Phosphoethanolamine transferase eptB (P37661)

Identification
Name:Phosphoethanolamine transferase eptB
Synonyms:Not Available
Gene Name:eptB
Enzyme Class:Not Available
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Catalyzes the addition of a phosphoethanolamine (pEtN) moiety to the outer 3-deoxy-D-manno-octulosonic acid (KDO) residue of a KDO(2)-lipid A. Phosphatidylethanolamines with one unsaturated acyl group functions as pEtN donors and the reaction releases diacylglycerol
Cellular Location:Cell inner membrane; Multi-pass membrane protein
SMPDB Pathways:
KEGG Pathways:
  • Lipopolysaccharide biosynthesis ec00540
SMPDB Reactions:
1.0a-Kdo-(2->4)-a-Kdo-(2->6)-lipid IVA+1.0Thumb+1.0Thumb → 1.0Thumb+1.0phosphoethanolamine-Kdo2-lipid A+1.0Thumb
1.0a-Kdo-(2->4)-a-Kdo-(2->6)-lipid IVA + 1.0PE(12:0/10:0) + 1.0a-Kdo-(2->4)-a-Kdo-(2->6)-lipid IVA → 1.01,2-Diacyl-sn-glycerol (didodecanoyl, n-C12:0) + 1.0phosphoethanolamine-Kdo2-lipid A + 1.0Phosphoethanolamine KDO(2)-lipid (A)
ReactionCard
1.0Thumb+1.0a-Kdo-(2->4)-a-Kdo-(2->6)-lipid IVA+1.0Thumb → 1.0phosphoethanolamine-Kdo2-lipid A+1.01,2-dihexadecanoyl-rac-glycerol+1.0Thumb
1.0PE(16:0/16:0) + 1.0a-Kdo-(2->4)-a-Kdo-(2->6)-lipid IVA + 1.0a-Kdo-(2->4)-a-Kdo-(2->6)-lipid IVA → 1.0phosphoethanolamine-Kdo2-lipid A + 1.01,2-dihexadecanoyl-rac-glycerol + 1.0Phosphoethanolamine KDO(2)-lipid (A)
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0α-Kdo-(2->4)-α-Kdo-(2->6)-lipid IVA ? 1.0a 1,2-diacylglycerol+1.0phosphatidylethanolamine-KDO2-lipidA
1.0PE(14:0/14:0) + 1.0α-Kdo-(2->4)-α-Kdo-(2->6)-lipid IVA ? 1.0a 1,2-diacylglycerol + 1.0phosphatidylethanolamine-KDO2-lipidA
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0KDO2-Lipid A + 1.0PE(14:0/14:0) → 1.01,2-Diacyl-sn-glycerol (dihexadec-9-enoyl, n-C16:1) + 1.0Phosphoethanolamine KDO(2)-lipid (A)
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0KDO2-Lipid A + 1.0PE(14:0/14:0) → 1.01,2-Diacyl-sn-glycerol (dioctadec-11-enoyl, n-C18:1) + 1.0Phosphoethanolamine KDO(2)-lipid (A)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB211031,2-Diacyl-sn-glycerol (didodecanoyl, n-C12:0)MetaboCard
ECMDB211041,2-Diacyl-sn-glycerol (dihexadec-9-enoyl, n-C16:1)MetaboCard
ECMDB211061,2-Diacyl-sn-glycerol (dioctadec-11-enoyl, n-C18:1)MetaboCard
ECMDB24178a-Kdo-(2->4)-a-Kdo-(2->6)-lipid IVAMetaboCard
ECMDB21031KDO2-Lipid AMetaboCard
ECMDB21417O-PhosphoethanolamineMetaboCard
ECMDB21599PE(12:0/10:0)MetaboCard
ECMDB08821PE(14:0/14:0)MetaboCard
ECMDB08923PE(16:0/16:0)MetaboCard
ECMDB21352Phosphoethanolamine KDO(2)-lipid (A)MetaboCard
GO Classification:
Component
cell part
integral to membrane
intrinsic to membrane
membrane part
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on ester bonds
sulfuric ester hydrolase activity
Process
metabolic process
Gene Properties
Blattner:b3546
Gene OrientationCounterclockwise
Centisome Percentage:79.89
Left Sequence End3706807
Right Sequence End3708498
Gene Sequence:
>1692 bp
ATGAGATACATCAAATCGATTACACAGCAGAAGCTGAGCTTTTTGCTTGCAATCTATATT
GGCCTTTTTATGAATGGCGCGGTTTTTTACCGCCGCTTCGGCAGCTATGCGCACGATTTT
ACCGTCTGGAAAGGCATTTCTGCTGTTGTTGAACTGGCCGCCACCGTACTGGTGACCTTC
TTTTTACTACGTCTTCTTTCGCTGTTTGGCCGCCGCAGCTGGCGTATTCTGGCATCGCTG
GTGGTGCTCTTTTCCGCAGGTGCCAGCTATTACATGACCTTCCTTAATGTGGTCATTGGT
TATGGCATCATCGCTTCCGTCATGACCACCGATATCGACCTGTCAAAAGAAGTTGTTGGT
CTGAACTTTATTCTCTGGTTAATCGCCGTTAGTGCATTGCCTCTTATCCTTATCTGGAAT
AACCGCTGTCGCTACACCTTGCTCCGACAACTGCGAACCCCAGGGCAGCGTATTCGCAGC
CTGGCGGTCGTCGTACTGGCGGGTATTATGGTTTGGGCACCGATTCGTTTGCTGGATATC
CAGCAGAAGAAAGTGGAGAGGGCGACCGGCGTTGATTTGCCGAGTTATGGCGGTGTCGTA
GCGAACTCTTATCTGCCATCAAACTGGCTTTCTGCGTTGGGGCTGTATGCCTGGGCGCGG
GTCGATGAATCTTCCGATAATAATTCATTGCTTAATCCGGCGAAGAAATTCACTTATCAG
GCACCGCAAAACGTTGATGACACTTATGTCGTGTTTATCATCGGTGAAACCACGCGTTGG
GACCATATGGGTATTTTCGGCTATGAGCGTAATACCACGCCGAAACTGGCCCAGGAGAAA
AATCTGGCGGCGTTCCGTGGTTACTCCTGTGATACCGCAACCAAACTCTCACTGCGTTGC
ATGTTTGTACGTCAGGGGGGCGCGGAAGATAATCCGCAGCGCACATTAAAAGAACAGAAC
ATTTTCGCGGTTCTGAAGCAGTTAGGATTCAGTTCTGACCTCTACGCTATGCAGAGCGAA
ATGTGGTTCTACAGCAACACGATGGCGGACAACATTGCTTATCGTGAGCAGATTGGTGCG
GAGCCACGTAATCGTGGCAAGCCGGTAGATGATATGTTGCTGGTAGACGAAATGCAGCAA
TCGCTAGGGCGCAACCCGGATGGTAAGCATCTGATCATTCTGCATACCAAAGGTTCGCAT
TTTAACTACACCCAGCGTTATCCGCGTAGCTTCGCGCAGTGGAAGCCGGAATGTATTGGT
GTTGATAGCGGCTGTACCAAAGCGCAGATGATCAACTCCTATGACAACTCGGTGACCTAT
GTGGATCACTTTATCTCCAGCGTGATTGATCAGGTTCGCGATAAGAAAGCGATTGTGTTC
TACGCAGCTGACCACGGTGAGTCAATTAATGAACGCGAGCACCTGCACGGCACGCCGCGT
GAACTGGCACCGCCGGAGCAGTTCCGCGTACCGATGATGGTCTGGATGTCAGATAAATAT
CTGGAAAATCCGGCCAATGCGCAGGCGTTTGCGCAGCTGAAAAAAGAAGCCGACATGAAA
GTGCCACGCCGTCACGTAGAGCTGTACGATACCATCATGGGTTGTCTTGGCTATACTTCA
CCGGATGGTGGAATTAACGAAAACAACAACTGGTGTCACATCCCGCAGGCAAAAGAGGCA
GCGGCTAACTAA
Protein Properties
Pfam Domain Function:
Protein Residues:563
Protein Molecular Weight:63804
Protein Theoretical pI:9
Signaling Regions:
  • None
Transmembrane Regions:
  • 10-30
  • 49-69
  • 80-100
  • 118-138
  • 160-180
Protein Sequence:
>Phosphoethanolamine transferase eptB
MRYIKSITQQKLSFLLAIYIGLFMNGAVFYRRFGSYAHDFTVWKGISAVVELAATVLVTF
FLLRLLSLFGRRSWRILASLVVLFSAGASYYMTFLNVVIGYGIIASVMTTDIDLSKEVVG
LNFILWLIAVSALPLILIWNNRCRYTLLRQLRTPGQRIRSLAVVVLAGIMVWAPIRLLDI
QQKKVERATGVDLPSYGGVVANSYLPSNWLSALGLYAWARVDESSDNNSLLNPAKKFTYQ
APQNVDDTYVVFIIGETTRWDHMGIFGYERNTTPKLAQEKNLAAFRGYSCDTATKLSLRC
MFVRQGGAEDNPQRTLKEQNIFAVLKQLGFSSDLYAMQSEMWFYSNTMADNIAYREQIGA
EPRNRGKPVDDMLLVDEMQQSLGRNPDGKHLIILHTKGSHFNYTQRYPRSFAQWKPECIG
VDSGCTKAQMINSYDNSVTYVDHFISSVIDQVRDKKAIVFYAADHGESINEREHLHGTPR
ELAPPEQFRVPMMVWMSDKYLENPANAQAFAQLKKEADMKVPRRHVELYDTIMGCLGYTS
PDGGINENNNWCHIPQAKEAAAN
References
External Links:
ResourceLink
Uniprot ID:P37661
Uniprot Name:EPTB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85676499
Ecogene ID:EG12267
Ecocyc:EG12267
ColiBase:b3546
Kegg Gene:b3546
EchoBASE ID:EB2176
CCDB:EPTB_ECOLI
BacMap:90111611
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
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Reynolds, C. M., Kalb, S. R., Cotter, R. J., Raetz, C. R. (2005). "A phosphoethanolamine transferase specific for the outer 3-deoxy-D-manno-octulosonic acid residue of Escherichia coli lipopolysaccharide. Identification of the eptB gene and Ca2+ hypersensitivity of an eptB deletion mutant." J Biol Chem 280:21202-21211. Pubmed: 15795227
  • 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