MG_372_MONOMER – thiamine biosynthesis/tRNA modification protein ThiI

Name
WID MG_372_MONOMER View in model
Name thiamine biosynthesis/tRNA modification protein ThiI View in model
 
Genetics
Gene MG_372 View in model
 
Structure
Sequence
1
51
101
151
201
251
301
351
MELNSEDVLVARYGELVLKGKNRSYFTKQLKINIKKAFKKLEINNSIVYE
FDRIVVFDIKKEQRAILQELFSFLPGISLFFFASQIVREENKLLDLLFNL
FKDFNSFKLEVKRRDKNFAENSSNFKKYLAVKLFEKYQLKGVINNPEIIA
NIEILKEHFLVFTERFKGKGGLPVYSSGKALVLLSGGIDSPVAASLVMQR
GFNIDFITFINEPNKNQKTIEKITRLANLISFNKTICSGKLLVFDFTAIQ
KELIHISNESYRIVLMRRVFYKAASMFKYDCLVTGEVLGQVASQTIENLK
VIQSATPDTFIVRPLIGFSKDKIIELAKFFNTFDISIEQHLDTCSEFSPK
NPTTKAKLINVEKLESELIFLNDLIEKGVSELSND*
50
100
150
200
250
300
350
386
View in model
Is N‑terminal methionine cleaved
No
View in model
Prosthetic groups View in model
Empirical formula (pH 7.5) H3238C2033N513O569S7
Molecular weight (pH 7.5; Da) 44194.88 View in model
Extinction coefficient 
(260 nm, 25C, pH 7.0)
13785
Instability index 35.87
Is stable True
Aliphatic index 105.28
GRAVY (25C, pH 7.0) -0.0363
Half life (OD (600 nm) = 0.3, 
M9 media, 36C; min)
1200 View in model
 
Synthesis
Localization c View in model
 
Function
Complex subunit thiamine biosynthesis/tRNA modification protein ThiI
[c]: (2) MG_372_MONOMERMG_372_DIMER
View in model
 
Comments
Comments Functional Macromolecule Functional as homodimer [PUB_0325]. Coenzymes Monomer interacts with MG with unknown stoichiometry as prosthetic group.
References
  1. Andjelković N, Zolnierowicz S, Van Hoof C, Goris J, Hemmings BA. The catalytic subunit of protein phosphatase 2A associates with the translation termination factor eRF1. EMBO J 15, 7156-67 (1996). WholeCell: PUB_0325, PubMed: 9003791

 
Metadata
Created 2012-10-01 15:08:00
Last updated 2012-10-01 15:14:46