L-arabinose-binding periplasmic protein (P02924)

Identification
Name:L-arabinose-binding periplasmic protein
Synonyms:
  • ABP
Gene Name:araF
Enzyme Class:Not Available
Biological Properties
General Function:Carbohydrate transport and metabolism
Specific Function:Involved in the high-affinity L-arabinose membrane transport system. Binds with high affinity to arabinose, but can also bind D-galactose (approximately 2-fold reduction) and D- fucose (approximately 40-fold reduction)
Cellular Location:Periplasm
SMPDB Pathways:Not Available
KEGG Pathways:
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.0L-Arabinose → 1.0ADP + 1.0L-Arabinose + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00646L-ArabinoseMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:Not Available
Gene Properties
Blattner:b1901
Gene OrientationCounterclockwise
Centisome Percentage:42.74
Left Sequence End1983163
Right Sequence End1984152
Gene Sequence:
>990 bp
ATGGCTTCACAACTGACTGATGCATTTGCGCGTAAGTTTTACTACTTGCGCCTGTCGATT
ACCGATGTGTGTAACTTTCGTTGCACCTACTGCCTGCCGGATGGCTACAAACCGAGCGGC
GTCACCAATAAAGGCTTTCTTACCGTCGATGAAATTCGCCGGGTTACGCGCGCCTTCGCC
AGACTGGGCACCGAAAAAGTGCGCCTGACAGGAGGAGAGCCGTCTTTACGCCGCGACTTT
ACCGATATCATCGCCGCTGTGCGGGAAAACGACGCTATCCGCCAGATTGCGGTCACAACC
AATGGTTACCGTCTGGAACGCGATGTGGCGAGCTGGCGCGATGCGGGACTTACTGGCATT
AACGTCAGTGTCGACAGTCTGGACGCCCGCCAGTTTCACGCTATTACCGGGCAGGATAAA
TTCAACCAGGTCATGGCAGGGATTGATGCTGCATTTGAGGCCGGTTTTGAGAAGGTCAAA
GTCAATACCGTGCTGATGCGTGATGTTAATCATCACCAGCTCGACACCTTTCTGAACTGG
ATCCAGCATCGCCCTATCCAGCTGCGTTTCATCGAACTGATGGAAACGGGCGAGGGCAGC
GAGCTCTTCCGTAAGCATCACATCTCTGGTCAGGTTCTGCGTGACGAGCTACTGCGTCGC
GGCTGGATCCACCAATTACGTCAACGCAGCGACGGTCCCGCGCAAGTCTTTTGCCATCCA
GATTACGCCGGAGAGATTGGCCTTATCATGCCGTATGAAAAAGACTTCTGCGCCACTTGC
AACCGCCTGCGCGTTTCCTCCATTGGTAAACTCCATCTCTGCCTGTTTGGTGAAGGCGGC
GTTAACCTGCGCGATCTGCTGGAAGACGATACCCAGCAACAGGCGCTGGAAGCGCGTATT
TCAGCGGCGCTGCGGGAGAAGAAACAGACCCATTTCCTGCATCAAAACAACACCGGTATT
ACGCAAAACTTATCGTACATTGGCGGCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:329
Protein Molecular Weight:35541
Protein Theoretical pI:7
PDB File:1ABE
Signaling Regions:
  • 1-23
Transmembrane Regions:
  • None
Protein Sequence:
>L-arabinose-binding periplasmic protein
MHKFTKALAAIGLAAVMSQSAMAENLKLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIK
IAVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGSAIVAKARGYDMKVIAVDDQFVNAKG
KPMDTVPLVMMAATKIGERQGQELYKEMQKRGWDVKESAVMAITANELDTARRRTTGSMD
ALKAAGFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKHWLIVGMNDSTVLGGVRATE
GQGFKAADIIGIGINGVDAVSELSKAQATGFYGSLLPSPDVHGYKSSEMLYNWVAKDVEP
PKFTEVTDVVLITRDNFKEELEKKGLGGK
References
External Links:
ResourceLink
Uniprot ID:P02924
Uniprot Name:ARAF_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651354
PDB ID:1ABE
Ecogene ID:EG10057
Ecocyc:EG10057
ColiBase:b1901
Kegg Gene:b1901
EchoBASE ID:EB0055
CCDB:ARAF_ECOLI
BacMap:16129851
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
  • 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
  • Hogg, R. W., Hermodson, M. A. (1977). "Amino acid sequence of the L-arabinose-binding protein from Escherichia coli B/r." J Biol Chem 252:5135-5141. Pubmed: 326784
  • 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
  • Newcomer, M. E., Gilliland, G. L., Quiocho, F. A. (1981). "L-Arabinose-binding protein-sugar complex at 2.4 A resolution. Stereochemistry and evidence for a structural change." J Biol Chem 256:13213-13217. Pubmed: 7031057
  • Quiocho, F. A., Gilliland, G. L., Phillips, G. N. Jr (1977). "The 2.8-A resolution structure of the L-arabinose-binding protein from Escherichia coli. Polypeptide chain folding, domain similarity, and probable location of sugar-binding site." J Biol Chem 252:5142-5149. Pubmed: 326785
  • Scripture, J. B., Hogg, R. W. (1983). "The nucleotide sequences defining the signal peptides of the galactose-binding protein and the arabinose-binding protein." J Biol Chem 258:10853-10855. Pubmed: 6885805
  • Scripture, J. B., Voelker, C., Miller, S., O'Donnell, R. T., Polgar, L., Rade, J., Horazdovsky, B. F., Hogg, R. W. (1987). "High-affinity L-arabinose transport operon. Nucleotide sequence and analysis of gene products." J Mol Biol 197:37-46. Pubmed: 2445996
  • Vermersch, P. S., Tesmer, J. J., Lemon, D. D., Quiocho, F. A. (1990). "A Pro to Gly mutation in the hinge of the arabinose-binding protein enhances binding and alters specificity. Sugar-binding and crystallographic studies." J Biol Chem 265:16592-16603. Pubmed: 2204627