PTS system mannose-specific EIIAB component (P69797)

Identification
Name:PTS system mannose-specific EIIAB component
Synonyms:
  • EIIAB-Man
  • Mannose-specific phosphotransferase enzyme IIA component
  • EIII-Man
  • PTS system mannose-specific EIIA component
  • Mannose-specific phosphotransferase enzyme IIB component
  • PTS system mannose-specific EIIB component
Gene Name:manX
Enzyme Class:
Biological Properties
General Function:Involved in phosphoenolpyruvate-dependent sugar phosphotransferase system
Specific Function:The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in mannose transport
Cellular Location:Cytoplasm. Cell inner membrane; Peripheral membrane protein
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Protein N(pi)-phospho-L-histidine+1.0Thumb ↔ 1.0Protein histidine+1.0Thumb
1.0Protein N(pi)-phospho-L-histidine + 1.0D-Mannose ↔ 1.0Protein histidine + 1.0Mannose 6-phosphate
ReactionCard
1.0Protein N(pi)-phospho-L-histidine+1.0Sugar ↔ 1.0Protein histidine+1.0Thumb
1.0Protein N(pi)-phospho-L-histidine + 1.0Sugar ↔ 1.0Protein histidine + 1.0Sugar phosphate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0HPr - phosphorylated → 1.0α-D-mannose 6-phosphate+1.0HPr
1.0D-allopyranose + 1.0HPr - phosphorylated → 1.0α-D-mannose 6-phosphate + 1.0HPr
ReactionCard
1.0β-D-fructofuranose+1.0HPr - phosphorylated+1.0Thumb → 1.0Thumb+1.0HPr
1.0β-D-fructofuranose + 1.0HPr - phosphorylated + 1.0D-Fructose → 1.0D-tagatofuranose 6-phosphate + 1.0HPr
ReactionCard
1.0D-Fructose+1.0HPr - phosphorylated+1.0Thumb → 1.0HPr+1.0Fructose 6-phosphate+1.0Thumb
1.0D-Fructose + 1.0HPr - phosphorylated + 1.0D-Fructose → 1.0HPr + 1.0Fructose 6-phosphate + 1.0Fructose 6-phosphate
ReactionCard
1.0Thumb+1.0HPr - phosphorylated → 1.0Thumb+1.0HPr
1.02-Deoxyglucose + 1.0HPr - phosphorylated → 1.02-Deoxy-D-glucose 6-phosphate + 1.0HPr
ReactionCard
1.0Thumb+1.0HPr - phosphorylated → 1.0HPr
1.0Sorbitol-6-phosphate + 1.0HPr - phosphorylated → 1.0HPr
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Phosphoenolpyruvic acid + 1.0D-Mannose → 1.0Mannose 6-phosphate + 1.0Pyruvic acid
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Phosphoenolpyruvic acid + 1.0N-Acetylmannosamine → 1.0N-Acetyl-D-mannosamine 6-phosphate + 1.0Pyruvic acid
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Phosphoenolpyruvic acid + 1.0Glucosamine → 1.0Glucosamine 6-phosphate + 1.0Pyruvic acid
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Phosphoenolpyruvic acid + 1.0D-Glucose → 1.0Glucose 6-phosphate + 1.0Pyruvic acid
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Phosphoenolpyruvic acid + 1.0D-Fructose → 1.0Fructose 6-phosphate + 1.0Pyruvic acid
ReactionCard
1.0Protein EIIA N(pi)-phospho-L-histidine+1.0protein EIIB → 1.0protein EIIA+1.0protein EIIB N(pi)-phospho-L-histidine/cysteine
1.0Protein EIIA N(pi)-phospho-L-histidine + 1.0protein EIIB → 1.0protein EIIA + 1.0protein EIIB N(pi)-phospho-L-histidine/cysteine
ReactionCard
1.0Protein EIIB N(pi)-phospho-L-histidine/cysteine+1.0Thumb → 1.0protein EIIB+1.0sugar phosphate
1.0Protein EIIB N(pi)-phospho-L-histidine/cysteine + 1.0Sucrose → 1.0protein EIIB + 1.0sugar phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB202252-Deoxy-D-glucose 6-phosphateMetaboCard
ECMDB031742-DeoxyglucoseMetaboCard
ECMDB24208D-allopyranoseMetaboCard
ECMDB00660D-FructoseMetaboCard
ECMDB00122D-GlucoseMetaboCard
ECMDB00169D-MannoseMetaboCard
ECMDB24205D-tagatofuranose 6-phosphateMetaboCard
ECMDB00124Fructose 6-phosphateMetaboCard
ECMDB01514GlucosamineMetaboCard
ECMDB01254Glucosamine 6-phosphateMetaboCard
ECMDB01401Glucose 6-phosphateMetaboCard
ECMDB01078Mannose 6-phosphateMetaboCard
ECMDB01121N-Acetyl-D-mannosamine 6-phosphateMetaboCard
ECMDB01129N-AcetylmannosamineMetaboCard
ECMDB00263Phosphoenolpyruvic acidMetaboCard
ECMDB00243Pyruvic acidMetaboCard
ECMDB01400Sorbitol-6-phosphateMetaboCard
ECMDB00258SucroseMetaboCard
GO Classification:
Component
cell part
cytoplasm
integral to membrane
intracellular part
intrinsic to membrane
membrane part
Function
carbohydrate transmembrane transporter activity
catalytic activity
phosphotransferase activity, alcohol group as acceptor
protein-N(PI)-phosphohistidine-sugar phosphotransferase activity
substrate-specific transmembrane transporter activity
transferase activity
transferase activity, transferring phosphorus-containing groups
transmembrane transporter activity
transporter activity
Process
carbohydrate transport
establishment of localization
phosphoenolpyruvate-dependent sugar phosphotransferase system
transport
Gene Properties
Blattner:b1817
Gene OrientationClockwise
Centisome Percentage:40.95
Left Sequence End1900072
Right Sequence End1901043
Gene Sequence:
>972 bp
GTGGCACAGGAATATACTGTTGAACAACTAAACCACGGCCGTAAAGTCTATGACTTTATG
CGCTGGGACTACTGGGCTTTCGGCATCTCTGGTCTGCTGTTAATCGCTGCTATCGTTATT
ATGGGCGTGCGCGGCTTTAACTGGGGGCTGGATTTCACCGGTGGTACGGTTATTGAAATT
ACGCTCGAAAAACCGGCTGAAATTGACGTAATGCGTGATGCATTGCAAAAAGCCGGTTTT
GAAGAGCCGATGCTGCAAAACTTTGGTAGCAGCCATGACATCATGGTCCGTATGCCGCCT
GCTGAAGGCGAAACCGGCGGTCAGGTGTTGGGCAGCCAGGTTCTGAAGGTGATTAACGAA
TCCACCAATCAGAATGCAGCAGTGAAGCGTATTGAGTTCGTCGGTCCGAGCGTGGGGGCA
GACCTTGCGCAAACCGGTGCGATGGCGTTGATGGCAGCGCTGCTGTCTATCCTCGTGTAC
GTAGGTTTCCGCTTTGAGTGGCGACTGGCGGCAGGGGTGGTTATTGCGCTGGCGCACGAC
GTTATCATTACGCTGGGTATTTTGTCGTTATTCCATATCGAGATTGACCTGACCATTGTG
GCATCGTTGATGTCGGTTATCGGTTACTCGCTTAACGACAGTATCGTGGTATCGGACCGT
ATTCGTGAAAACTTCCGCAAGATCCGTCGCGGTACGCCTTACGAAATCTTTAACGTGTCC
TTGACCCAGACGCTGCACCGTACCTTGATCACATCCGGTACTACCTTGATGGTTATCCTG
ATGCTGTACCTCTTCGGTGGTCCGGTACTGGAAGGCTTCTCGCTGACCATGCTTATCGGT
GTTTCCATCGGTACTGCATCTTCCATCTATGTGGCATCTGCGTTGGCTCTGAAACTGGGT
ATGAAGCGCGAACACATGTTGCAGCAGAAAGTGGAAAAAGAAGGGGCGGATCAGCCGTCA
ATTCTGCCGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:323
Protein Molecular Weight:35047
Protein Theoretical pI:6
PDB File:1VRC
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>PTS system mannose-specific EIIAB component
MTIAIVIGTHGWAAEQLLKTAEMLLGEQENVGWIDFVPGENAETLIEKYNAQLAKLDTTK
GVLFLVDTWGGSPFNAASRIVVDKEHYEVIAGVNIPMLVETLMARDDDPSFDELVALAVE
TGREGVKALKAKPVEKAAPAPAAAAPKAAPTPAKPMGPNDYMVIGLARIDDRLIHGQVAT
RWTKETNVSRIIVVSDEVAADTVRKTLLTQVAPPGVTAHVVDVAKMIRVYNNPKYAGERV
MLLFTNPTDVERLVEGGVKITSVNVGGMAFRQGKTQVNNAVSVDEKDIEAFKKLNARGIE
LEVRKVSTDPKLKMMDLISKIDK
References
External Links:
ResourceLink
Uniprot ID:P69797
Uniprot Name:PTNAB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674549
PDB ID:1VRC
Ecogene ID:EG10567
Ecocyc:EG10567
ColiBase:b1817
Kegg Gene:b1817
EchoBASE ID:EB0562
CCDB:PTNAB_ECOLI
BacMap:16129771
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
  • Erni, B., Zanolari, B., Kocher, H. P. (1987). "The mannose permease of Escherichia coli consists of three different proteins. Amino acid sequence and function in sugar transport, sugar phosphorylation, and penetration of phage lambda DNA." J Biol Chem 262:5238-5247. Pubmed: 2951378
  • Gschwind, R. M., Gemmecker, G., Leutner, M., Kessler, H., Gutknecht, R., Lanz, R., Flukiger, K., Erni, B. (1997). "Secondary structure of the IIB domain of the Escherichia coli mannose transporter, a new fold in the class of alpha/beta twisted open-sheet structures." FEBS Lett 404:45-50. Pubmed: 9074635
  • 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
  • Itoh, T., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Kasai, H., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Seki, Y., Horiuchi, T., et, a. l. .. (1996). "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." DNA Res 3:379-392. Pubmed: 9097040
  • 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
  • Markovic-Housley, Z., Balbach, J., Stolz, B., Genovesio-Taverne, J. C. (1994). "Predicted topology of the N-terminal domain of the hydrophilic subunit of the mannose transporter of Escherichia coli." FEBS Lett 340:202-206. Pubmed: 8131846
  • Nunn, R. S., Markovic-Housley, Z., Genovesio-Taverne, J. C., Flukiger, K., Rizkallah, P. J., Jansonius, J. N., Schirmer, T., Erni, B. (1996). "Structure of the IIA domain of the mannose transporter from Escherichia coli at 1.7 angstroms resolution." J Mol Biol 259:502-511. Pubmed: 8676384
  • Stenberg, F., Chovanec, P., Maslen, S. L., Robinson, C. V., Ilag, L. L., von Heijne, G., Daley, D. O. (2005). "Protein complexes of the Escherichia coli cell envelope." J Biol Chem 280:34409-34419. Pubmed: 16079137
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842