MG_270_MONOMER – lipoyltransferase/lipoate-protein ligase, putative

Name
WID MG_270_MONOMER View in model
Name lipoyltransferase/lipoate-protein ligase, putative View in model
Cross references PDB: 1X2H
 
Genetics
Gene MG_270 View in model
 
Structure
Sequence
1
51
101
151
201
251
301
MQTFIITSPVFNPYFNAALEEWLLTEFRKNELVKVIYFWQNANTIVVGRN
QNTYAEVNLKELESDKVNLFRRFSGGGAVFHDLGNICFSIILPRTGKVME
NAYEQTTRNVVKFLNSLNVPAVFHGRNDLEINNKKFSGLAEYIAKDRLLV
HGTLLFDTDFSKLAKYLNVDKTKIASKGVDSVAKRVVNVKEYLPNWTTAK
FLEEMINFFTVTEKAETIVLTKDALAKVEKRAKEHFQSWEWNFGKTYEYN
FKNKRYFNNAGLFECNVQVEKGTVVDIKFYGDFLSVVDITPVTKKLIGQK
YDYKTFEKLFNELDHFSDYFGSLKPEQLLGVIFDNK*
50
100
150
200
250
300
337
View in model
Is N‑terminal methionine cleaved
No
View in model
Prosthetic groups View in model
Empirical formula (pH 7.5) H2751C1796N455O505S5
Molecular weight (pH 7.5; Da) 38957.02 View in model
Extinction coefficient 
(260 nm, 25C, pH 7.0)
48610
Instability index 21.24
Is stable True
Aliphatic index 86.41
GRAVY (25C, pH 7.0) -0.277
Half life (OD (600 nm) = 0.3, 
M9 media, 36C; min)
1200 View in model
 
Synthesis
Localization c View in model
 
Function
Enzyme View in model
 
Comments
Comments Functional Macromolecule Functional as monomer [PUB_0156]. Coenzymes Monomer interacts with MG with unknown stoichiometry as prosthetic group [95].
References
  1. Kim DJ, Kim KH, Lee HH, Lee SJ, Ha JY, Yoon HJ, Suh SW. Crystal structure of lipoate-protein ligase A bound with the activated intermediate: insights into interaction with lipoyl domains. J Biol Chem 280, 38081-9 (2005). WholeCell: PUB_0156, PubMed: 16141198

 
Metadata
Created 2012-10-01 15:07:55
Last updated 2012-10-01 15:14:38