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Extremophile Protein Database
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Protein Information

 

Protein Details

ExProtDB ID
A.0000H0.05.H08
Name
FERREDOXIN
Extreme Stable Behaviour
Halostable

Source Organism

ExProtDB ID
A.0000H0.05
Name
Halobacterium salinarum
Domain
Archaea
Extremophile Type
Halophile

Protein Function

Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.

Protein Classification

EC ID
E0
EC Number
-
Type
ELECTRON TRANSPORT

Optimum Physiochemical Conditions

Extreme-Stability ID
HA03
Optimum Condition
2.5-5.2M NaCl

Protein Sequence

UniProt KB ID
Molecular Weight (Da)
14418.0
Sequence Length
(amino acid numbers)
129
Sequence
MPTVEYLNYETLDDQGWDMDDDDLFEKAADAGLDGEDYGTMEVAEGEYILEAAEAQGYDWPFSCRAGACANCASIVKEGEIDMDMQQILSDEEVEEKDVRLTCIGSPAADEVKIVYNAKHLDYLQNRVI

Protein Parameters

PID
H.P0017
Amino acid content (%)
 
Ala
10.853
Cys
3.101
Asp
13.178
Glu
12.403
Phe
1.55
Gly
6.977
His
0.775
Ile
5.426
Lys
3.876
Leu
6.977
Met
3.876
Asn
3.101
Pro
2.326
Gln
3.876
Arg
2.326
Ser
3.101
Thr
3.101
Val
6.202
Trp
1.55
Tyr
5.426
Amino acid class contents(%)
 
Tiny (A+C+G+S+T)
27.13
Small (A+C+D+G+N+P+S+T+V)
51.94
Aliphatic (A+I+L+V)
29.46
Aromatic (F+H+W+Y)
9.30
Non Polar (A+C+F+G+I+L+M+P+V+W+Y)
54.26
Polar (D+E+H+K+N+Q+R+S)
45.74
Charged (D+E+H+K+R)
32.56
Basic (H+K+R)
6.98
Acidic (D+E)
25.58
Intraprotein interactions (%)
 
Main Chain Main Chain Hydrogen Bonds
0.92
Main Chain Side Chain Hydrogen Bonds
12.08
Side Chain Side Chain Hydrogen Bonds
10.46
Hydrophonic Interactions
0.94
Ionic Interactions
0.23
Salt Bridges
3.68
Aromatic Aromatic Interactions
0.05
Aromatic Sulphur Interactions
0.01
Cation Pi Interactions
0.02
Disulphide Bridge Interactions
2.02

Protein Structure Details

RCSB PDB ID
Structure Resolution (A)
NA
PMID
Authors
Marg, B., Schweimer, K., Sticht, H., Oesterhelt, D.
Journal
Biochemistry
Title
A Two-Alpha-Helix Extra Domain Mediates the Halophilic Character of a Plant-Type Ferredoxin from Halophilic Archaea.
Volume
44
Year
2005

Information Source

UniProt, RCSB PDB and BRENDA