DP00430: Triosephosphate isomeraseFASTA viewXML view

General information
DisProt:DP00430
Name:Triosephosphate isomerase
Synonym(s):TPIS_YEAST
TIM
EC 5.3.1.1
Triose-phosphate isomerase
First appeared in release:Release 3.0 (02/17/2006)
UniProt:P00942
UniGene: 
SwissProt: TPIS_YEAST
TrEMBL:  
NCBI (GI): 136069
Source organism:Saccharomyces cerevisiae (Baker's yeast)
Sequence length:248
Percent disordered:4%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MARTFFVGGN FKLNGSKQSI KEIVERLNTA SIPENVEVVI CPPATYLDYS VSLVKKPQVT - 60
VGAQNAYLKA SGAFTGENSV DQIKDVGAKW VILGHSERRS YFHEDDKFIA DKTKFALGQG - 120
VGVILCIGET LEEKKAGKTL DVVERQLNAV LEEVKDWTNV VVAYEPVWAI GTGLAATPED - 180
AQDIHASIRK FLASKLGDKA ASELRILYGG SANGSNAVTF KDKADVDGFL VGGASLKPEF - 240
VDIINSRN



Functional narrative    

Involved in carbohydrate biosynthesis.

Region 1: 166-176

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name: 
Location:166 - 176
Length:11
Region sequence:

PVWAIGTGLAA

Modification type:  
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Substrate/ligand binding
Detection methods:
  1. X-ray crystallography

References:
  1. Brown FK, Kollman PA. "Molecular dynamics simulations of "loop closing" in the enzyme triose phosphate isomerase." J Mol Biol. 1987; 198(3): 533-46. PubMed: 3430618

  2. Joseph D, Petsko GA, Karplus M. "Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop." Science. 1990; 249(4975): 1425-8. PubMed: 2402636

Comments:
 



References

  1. Lolis E, Alber T, Davenport RC, Rose D, Hartman FC, Petsko GA. "Structure of yeast triosephosphate isomerase at 1.9-A resolution." Biochemistry. 1990; 29(28): 6609-18. PubMed: 2204417


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