Identification |
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Name: | 3-deoxy-D-manno-octulosonic-acid transferase |
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Synonyms: | |
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Gene Name: | waaA |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Involved in biosynthetic process |
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Specific Function: | Essential step in lipopolysaccharides biosynthesis. Acts at transfer of 3-deoxy-D-mono octulonic acid (KDO) from CMP-KDO to a tetraacyldisaccharide 1,4'-bisphosphate precursor of lipid A (lipid IVA). Transfers two molecules of KDO to lipid IVA. Degraded by FtsH; therefore FtsH regulates the addition of the sugar moiety of the LPS and thus the maturation of the LPS precursor |
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Cellular Location: | Cell inner membrane; Single-pass membrane protein (Probable) |
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SMPDB Pathways: | - Lipopolysaccharide biosynthesis PW000831
- lipopolysaccharide biosynthesis II PW001905
- lipopolysaccharide biosynthesis III PW002059
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KEGG Pathways: | |
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KEGG Reactions: | | | |
1.0 | + | 1.0 | ↔ | 1.0Di[3-deoxy-D-manno-octulosonyl]-lipid IV(A) | + | 1.0 |
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1.0Di[3-deoxy-D-manno-octulosonyl]-lipid IV(A) | + | 1.0 | ↔ | 1.0alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA | + | 1.0 |
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SMPDB Reactions: | |
1.0 | + | 1.0 | → | 1.0Cytidine monophosphate | + | 1.0 | + | 1.0 | + | 1.0 |
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1.0 | + | 1.0 | → | 1.0Cytidine monophosphate | + | 1.0 | + | 1.0a-Kdo-(2->4)-a-Kdo-(2->6)-lipid IVA | + | 1.0 | + | 1.0 |
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EcoCyc Reactions: | |
1.0 | + | 1.0lipid IVA | ↔ | 1.0 | + | 1.0 | + | 1.0 |
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1.0 | + | 1.0 | ↔ | 1.0 | + | 1.0α-Kdo-(2->4)-α-Kdo-(2->6)-lipid IVA | + | 1.0 |
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Complex Reactions: | | | | | |
1.0 | + | 1.0 | → | 1.0alpha-Kdo-(2->6)-lipid IV(A) | + | 1.0 |
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1.0Alpha-Kdo-(2->6)-lipid IV(A) | + | 1.0 | → | 1.0alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IV(A) | + | 1.0 |
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Metabolites: | ECMDB ID | Name | View |
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ECMDB23091 | (2-N,3-O-bis(3-Hydroxytetradecanoyl)-4-O-phosphono-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl phosphate) | MetaboCard | ECMDB20057 | 2,3,2'3'-Tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate | MetaboCard | ECMDB21136 | 2,3,2'3'-Tetrakis(beta-hydroxymyristoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate | MetaboCard | ECMDB24178 | a-Kdo-(2->4)-a-Kdo-(2->6)-lipid IVA | MetaboCard | ECMDB24218 | alpha-Kdo-(2→6)-lipid IVA | MetaboCard | ECMDB20133 | CMP-3-Deoxy-D-manno-octulosonate | MetaboCard | ECMDB00095 | Cytidine monophosphate | MetaboCard | ECMDB21225 | Hydrogen ion | MetaboCard | ECMDB21235 | KDO(2)-lipid IV(A) | MetaboCard | ECMDB21236 | KDO-lipid IV(A) | MetaboCard |
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GO Classification: | Function |
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binding | carbohydrate binding | catalytic activity | sugar binding | transferase activity | Process |
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biosynthetic process | carbohydrate metabolic process | metabolic process | primary metabolic process |
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Gene Properties |
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Blattner: | b3633 |
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Gene Orientation | Clockwise |
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Centisome Percentage: | 82.04 |
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Left Sequence End | 3806563 |
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Right Sequence End | 3807840 |
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Gene Sequence: | >1278 bp
ATGAAAACAACAGCAAAGCTGTCGTTCATGATGTTTGTTGAATGGTTTATCTGGGGCGCG
TGGTTTGTGCCATTGTGGTTGTGGTTAAGTAAAAGCGGTTTTAGTGCCGGAGAAATTGGC
TGGTCGTATGCCTGTACCGCCATTGCGGCGATCCTGTCGCCAATTCTGGTTGGCTCCATC
ACTGACCGCTTTTTCTCGGCGCAAAAAGTGCTGGCGGTATTGATGTTCGCAGGCGCGCTG
CTGATGTATTTCGCTGCGCAACAGACCACTTTTGCCGGGTTCTTCCCGTTACTGCTGGCC
TACTCGCTAACCTATATGCCGACCATTGCGCTGACTAACAGCATCGCTTTTGCCAACGTG
CCGGATGTTGAGCGTGATTTCCCGCGCATTCGTGTGATGGGCACTATCGGCTGGATTGCC
TCCGGTCTGGCATGTGGTTTCTTGCCGCAAATACTGGGGTATGCCGATATCTCACCGACT
AACATCCCGCTGCTGATTACCGCCGGAAGTTCTGCTCTGCTCGGTGTGTTTGCGTTTTTC
CTGCCCGACACGCCACCAAAAAGCACCGGCAAAATGGATATTAAAGTCATGCTCGGCCTG
GATGCGCTGATCCTGCTGCGCGATAAAAACTTCCTCGTCTTTTTCTTCTGTTCATTCCTG
TTTGCGATGCCACTAGCGTTCTATTACATCTTTGCCAACGGTTATCTGACCGAAGTTGGC
ATGAAAAACGCCACCGGCTGGATGACGCTCGGCCAGTTCTCTGAAATCTTCTTTATGCTG
GCATTGCCGTTTTTCACTAAACGCTTTGGTATCAAAAAGGTATTATTGCTTGGTCTGGTC
ACCGCTGCGATCCGCTATGGCTTCTTTATTTACGGTAGTGCGGATGAATATTTCACCTAC
GCGTTACTGTTCCTCGGTATTTTGCTTCACGGCGTAAGTTACGATTTTTACTACGTTACC
GCTTACATCTATGTCGATAAAAAAGCCCCCGTGCATATGCGTACCGCTGCGCAGGGGCTG
ATCACGCTCTGCTGCCAGGGCTTCGGCAGTTTGCTCGGCTATCGTCTTGGCGGTGTGATG
ATGGAAAAGATGTTCGCTTATCAGGAACCGGTAAACGGACTGACTTTCAACTGGTCCGGG
ATGTGGACTTTCGGCGCGGTGATGATTGCCATTATCGCCGTGCTGTTCATGATTTTTTTC
CGCGAATCCGACAACGAAATTACGGCTATCAAGGTCGATGATCGCGATATTGCGTTGACA
CAAGGGGAAGTTAAATGA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 425 |
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Protein Molecular Weight: | 47291 |
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Protein Theoretical pI: | 10 |
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Signaling Regions: | |
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Transmembrane Regions: | |
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Protein Sequence: | >3-deoxy-D-manno-octulosonic-acid transferase
MLELLYTALLYLIQPLIWIRLWVRGRKAPAYRKRWGERYGFYRHPLKPGGIMLHSVSVGE
TLAAIPLVRALRHRYPDLPITVTTMTPTGSERVQSAFGKDVQHVYLPYDLPDALNRFLNK
VDPKLVLIMETELWPNLIAALHKRKIPLVIANARLSARSAAGYAKLGKFVRRLLRRITLI
AAQNEEDGARFVALGAKNNQVTVTGSLKFDISVTPQLAAKAVTLRRQWAPHRPVWIATST
HEGEESVVIAAHQALLQQFPNLLLILVPRHPERFPDAINLVRQAGLSYITRSSGEVPSTS
TQVVVGDTMGELMLLYGIADLAFVGGSLVERGGHNPLEAAAHAIPVLMGPHTFNFKDICA
RLEQASGLITVTDATTLAKEVSSLLTDADYRSFYGRHAVEVLYQNQGALQRLLQLLEPYL
PPKTH |
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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
- Clementz, T. (1992). "The gene coding for 3-deoxy-manno-octulosonic acid transferase and the rfaQ gene are transcribed from divergently arranged promoters in Escherichia coli." J Bacteriol 174:7750-7756. Pubmed: 1447141
- Clementz, T., Raetz, C. R. (1991). "A gene coding for 3-deoxy-D-manno-octulosonic-acid transferase in Escherichia coli. Identification, mapping, cloning, and sequencing." J Biol Chem 266:9687-9696. Pubmed: 2033061
- 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
- Katz, C., Ron, E. Z. (2008). "Dual role of FtsH in regulating lipopolysaccharide biosynthesis in Escherichia coli." J Bacteriol 190:7117-7122. Pubmed: 18776015
- Sofia, H. J., Burland, V., Daniels, D. L., Plunkett, G. 3rd, Blattner, F. R. (1994). "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Nucleic Acids Res 22:2576-2586. Pubmed: 8041620
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