| Revision as of 07:50, 26 July 2016 editRjwilmsi (talk | contribs)Extended confirmed users, Pending changes reviewers, Rollbackers932,073 editsm →Structure and function: Journal cites, Added 1 doi to a journal cite using AWB (12058)← Previous edit | Revision as of 10:26, 30 July 2016 edit undoRjwilmsi (talk | contribs)Extended confirmed users, Pending changes reviewers, Rollbackers932,073 editsm Journal cites:, added 1 PMC using AWB (12061)Next edit → | ||
| Line 19: | Line 19: | ||
| ==Structure and function== | ==Structure and function== | ||
| Known 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 () and AgcS (), although Acp () 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''.<ref name="Bualuang">{{cite journal|last1 = Bualuang|first1 = A|last2 = Kageyama|first2 = H|last3 = Tanaka|first3 = Y|last4 = Incharoensakdi|first4 = A|last5 = Takabe|first5 = T|title = Functional characterization of a member of alanine or glycine: cation symporter family in halotolerant cyanobacterium Aphanothece halophytica.|date = 2015|volume = 79|issue = 2|pages = 230–5|doi = 10.1080/09168451.2014.968091|pmid = 25421789}}</ref><ref>{{Cite journal|title = Overexpression of the alanine carrier protein gene from thermophilic bacterium PS3 in Escherichia coli|url = http://www.ncbi.nlm.nih.gov/pubmed/10050032|journal = Journal of Biochemistry|date = 1999-03-01|issn = 0021-924X|pmid = 10050032|pages = 454–459|volume = 125|issue = 3|first = M.|last = Kanamori|first2 = H.|last2 = Kamata|first3 = H.|last3 = Yagisawa|first4 = H.|last4 = Hirata|doi=10.1093/oxfordjournals.jbchem.a022308}}</ref> As of 2015, only three members of the family have been functionally characterized. These proteins show limited sequence similarity in the APC family ().<ref name=TCDB/> As of early 2016, there do not appear to be any crystal structures available for members of the AGCS family. | Known 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 () and AgcS (), although Acp () 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''.<ref name="Bualuang">{{cite journal|last1 = Bualuang|first1 = A|last2 = Kageyama|first2 = H|last3 = Tanaka|first3 = Y|last4 = Incharoensakdi|first4 = A|last5 = Takabe|first5 = T|title = Functional characterization of a member of alanine or glycine: cation symporter family in halotolerant cyanobacterium Aphanothece halophytica.|date = 2015|volume = 79|issue = 2|pages = 230–5|doi = 10.1080/09168451.2014.968091|pmid = 25421789|journal=Biosci. Biotechnol. Biochem.}}</ref><ref>{{Cite journal|title = Overexpression of the alanine carrier protein gene from thermophilic bacterium PS3 in Escherichia coli|url = http://www.ncbi.nlm.nih.gov/pubmed/10050032|journal = Journal of Biochemistry|date = 1999-03-01|issn = 0021-924X|pmid = 10050032|pages = 454–459|volume = 125|issue = 3|first = M.|last = Kanamori|first2 = H.|last2 = Kamata|first3 = H.|last3 = Yagisawa|first4 = H.|last4 = Hirata|doi=10.1093/oxfordjournals.jbchem.a022308}}</ref> As of 2015, only three members of the family have been functionally characterized. These proteins show limited sequence similarity in the APC family ().<ref name=TCDB/> As of early 2016, there do not appear to be any crystal structures available for members of the AGCS family. | ||
| ===Transport reaction=== | ===Transport reaction=== | ||
| Line 31: | Line 31: | ||
| ==Further reading== | ==Further reading== | ||
| {{refbegin}} | {{refbegin}} | ||
| * {{cite journal|last1=Rodionov|first1=DA|last2=Hebbeln|first2=P|last3=Eudes|first3=A|last4=ter Beek|first4=J|last5=Rodionova|first5=IA|last6=Erkens|first6=GB|last7=Slotboom|first7=DJ|last8=Gelfand|first8=MS|last9=Osterman|first9=AL|last10=Hanson|first10=AD|last11=Eitinger|first11=T|title=A novel class of modular transporters for vitamins in prokaryotes.|journal=Journal of Bacteriology|date=January 2009|volume=191|issue=1|pages=42–51|doi=10.1128/JB.01208-08|pmid=18931129}} | * {{cite journal|last1=Rodionov|first1=DA|last2=Hebbeln|first2=P|last3=Eudes|first3=A|last4=ter Beek|first4=J|last5=Rodionova|first5=IA|last6=Erkens|first6=GB|last7=Slotboom|first7=DJ|last8=Gelfand|first8=MS|last9=Osterman|first9=AL|last10=Hanson|first10=AD|last11=Eitinger|first11=T|title=A novel class of modular transporters for vitamins in prokaryotes.|journal=Journal of Bacteriology|date=January 2009|volume=191|issue=1|pages=42–51|doi=10.1128/JB.01208-08|pmid=18931129|pmc=2612444}} | ||
| * {{cite journal|last1=Kamata|first1=H|last2=Akiyama|first2=S|last3=Morosawa|first3=H|last4=Ohta|first4=T|last5=Hamamoto|first5=T|last6=Kambe|first6=T|last7=Kagawa|first7=Y|last8=Hirata|first8=H|title=Primary structure of the alanine carrier protein of thermophilic bacterium PS3.|journal=Journal of Biological Chemistry|date=October 25, 1992|volume=267|issue=30|pages=21650–5|pmid=1400476}} | * {{cite journal|last1=Kamata|first1=H|last2=Akiyama|first2=S|last3=Morosawa|first3=H|last4=Ohta|first4=T|last5=Hamamoto|first5=T|last6=Kambe|first6=T|last7=Kagawa|first7=Y|last8=Hirata|first8=H|title=Primary structure of the alanine carrier protein of thermophilic bacterium PS3.|journal=Journal of Biological Chemistry|date=October 25, 1992|volume=267|issue=30|pages=21650–5|pmid=1400476}} | ||
| {{refend}} | {{refend}} | ||
Revision as of 10:26, 30 July 2016
Protein family| Alanine/glycine:cation symporter (AGCS) family protein | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | A3P053 | ||||||||
| Pfam | PF01235 | ||||||||
| InterPro | IPR001463 | ||||||||
| PROSITE | PS00873 | ||||||||
| |||||||||
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.
Structure and function
Known 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. 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). As of early 2016, there do not appear to be any crystal structures available for members of the AGCS family.
Transport reaction
The generalized transport reaction catalyzed by the AGCS family is:
alanine or glycine (out) + Na or H (out) → alanine or glycine (in) + Na or H (in).
Proteins in the AGCS family
There are currently 10 proteins belonging to the AGCS family. These proteins and their descriptions can be found in the Transporter Classification Database.
Further reading
- Rodionov, DA; Hebbeln, P; Eudes, A; ter Beek, J; Rodionova, IA; Erkens, GB; Slotboom, DJ; Gelfand, MS; Osterman, AL; Hanson, AD; Eitinger, T (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; Kagawa, Y; Hirata, H (October 25, 1992). "Primary structure of the alanine carrier protein of thermophilic bacterium PS3". Journal of Biological Chemistry. 267 (30): 21650–5. PMID 1400476.
References
- 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". Biosci. Biotechnol. Biochem. 79 (2): 230–5. doi:10.1080/09168451.2014.968091. PMID 25421789.
- Kanamori, M.; Kamata, H.; Yagisawa, H.; Hirata, H. (1999-03-01). "Overexpression of the alanine carrier protein gene from thermophilic bacterium PS3 in Escherichia coli". Journal of Biochemistry. 125 (3): 454–459. doi:10.1093/oxfordjournals.jbchem.a022308. ISSN 0021-924X. PMID 10050032.
- ^ Saier, MH Jr. "2.A.25 The Alanine or Glycine:Cation Symporter (AGCS) Family". Transporter Classification Database. Saier Lab Bioinformatics Group / SDSC.
As of this edit, this article uses content from "2.A.25 The Alanine or Glycine:Cation Symporter (AGCS) Family", which is licensed in a way that permits reuse under the Creative Commons Attribution-ShareAlike 3.0 Unported License, but not under the GFDL. All relevant terms must be followed.
 | This membrane protein–related article is a stub. You can help Misplaced Pages by expanding it. |