Members of the Alanine or Glycine:Cation Symporter (AGCS) Family (TC# 2.A.25) transport alanine and/or glycine in symport with Na+ and or H+.
| Alanine/glycine:cation symporter (AGCS) family protein | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | A3P053 | ||||||||
| Pfam | PF01235 | ||||||||
| InterPro | IPR001463 | ||||||||
| PROSITE | PS00873 | ||||||||
| |||||||||
Structure and function
editKnown proteins in the AGCS family are between 445 and 550 amino acyl residues in length and possess 8 to 12 putative transmembrane α-helical spanners. Members may possess 11 transmembrane segments (TMSs), as seems to be true for DagA (TC# 2.A.25.1.1) and AgcS (TC# 2.A.25.1.3), although Acp (TC# 2.A.25.1.2) has only 8 TMSs, perhaps the result of truncation. As of early 2016, there does not appear to be any 3D crystal structure data available for these proteins. Members of the AGCS family have been found in bacteria and archaea, such as extremophile halotolerant cyanobacterium Aphanothece halophytica, and thermophilic bacteria, Bacillus PS3.[1][2] As of 2015, only three members of the family have been functionally characterized. These proteins show limited sequence similarity in the APC family (TC# 2.A.3).[3] High-resolution structures of AgcS from Methanococcus maripaludis were obtained using X-ray crystallography and released in 2019 and show structural homology to other members of the Amino acid-Polyamine-Organocation superfamily of transporters.[4]
Transport reaction
editThe generalized transport reaction catalyzed by the AGCS family is:[3]
alanine or glycine (out) + Na+ or H+ (out) → alanine or glycine (in) + Na+ or H+ (in).
Proteins in the AGCS family
editThere are currently 10 proteins belonging to the AGCS family. These proteins and their descriptions can be found in the Transporter Classification Database.
References
edit- ^ Bualuang A, Kageyama H, Tanaka Y, Incharoensakdi A, Takabe T (2015). "Functional characterization of a member of alanine or glycine: cation symporter family in halotolerant cyanobacterium Aphanothece halophytica". Bioscience, Biotechnology, and Biochemistry. 79 (2): 230–5. doi:10.1080/09168451.2014.968091. PMID 25421789. S2CID 205616830.
- ^ Kanamori M, Kamata H, Yagisawa H, Hirata H (March 1999). "Overexpression of the alanine carrier protein gene from thermophilic bacterium PS3 in Escherichia coli". Journal of Biochemistry. 125 (3): 454–9. doi:10.1093/oxfordjournals.jbchem.a022308. PMID 10050032.
- ^ a b Saier MH. "2.A.25 The Alanine or Glycine:Cation Symporter (AGCS) Family". Transporter Classification Database. Saier Lab Bioinformatics Group / SDSC.
- ^ Ma J, Lei HT, Reyes FE, Sanchez-Martinez S, Sarhan MF, Hattne J, Gonen T (February 2019). "Structural basis for substrate binding and specificity of a sodium-alanine symporter AgcS". Proceedings of the National Academy of Sciences of the United States of America. 116 (6): 2086–2090. Bibcode:2019PNAS..116.2086M. doi:10.1073/pnas.1806206116. PMC 6369739. PMID 30659158.
Further reading
edit- Rodionov DA, Hebbeln P, Eudes A, ter Beek J, Rodionova IA, Erkens GB, et al. (January 2009). "A novel class of modular transporters for vitamins in prokaryotes". Journal of Bacteriology. 191 (1): 42–51. doi:10.1128/JB.01208-08. PMC 2612444. PMID 18931129.
- Kamata H, Akiyama S, Morosawa H, Ohta T, Hamamoto T, Kambe T, et al. (October 1992). "Primary structure of the alanine carrier protein of thermophilic bacterium PS3". The Journal of Biological Chemistry. 267 (30): 21650–5. doi:10.1016/S0021-9258(19)36661-X. PMID 1400476.
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