Glutamate/aspartate transport ATP-binding protein gltL (P0AAG3)

Identification
Name:Glutamate/aspartate transport ATP-binding protein gltL
Synonyms:Not Available
Gene Name:gltL
Enzyme Class:Not Available
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:Part of the binding-protein-dependent transport system for glutamate and aspartate. Probably responsible for energy coupling to the transport system
Cellular Location:Cell inner membrane; Peripheral membrane protein (Potential)
SMPDB Pathways:
KEGG Pathways:
SMPDB Reactions:
1.0L-Glutamic acid+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Adenosine diphosphate+1.0Thumb+1.0Thumb+1.0L-Glutamic acid+1.0Thumb
1.0L-Glutamic acid + 1.0Adenosine triphosphate + 1.0Water + 1.0L-Glutamate → 1.0Adenosine diphosphate + 1.0Phosphate + 1.0Hydrogen ion + 1.0L-Glutamic acid + 1.0ADP
ReactionCard
1.0L-Aspartic acid+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Adenosine diphosphate+1.0Thumb+1.0Thumb+1.0L-Aspartic acid+1.0Thumb
1.0L-Aspartic acid + 1.0Adenosine triphosphate + 1.0Water + 1.0L-Aspartic acid → 1.0Adenosine diphosphate + 1.0Phosphate + 1.0Hydrogen ion + 1.0L-Aspartic acid + 1.0ADP
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.0L-Glutamate → 1.0ADP + 1.0L-Glutamate + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.0L-Aspartic acid → 1.0ADP + 1.0L-Aspartic acid + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00191L-Aspartic acidMetaboCard
ECMDB00148L-GlutamateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
ATPase activity
binding
catalytic activity
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
nucleoside binding
nucleoside-triphosphatase activity
nucleotide binding
purine nucleoside binding
pyrophosphatase activity
Gene Properties
Blattner:b0652
Gene OrientationCounterclockwise
Centisome Percentage:14.74
Left Sequence End683753
Right Sequence End684478
Gene Sequence:
>726 bp
ATGGCAACTGTTTCCATGCGCGACATGCTCAAGGCTGGTGTTCACTTCGGTCACCAGACC
CGTTACTGGAACCCGAAAATGAAGCCGTTCATCTTCGGTGCGCGTAACAAAGTTCACATC
ATCAACCTTGAGAAAACTGTACCGATGTTCAACGAAGCTCTGGCTGAACTGAACAAGATT
GCTTCTCGCAAAGGTAAAATCCTTTTCGTTGGTACTAAACGCGCTGCAAGCGAAGCGGTG
AAAGACGCTGCTCTGAGCTGCGACCAGTTCTTCGTGAACCATCGCTGGCTGGGCGGTATG
CTGACTAACTGGAAAACCGTTCGTCAGTCCATCAAACGTCTGAAAGACCTGGAAACTCAG
TCTCAGGACGGTACTTTCGACAAGCTGACCAAGAAAGAAGCGCTGATGCGCACTCGTGAG
CTGGAGAAACTGGAAAACAGCCTGGGCGGTATCAAAGACATGGGCGGTCTGCCGGACGCT
CTGTTTGTAATCGATGCTGACCACGAACACATTGCTATCAAAGAAGCAAACAACCTGGGT
ATTCCGGTATTTGCTATCGTTGATACCAACTCTGATCCGGACGGTGTTGACTTCGTTATC
CCGGGTAACGACGACGCAATCCGTGCTGTGACCCTGTACCTGGGCGCTGTTGCTGCAACC
GTACGTGAAGGCCGTTCTCAGGATCTGGCTTCCCAGGCGGAAGAAAGCTTCGTAGAAGCT
GAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:241
Protein Molecular Weight:26661
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Glutamate/aspartate transport ATP-binding protein gltL
MITLKNVSKWYGHFQVLTDCSTEVKKGEVVVVCGPSGSGKSTLIKTVNGLEPVQQGEITV
DGIVVNDKKTDLAKLRSRVGMVFQHFELFPHLSIIENLTLAQVKVLKRDKAPAREKALKL
LERVGLSAHANKFPAQLSGGQQQRVAIARALCMDPIAMLFDEPTSALDPEMINEVLDVMV
ELANEGMTMMVVTHEMGFARKVANRVIFMDEGKIVEDSPKDAFFDDPKSDRAKDFLAKIL
H
References
External Links:
ResourceLink
Uniprot ID:P0AAG3
Uniprot Name:GLTL_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21239023
Ecogene ID:EG12663
Ecocyc:EG12663
ColiBase:b0652
Kegg Gene:b0652
EchoBASE ID:EB2529
CCDB:GLTL_ECOLI
BacMap:16128635
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
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232