3-deoxy-D-manno-octulosonic-acid transferase (P0AC75)

Identification
Name:3-deoxy-D-manno-octulosonic-acid transferase
Synonyms:
  • KDO transferase
Gene Name:waaA
Enzyme Class:
Biological Properties
General Function:Involved in biosynthetic process
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
Cellular Location:Cell inner membrane; Single-pass membrane protein (Probable)
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.02,3,2'3'-Tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate + 1.0CMP-3-Deoxy-D-manno-octulosonate + 1.02,3,2'3'-Tetrakis(beta-hydroxymyristoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate ↔ 1.0KDO-lipid IV(A) + 1.0Cytidine monophosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Di[3-deoxy-D-manno-octulosonyl]-lipid IV(A)+1.0Thumb
1.0KDO-lipid IV(A) + 1.0CMP-3-Deoxy-D-manno-octulosonate ↔ 1.0Di[3-deoxy-D-manno-octulosonyl]-lipid IV(A) + 1.0Cytidine monophosphate
ReactionCard
1.0Di[3-deoxy-D-manno-octulosonyl]-lipid IV(A)+1.0Thumb ↔ 1.0alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA+1.0Thumb
1.0Di[3-deoxy-D-manno-octulosonyl]-lipid IV(A) + 1.0CMP-3-Deoxy-D-manno-octulosonate ↔ 1.0alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + 1.0Cytidine monophosphate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Cytidine monophosphate+1.0Thumb+1.0Thumb+1.0Thumb
1.0CMP-3-Deoxy-D-manno-octulosonate + 1.0(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) → 1.0Cytidine monophosphate + 1.0Hydrogen ion + 1.0alpha-Kdo-(2→6)-lipid IVA + 1.0Cytidine monophosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Cytidine monophosphate+1.0Thumb+1.0a-Kdo-(2->4)-a-Kdo-(2->6)-lipid IVA+1.0Thumb+1.0Thumb
1.0alpha-Kdo-(2→6)-lipid IVA + 1.0CMP-3-Deoxy-D-manno-octulosonate → 1.0Cytidine monophosphate + 1.0Hydrogen ion + 1.0a-Kdo-(2->4)-a-Kdo-(2->6)-lipid IVA + 1.0Cytidine monophosphate + 1.0a-Kdo-(2->4)-a-Kdo-(2->6)-lipid IVA
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0lipid IVA ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0CMP-3-Deoxy-D-manno-octulosonate + 1.0lipid IVA ↔ 1.0Hydrogen ion + 1.0KDO-lipid IV(A) + 1.0Cytidine monophosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0α-Kdo-(2->4)-α-Kdo-(2->6)-lipid IVA+1.0Thumb
1.0KDO-lipid IV(A) + 1.0CMP-3-Deoxy-D-manno-octulosonate ↔ 1.0Hydrogen ion + 1.0α-Kdo-(2->4)-α-Kdo-(2->6)-lipid IVA + 1.0Cytidine monophosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0CMP-3-Deoxy-D-manno-octulosonate + 1.02,3,2'3'-Tetrakis(beta-hydroxymyristoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate → 1.0Cytidine monophosphate + 1.0Hydrogen ion + 1.0KDO-lipid IV(A)
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0CMP-3-Deoxy-D-manno-octulosonate + 1.0KDO-lipid IV(A) → 1.0Cytidine monophosphate + 1.0Hydrogen ion + 1.0KDO(2)-lipid IV(A)
ReactionCard
1.0Thumb+1.0Thumb → 1.0alpha-Kdo-(2->6)-lipid IV(A)+1.0Thumb
1.02,3,2'3'-Tetrakis(beta-hydroxymyristoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate + 1.0CMP-3-Deoxy-D-manno-octulosonate → 1.0alpha-Kdo-(2->6)-lipid IV(A) + 1.0Cytidine monophosphate
ReactionCard
1.0Alpha-Kdo-(2->6)-lipid IV(A)+1.0Thumb → 1.0alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IV(A)+1.0Thumb
1.0Alpha-Kdo-(2->6)-lipid IV(A) + 1.0CMP-3-Deoxy-D-manno-octulosonate → 1.0alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IV(A) + 1.0Cytidine monophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
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
ECMDB200572,3,2'3'-Tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphateMetaboCard
ECMDB211362,3,2'3'-Tetrakis(beta-hydroxymyristoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphateMetaboCard
ECMDB24178a-Kdo-(2->4)-a-Kdo-(2->6)-lipid IVAMetaboCard
ECMDB24218alpha-Kdo-(2→6)-lipid IVAMetaboCard
ECMDB20133CMP-3-Deoxy-D-manno-octulosonateMetaboCard
ECMDB00095Cytidine monophosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21235KDO(2)-lipid IV(A)MetaboCard
ECMDB21236KDO-lipid IV(A)MetaboCard
GO Classification:
Function
binding
carbohydrate binding
catalytic activity
sugar binding
transferase activity
Process
biosynthetic process
carbohydrate metabolic process
metabolic process
primary metabolic process
Gene Properties
Blattner:b3633
Gene OrientationClockwise
Centisome Percentage:82.04
Left Sequence End3806563
Right Sequence End3807840
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
Protein Properties
Pfam Domain Function:
Protein Residues:425
Protein Molecular Weight:47291
Protein Theoretical pI:10
Signaling Regions:
  • None
Transmembrane Regions:
  • 1-20
Protein Sequence:
>3-deoxy-D-manno-octulosonic-acid transferase
MLELLYTALLYLIQPLIWIRLWVRGRKAPAYRKRWGERYGFYRHPLKPGGIMLHSVSVGE
TLAAIPLVRALRHRYPDLPITVTTMTPTGSERVQSAFGKDVQHVYLPYDLPDALNRFLNK
VDPKLVLIMETELWPNLIAALHKRKIPLVIANARLSARSAAGYAKLGKFVRRLLRRITLI
AAQNEEDGARFVALGAKNNQVTVTGSLKFDISVTPQLAAKAVTLRRQWAPHRPVWIATST
HEGEESVVIAAHQALLQQFPNLLLILVPRHPERFPDAINLVRQAGLSYITRSSGEVPSTS
TQVVVGDTMGELMLLYGIADLAFVGGSLVERGGHNPLEAAAHAIPVLMGPHTFNFKDICA
RLEQASGLITVTDATTLAKEVSSLLTDADYRSFYGRHAVEVLYQNQGALQRLLQLLEPYL
PPKTH
References
External Links:
ResourceLink
Uniprot ID:P0AC75
Uniprot Name:KDTA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1736823
Ecogene ID:EG10520
Ecocyc:EG10520
ColiBase:b3633
Kegg Gene:b3633
EchoBASE ID:EB0515
CCDB:KDTA_ECOLI
BacMap:16131504
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