| Identification |
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| Name: | 1,4-dihydroxy-2-naphthoate octaprenyltransferase |
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| Synonyms: | - DHNA-octaprenyltransferase
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| Gene Name: | menA |
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| Enzyme Class: | |
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| Biological Properties |
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| General Function: | Involved in transferase activity |
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| Specific Function: | Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to dimethylmenaquinone (DMK). Attaches octaprenylpyrophosphate, a membrane-bound 40-carbon side chain to DHNA. The conversion of DHNA to DMK proceeds in three stages:the removal of the carboxyl group of DHNA as CO(2), the attachment of the isoprenoid side chain, and a quinol-to-quinone oxidation, which is thought to be spontaneous |
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| Cellular Location: | Cell inner membrane; Multi-pass membrane protein |
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| SMPDB Pathways: | |
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| KEGG Pathways: | - Metabolic pathways eco01100
- Ubiquinone and other terpenoid-quinone biosynthesis ec00130
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| KEGG Reactions: | | | |
1.0 | + | 1.0Phytyl diphosphate | ↔ | 1.02-Phytyl-1,4-naphthoquinone | + | 1.0 | + | 1.0 |
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| SMPDB Reactions: | |
1.01,4-dihydroxy-2-naphthoate | + | 1.0 | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0Pyrophosphate | + | 1.0 |
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1.0Octaprenyl diphosphate | + | 1.01,4-dihydroxy-2-naphthoate | + | 1.0 | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0Pyrophosphate | + | 1.0 |
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| EcoCyc Reactions: | |
1.0all-trans-octaprenyl diphosphate | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 | + | 1.0 |
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| Complex Reactions: | |
1.0 | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 | + | 1.0 |
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1.0An all-trans-polyprenyl diphosphate | + | 1.0 | → | 1.0a demethylmenaquinol | + | 1.0 | + | 1.0 |
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| Metabolites: | |
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| GO Classification: | | Component |
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| cell part | | integral to membrane | | intrinsic to membrane | | membrane part | | Function |
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| catalytic activity | | prenyltransferase activity | | transferase activity | | transferase activity, transferring alkyl or aryl (other than methyl) groups | | Process |
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| fat-soluble vitamin metabolic process | | menaquinone biosynthetic process | | menaquinone metabolic process | | metabolic process | | small molecule metabolic process | | vitamin K metabolic process | | vitamin metabolic process |
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| Gene Properties |
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| Blattner: | b3930 |
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| Gene Orientation | Counterclockwise |
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| Centisome Percentage: | 88.74 |
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| Left Sequence End | 4117446 |
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| Right Sequence End | 4118372 |
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| Gene Sequence: | >927 bp
ATGACCATTGCACTGGAACTTCAACAGCTTAAAAAAACCTATCCAGGCGGCGTTCAGGCG
CTTCGTGGGATAGATTTGCAGGTCGAAGCGGGTGATTTTTATGCGCTTCTCGGGCCGAAC
GGGGCCGGGAAATCGACCACTATCGGTATTATCAGCTCTCTGGTAAATAAAACCTCCGGG
CGGGTCAGCGTATTTGGTTACGATCTCGAGAAGGATGTCGTGAACGCTAAACGTCAGTTG
GGACTGGTGCCGCAGGAATTTAACTTCAACCCGTTTGAAACCGTGCAGCAAATTGTGGTG
AATCAGGCAGGGTACTACGGCGTGGAGCGCAAAGAAGCGTACATCCGCAGCGAAAAGTAT
CTTAAACAACTCGATCTATGGGGAAAACGCAACGAACGTGCGCGTATGTTATCTGGCGGG
ATGAAGCGCCGTTTAATGATTGCCCGTGCGTTAATGCATGAACCTAAACTACTGATTCTC
GACGAACCGACCGCAGGCGTGGATATTGAACTTCGCCGCTCAATGTGGGGCTTTTTGAAG
GATTTAAACGACAAAGGCACCACCATCATTCTCACCACACACTACCTGGAAGAAGCAGAA
ATGCTGTGCCGCAATATCGGCATTATTCAACACGGTGAGCTGGTGGAAAATACCTCGATG
AAGGCGCTGCTGGCGAAGCTGAAATCGGAAACCTTTATTCTCGATCTCGCACCGAAAAGC
CCGTTACCGAAGCTCGATGGCTATCAGTATCGACTGGTCGATACCGCGACGCTGGAAGTT
GAAGTGCTGCGTGAGCAGGGGATCAACAGCGTATTTACGCAGTTAAGTGAGCAGGGCATT
CAGGTATTAAGTATGCGTAACAAAGCTAACCGTCTGGAAGAGCTGTTTGTTTCACTGGTT
AATGAAAAACAAGGAGATCGCGCATGA |
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| Protein Properties |
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| Pfam Domain Function: | |
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| Protein Residues: | 308 |
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| Protein Molecular Weight: | 33594 |
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| Protein Theoretical pI: | 9 |
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| Signaling Regions: | |
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| Transmembrane Regions: | - 21-41
- 43-63
- 98-118
- 124-144
- 149-169
- 177-197
- 238-258
- 287-307
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| Protein Sequence: | >1,4-dihydroxy-2-naphthoate octaprenyltransferase
MTEQQISRTQAWLESLRPKTLPLAFAAIIVGTALAWWQGHFDPLVALLALITAGLLQILS
NLANDYGDAVKGSDKPDRIGPLRGMQKGVITQQEMKRALIITVVLICLSGLALVAVACHT
LADFVGFLILGGLSIIAAITYTVGNRPYGYIGLGDISVLVFFGWLSVMGSWYLQAHTLIP
ALILPATACGLLATAVLNINNLRDINSDRENGKNTLVVRLGEVNARRYHACLLMGSLVCL
ALFNLFSLHSLWGWLFLLAAPLLVKQARYVMREMDPVAMRPMLERTVKGALLTNLLFVLG
IFLSQWAA |
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| References |
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| External Links: | |
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| General Reference: | - Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
- Daley, D. O., Rapp, M., Granseth, E., Melen, K., Drew, D., von Heijne, G. (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308:1321-1323. Pubmed: 15919996
- Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
- Plunkett, G. 3rd, Burland, V., Daniels, D. L., Blattner, F. R. (1993). "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Nucleic Acids Res 21:3391-3398. Pubmed: 8346018
- Suvarna, K., Stevenson, D., Meganathan, R., Hudspeth, M. E. (1998). "Menaquinone (vitamin K2) biosynthesis: localization and characterization of the menA gene from Escherichia coli." J Bacteriol 180:2782-2787. Pubmed: 9573170
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