferase 28 family
- Protein Sequence
-
MRVSCVYATASRWGGPPVASEVRGDAAISTTPDAAPGLAARRRRILFVAEAVTLAHVVRPFALAQSLDPSRYEVHFACDPRYNQLLGPLPFRHHAIHTIPSERFFGNLTQGRFYAMRTLRKYVEADLRVLDEIAPDLVVGDLRISLSVSARLAGIPYIAIANAYWSPYAQRRFPLPDVIWTRLFGVRLVKLLYRLERPLLFALQCMPLNWVRRRHGLSSLGWNLCRIFTDGDHTLYADVPELMPTYDLPANHEYLGPVLWSPAGKPPTWWDSLPTDRPIVYATLGTSGGRNLLQLVLNALAELPVTVIAATAGRSDLKTVPANAFVADYLPGEAAAARSAVVVCNGGSLTTQQALVAGVPVIGVAGNLDQHLNMEAVERAGAGVLLRTERLKSQRVAGAVMQVISRSEYRQAAARLADAFGRDRVGFPQHVENALRLMPENRPRTWLAS
- Mass
- 49,433 Da
- Length
- 449 Aa
Rv2962c doesn't seem to be a targeted by any drug.
Rv2962c doesn't seem to be involved in any pathway.
- 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.
- targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis.
- BMC Syst Biol. 2008 Dec 19;2:109. doi: 10.1186/1752-0509-2-109.
- Characterization of three glycosyltransferases involved in the biosynthesis of the phenolic glycolipid antigens from the Mycobacterium tuberculosis complex.
- J Biol Chem. 2004 Oct 8;279(41):42574-83. doi: 10.1074/jbc.M406246200. Epub 2004 Aug 3.
- Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
- Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.