[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1006/jmbi.1993.1010; PubMed=8421318 [NCBI, ExPASy, EBI, Israel, Japan] Rentier-Delrue F., Mande S.C., Moyens S., Terpstra P., Mainfroid V., Goraj K., Lion M., Hol W.G.J., Martial J.A.; "Cloning and overexpression of the triosephosphate isomerase genes from psychrophilic and thermophilic bacteria. Structural comparison of the predicted protein sequences."; J. Mol. Biol. 229:85-93(1993).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0378-1119(93)90188-9; PubMed=8244026 [NCBI, ExPASy, EBI, Israel, Japan] Rentier-Delrue F., Moyens S., Lion M., Martial J.A.; "Sequence of the triosephosphate isomerase-encoding gene isolated from the thermophile Bacillus stearothermophilus."; Gene 134:137-138(1993).
[3]	PRELIMINARY PROTEIN SEQUENCE. PubMed=6105959 [NCBI, ExPASy, EBI, Israel, Japan] Artavanis-Tsakonas S., Harris J.I.; "Primary structure of triosephosphate isomerase from Bacillus stearothermophilus."; Eur. J. Biochem. 108:599-611(1980).
[4]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, AND SUBUNIT. PubMed=8580851 [NCBI, ExPASy, EBI, Israel, Japan] Delboni L.F., Mande S.C., Rentier-Delrue F., Mainfroid V., Turley S., Vellieux F.M.D., Martial J.A., Hol W.G.J.; "Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions."; Protein Sci. 4:2594-2604(1995).
[5]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, AND SUBUNIT. DOI=10.1074/jbc.274.27.19181; PubMed=10383424 [NCBI, ExPASy, EBI, Israel, Japan] Alvarez M., Wouters J., Maes D., Mainfroid V., Rentier-Delrue F., Wyns L., Depiereux E., Martial J.A.; "Lys13 plays a crucial role in the functional adaptation of the thermophilic triose-phosphate isomerase from Bacillus stearothermophilus to high temperatures."; J. Biol. Chem. 274:19181-19187(1999).

Comments

CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate = glycerone phosphate.
PATHWAY: Carbohydrate biosynthesis; gluconeogenesis .
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1 .
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm (Probable).
SIMILARITY: Belongs to the triosephosphate isomerase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X66129; CAA46920.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JT0768; ISBSTF.

3D structure databases

PDB

1BTM; X-ray; 2.80 A; A/B=2-253.	[ExPASy / RCSB / EBI]
2BTM; X-ray; 2.40 A; A/B=2-253.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1BTM; -.
2BTM; -.

ModBase

P00943.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004807;	Molecular function: triose-phosphate isomerase activity (inferred from electronic annotation from HAMAP).
GO:0006094;	Biological process: gluconeogenesis (inferred from electronic annotation from HAMAP).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from HAMAP).
GO:0006098;	Biological process: pentose-phosphate shunt (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00147; -; 1.
PBIL [Tree]

InterPro

IPR013785; Aldolase_TIM.
IPR000652; Triophos_ismrse.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

PANTHER

PTHR21139; Triophos_ismrse; 1.

Pfam

PF00121; TIM; 1.
Pfam graphical view of domain structure.

ProDom

PD001005; Triophos_ismrse; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGR00419; tim; 1.

PS00171; TIM; 1.

Other

P00943; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cytoplasm; Direct protein sequencing; Gluconeogenesis; Glycolysis; Isomerase; Pentose shunt; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 253`	`253`	`Triosephosphate isomerase.`	`PRO_0000090178`
`ACT_SITE`	`95 95`		`Electrophile.`
`ACT_SITE`	`167 167`		`Proton acceptor.`
`BINDING`	`9 9`		`Substrate.`
`BINDING`	`11 11`		`Substrate.`
`MOD_RES`	`213 213`		`Phosphoserine (By similarity).`
`CONFLICT`	`37 37`		`I -> D (in Ref. 3; AA sequence).`
`CONFLICT`	`41 41`		`Missing (in Ref. 3; AA sequence).`
`CONFLICT`	`47 48`		`Missing (in Ref. 3; AA sequence).`
`CONFLICT`	`59 59`		`L -> LQ (in Ref. 3; AA sequence).`
`CONFLICT`	`100 100`		`Q -> H (in Ref. 3; AA sequence).`
`CONFLICT`	`135 135`		`E -> Q (in Ref. 3; AA sequence).`
`CONFLICT`	`138 140`		`QTN -> ETD (in Ref. 3; AA sequence).`
`CONFLICT`	`144 144`		`Missing (in Ref. 3; AA sequence).`
`CONFLICT`	`157 158`		`EQ -> QE (in Ref. 3; AA sequence).`
`CONFLICT`	`161 164`		`QAVI -> IIL (in Ref. 3; AA sequence).`
`CONFLICT`	`169 169`		`I -> L (in Ref. 3; AA sequence).`
`CONFLICT`	`231 231`		`P -> A (in Ref. 3; AA sequence).`
`CONFLICT`	`248 248`		`E -> Q (in Ref. 3; AA sequence).`
`STRAND`	`5 9`	`5`
`HELIX`	`16 26`	`11`
`TURN`	`27 29`	`3`
`TURN`	`33 35`	`3`
`STRAND`	`37 42`	`6`
`HELIX`	`44 46`	`3`
`HELIX`	`47 54`	`8`
`STRAND`	`57 64`	`8`
`STRAND`	`68 73`	`6`
`HELIX`	`80 86`	`7`
`STRAND`	`90 94`	`5`
`HELIX`	`96 101`	`6`
`HELIX`	`106 118`	`13`
`STRAND`	`122 127`	`6`
`HELIX`	`131 135`	`5`
`HELIX`	`139 151`	`13`
`HELIX`	`156 159`	`4`
`STRAND`	`163 166`	`4`
`HELIX`	`169 171`	`3`
`TURN`	`172 174`	`3`
`HELIX`	`180 198`	`19`
`HELIX`	`200 203`	`4`
`STRAND`	`206 213`	`8`
`TURN`	`216 218`	`3`
`HELIX`	`219 223`	`5`
`STRAND`	`230 234`	`5`
`HELIX`	`235 237`	`3`
`HELIX`	`240 248`	`9`

Sequence information

Length: 253 AA [This is the length of the unprocessed precursor]

Molecular weight: 27206 Da [This is the MW of the unprocessed precursor]

CRC64: 6532B5235362946C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRKPIIAGNW KMHKTLAEAV QFVEDVKGHV PPADEVISVV CAPFLFLDRL VQAADGTDLK 

        70         80         90        100        110        120 
IGAQTMHFAD QGAYTGEVSP VMLKDLGVTY VILGHSERRQ MFAETDETVN KKVLAAFTRG 

       130        140        150        160        170        180 
LIPIICCGES LEEREAGQTN AVVASQVEKA LAGLTPEQVK QAVIAYEPIW AIGTGKSSTP 

       190        200        210        220        230        240 
EDANSVCGHI RSVVSRLFGP EAAEAIRIQY GGSVKPDNIR DFLAQQQIDG PLVGGASLEP 

       250 
ASFLQLVEAG RHE

P00943 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools