MG_245_MONOMER – 5-formyltetrahydrofolate cyclo-ligase, putative

Name
WID MG_245_MONOMER View in model
Name 5-formyltetrahydrofolate cyclo-ligase, putative View in model
 
Genetics
Gene MG_245 View in model
 
Structure
Sequence
1
51
101
151
MVDKNSLRKLMLLKRAELNDLEKSHLDQKINQKLMAFLITRPTIKNLALY
IPIKNEVAFLDNFLDFLKLNKITSCFPSIVDQFNMKFIDQNNNEINPNDI
DCFFIPLLAFNKANHRIGFGKGYYDRYLSLTSKKQLKIGIAYDFQYAEFT
NDPWDYQLDLIICNG*
50
100
150
166
View in model
Is N‑terminal methionine cleaved
No
View in model
Prosthetic groups View in model
Empirical formula (pH 7.5) H1379C888N225O246S7
Molecular weight (pH 7.5; Da) 19367.21 View in model
Extinction coefficient 
(260 nm, 25C, pH 7.0)
16305
Instability index 12.56
Is stable True
Aliphatic index 99.34
GRAVY (25C, pH 7.0) -0.227
Half life (OD (600 nm) = 0.3, 
M9 media, 36C; min)
1200 View in model
 
Synthesis
Localization c View in model
 
Function
Enzyme methylenetetrahydrofolate cyclohydrase
[c]: ATP + FTHF10 + (3) HADP + METTHF + PI
View in model
 
Comments
Comments Functional Macromolecule Functional as monomer [PUB_0353]. Crystal structure indicates could transiently form dimer [PUB_0354]. Has been suggested to form dimers in solution [PUB_0354]. Coenzymes Monomer interacts with MG with unknown stoichiometry as prosthetic group.
References
  1. Meier C, Carter LG, Winter G, Owens RJ, Stuart DI, Esnouf RM. Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489). Acta Crystallogr Sect F Struct Biol Cryst Commun 63, 168-72 (2007). WholeCell: PUB_0354, PubMed: 17329806

  2. Roje S, Janave MT, Ziemak MJ, Hanson AD. Cloning and characterization of mitochondrial 5-formyltetrahydrofolate cycloligase from higher plants. J Biol Chem 277, 42748-54 (2002). WholeCell: PUB_0353, PubMed: 12207015

 
Metadata
Created 2012-10-01 15:07:54
Last updated 2012-10-01 15:14:37