|Gene:||ulaG||Accession Numbers: G7855 (MetaCyc), b4192, ECK4188|
Species: Escherichia coli K-12 substr. MG1655
UlaG is required for the ability to utilize L-ascorbate as the sole carbon source under anaerobic growth conditions. The enzyme was suggested to be a cytoplasmic L-ascorbate 6-phosphate lactonase [Zhang03e], and its catalytic activity has recently been shown [Garces10]. Phosphodiesterase activity of UlaG was discovered in a high-throughput screen of purified proteins [Kuznetsova05].
Crystal structures of the UlaG apoenzyme and the Mn2+-bound holoenzyme have been solved at 2.6 Å resolution [Garces08, Garces10]. Phylogenetic analysis of the UlaG-like protein family indicates that it has a common evolutionary origin with RNA processing and metabolizing metallo-β-lactamases [Fernandez11].
Expression of ulaG is negatively regulated by UlaR [Campos02].
|Map Position: [4,416,584 <- 4,417,648]|
Molecular Weight of Polypeptide: 40.061 kD (from nucleotide sequence)
Molecular Weight of Multimer: 256.0 kD (experimental) [Garces08]
Unification Links: ASAP:ABE-0013717 , DIP:DIP-12596N , EchoBASE:EB2385 , EcoGene:EG12492 , EcoliWiki:b4192 , ModBase:P39300 , OU-Microarray:b4192 , PortEco:ulaG , Pride:P39300 , Protein Model Portal:P39300 , RefSeq:NP_418613 , RegulonDB:G7855 , SMR:P39300 , String:511145.b4192 , UniProt:P39300
|Biological Process:||GO:0019854 - L-ascorbic acid catabolic process [UniProtGOA12, GOA06, GOA01a, Zhang03e]|
|Molecular Function:||GO:0030145 - manganese ion binding
GO:0035460 - L-ascorbate 6-phosphate lactonase activity [GOA01a, Garces10]
GO:0016787 - hydrolase activity [UniProtGOA11a]
GO:0052689 - carboxylic ester hydrolase activity [GOA06]
|Cellular Component:||GO:0005737 - cytoplasm
[UniProtGOA11, UniProtGOA11a, GOA06]
GO:0005829 - cytosol
|MultiFun Terms:||metabolism → carbon utilization|
Enzymatic reaction of: L-ascorbate 6-phosphate lactonase
EC Number: 3.1.1.-
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
The reaction is physiologically favored in the direction shown.
In Pathways: L-ascorbate degradation I (bacterial, anaerobic)
Co2+ can substitute for Mn2+ [Garces10].
Peter D. Karp on Wed Jan 18, 2006:
Gene right-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06 ].
Peter D. Karp on Thu Jan 16, 2003:
Predicted gene function revised as a result of E. coli genome reannotation by Serres et al. [Serres01 ].
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.
Campos02: Campos E, Aguilar J, Baldoma L, Badia J (2002). "The gene yjfQ encodes the repressor of the yjfR-X regulon (ula), which is involved in L-ascorbate metabolism in Escherichia coli." J Bacteriol 184(21);6065-8. PMID: 12374842
Fernandez11: Fernandez FJ, Garces F, Lopez-Estepa M, Aguilar J, Baldoma L, Coll M, Badia J, Vega MC (2011). "The UlaG protein family defines novel structural and functional motifs grafted on an ancient RNase fold." BMC Evol Biol 11;273. PMID: 21943130
Garces08: Garces F, Fernandez FJ, Perez-Luque R, Aguilar J, Baldoma L, Coll M, Badia J, Vega MC (2008). "Overproduction, crystallization and preliminary X-ray analysis of the putative L-ascorbate-6-phosphate lactonase UlaG from Escherichia coli." Acta Crystallogr Sect F Struct Biol Cryst Commun 64(Pt 1);36-8. PMID: 18097099
Garces10: Garces F, Fernandez FJ, Montella C, Penya-Soler E, Prohens R, Aguilar J, Baldoma L, Coll M, Badia J, Vega MC (2010). "Molecular architecture of the Mn2+-dependent lactonase UlaG reveals an RNase-like metallo-beta-lactamase fold and a novel quaternary structure." J Mol Biol 398(5);715-29. PMID: 20359483
Kuznetsova05: Kuznetsova E, Proudfoot M, Sanders SA, Reinking J, Savchenko A, Arrowsmith CH, Edwards AM, Yakunin AF (2005). "Enzyme genomics: Application of general enzymatic screens to discover new enzymes." FEMS Microbiol Rev 29(2);263-79. PMID: 15808744
Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293
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