| 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
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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
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| Functional narrative |
Involved in carbohydrate biosynthesis.
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| 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.
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| 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:
- X-ray crystallography
| References:
- 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
- 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:
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| References |
- 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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