menB
- Type
- protein_coding
- Name
- menB
- Locus Name
-
Rv0548c
- Product
-
Naphthoate synthase MenB (dihydroxynaphthoic acid synthetase) (DHNA synthetase)
- Functional Category
-
Intermediary metabolism and respiration
- Location
- 639012..639956 (- strand)
- Gene Length
- 944 bp
- Nucleotides
-
GTGGTGGCTCCAGCCGGCGAACAAGGACGGAGTTCAACAGCCTTGAGTGACAACCCTTTTGATGCCAAGGCGTGGCGGCTCGTGGACGGGTTCGACGATCTGACCGACATCACCTACCACCGCCACGTCGACGATGCCACGGTGCGGGTGGCGTTCAACCGCCCTGAAGTGCGCAACGCATTTCGCCCGCACACCGTCGACGAGCTGTACCGGGTGCTCGACCATGCACGAATGTCGCCCGACGTCGGAGTGGTGCTGCTGACCGGCAACGGGCCGTCCCCGAAGGACGGCGGCTGGGCGTTCTGCTCCGGCGGCGACCAACGAATTCGTGGGCGCAGCGGTTACCAGTACGCCAGCGGAGACACCGCGGACACGGTTGATGTCGCCCGCGCCGGCCGGTTGCACATCCTGGAGGTGCAGCGGCTGATCCGGTTCATGCCCAAGGTGGTCATTTGTCTGGTCAATGGCTGGGCGGCCGGCGGGGGACACAGCCTGCACGTGGTCTGCGATCTCACCCTGGCCAGCCGCGAGTACGCCCGCTTCAAGCAGACCGACGCCGACGTCGGCAGCTTCGATGGCGGTTACGGCAGCGCATATCTGGCCCGTCAGGTCGGCCAGAAGTTTGCCCGCGAGATCTTCTTCCTAGGCCGCACCTACACCGCCGAGCAGATGCACCAGATGGGCGCGGTCAACGCGGTGGCCGAACACGCCGAGCTGGAGACAGTGGGGCTGCAGTGGGCGGCCGAGATCAACGCGAAATCGCCTCAGGCGCAACGGATGCTGAAGTTCGCGTTCAACCTGCTCGACGACGGGCTGGTGGGTCAGCAACTGTTTGCCGGTGAGGCCACCCGCCTGGCCTACATGACCGACGAGGCCGTCGAAGGCCGCGACGCCTTCCTACAGAAGCGTCCCCCCGACTGGAGCCCGTTTCCGCGCTATTTCTA
- Drug Resistance
- Mutations
- Function
- Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA). {ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000269|PubMed:12909628}.
- Family
-
Enoyl-CoA hydratase/isomerase family, MenB subfamily
- GO
-
- protein hexamerization GO:0034214 biological_process
- menaquinone biosynthetic process GO:0009234 biological_process
- cytosol GO:0005829 cellular_component
- 1,4-dihydroxy-2-naphthoyl-CoA synthase activity GO:0008935 molecular_function
- plasma membrane GO:0005886 cellular_component
- InterPro
1Q51
- Name
- 1,4-dihydroxy-2-naphthoyl-CoA synthase (DHNA-CoA synthase) (EC 4.1.3.36)
- Family
- Enoyl-CoA hydratase/isomerase family, MenB subfamily
- Protein Sequence
-
MVAPAGEQGRSSTALSDNPFDAKAWRLVDGFDDLTDITYHRHVDDATVRVAFNRPEVRNAFRPHTVDELYRVLDHARMSPDVGVVLLTGNGPSPKDGGWAFCSGGDQRIRGRSGYQYASGDTADTVDVARAGRLHILEVQRLIRFMPKVVICLVNGWAAGGGHSLHVVCDLTLASREYARFKQTDADVGSFDGGYGSAYLARQVGQKFAREIFFLGRTYTAEQMHQMGAVNAVAEHAELETVGLQWAAEINAKSPQAQRMLKFAFNLLDDGLVGQQLFAGEATRLAYMTDEAVEGRDAFLQKRPPDWSPFPRYF
- Mass
- 34,689 Da
- Length
- 314 Aa
Summary
Rv0548c doesn't seem to be a targeted by any drug.
-
-
Ubiquinone and other terpenoid-quinone biosynthesis mtu00130
mtu00130Metabolism; Metabolism of cofactors and vitamins
-
- Mechanism of the intramolecular Claisen condensation reaction catalyzed by MenB, a crotonase superfamily member.
- Biochemistry. 2011 Nov 8;50(44):9532-44. doi: 10.1021/bi200877x. Epub 2011 Oct 11.
- Structure of naphthoate synthase (MenB) from Mycobacterium tuberculosis in both native and product-bound forms.
- Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1199-206. doi: 10.1107/S0907444905017531. Epub 2005 Aug 16.
- Crystal structure of Mycobacterium tuberculosis MenB, a key enzyme in vitamin K2 biosynthesis.
- J Biol Chem. 2003 Oct 24;278(43):42352-60. doi: 10.1074/jbc.M307399200. Epub 2003 Aug 8.
- 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.
- A bicarbonate cofactor modulates 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase in menaquinone biosynthesis of Escherichia coli.
- J Biol Chem. 2010 Sep 24;285(39):30159-69. doi: 10.1074/jbc.M110.147702. Epub 2010 Jul 19.
- Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
- Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.