Reviewed, UniProtKB/Swiss-Prot P00943 (TPIS_BACST)

Names and origin

Protein names

Recommended name:
    Triosephosphate isomerase
      Short name=TIM
    EC=5.3.1.1
Alternative name(s):
    Triose-phosphate isomerase

Gene names

Name:	tpiA
Synonyms:	tpi

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	253 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	D-glyceraldehyde 3-phosphate = glycerone phosphate. HAMAP MF_00147
Pathway	Carbohydrate biosynthesis; gluconeogenesis. HAMAP MF_00147 Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. HAMAP MF_00147
Subunit structure	Homodimer. Ref.4 Ref.5
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the triosephosphate isomerase family.

Ontologies

Keywords
Biological process	Gluconeogenesis Glycolysis Pentose shunt
Cellular component	Cytoplasm
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	gluconeogenesis Inferred from electronic annotation. Source: HAMAP glycolysis Inferred from electronic annotation. Source: HAMAP pentose-phosphate shunt Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	triose-phosphate isomerase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 253

253

Triosephosphate isomerase HAMAP MF_00147

PRO_0000090178

Sites

Active site

95

1

Electrophile HAMAP MF_00147

Active site

167

1

Proton acceptor HAMAP MF_00147

Binding site

9

1

Substrate HAMAP MF_00147

Binding site

11

1

Substrate HAMAP MF_00147

Amino acid modifications

Modified residue

213

1

Phosphoserine By similarity

Experimental info

Sequence conflict

37

1

I → D AA sequence Ref.3

Sequence conflict

41

1

Missing AA sequence Ref.3

Sequence conflict

47 – 48

2

Missing AA sequence Ref.3

Sequence conflict

59

1

L → LQ AA sequence Ref.3

Sequence conflict

100

1

Q → H AA sequence Ref.3

Sequence conflict

135

1

E → Q AA sequence Ref.3

Sequence conflict

138 – 140

3

QTN → ETD AA sequence Ref.3

Sequence conflict

144

1

Missing AA sequence Ref.3

Sequence conflict

157 – 158

2

EQ → QE AA sequence Ref.3

Sequence conflict

161 – 164

4

QAVI → IIL AA sequence Ref.3

Sequence conflict

169

1

I → L AA sequence Ref.3

Sequence conflict

231

1

P → A AA sequence Ref.3

Sequence conflict

248

1

E → Q AA sequence Ref.3

Secondary structure

1

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253

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Helix

16 – 26

11

Turn

27 – 29

3

Turn

33 – 35

3

Beta strand

37 – 42

6

Helix

44 – 46

3

Helix

47 – 54

8

Beta strand

57 – 64

8

Beta strand

68 – 73

6

Helix

80 – 86

7

Beta strand

90 – 94

5

Helix

96 – 101

6

Helix

106 – 118

13

Beta strand

122 – 127

6

Helix

131 – 135

5

Helix

139 – 151

13

Helix

156 – 159

4

Beta strand

163 – 166

4

Helix

169 – 171

3

Turn

172 – 174

3

Helix

180 – 198

19

Helix

200 – 203

4

Beta strand

206 – 213

8

Turn

216 – 218

3

Helix

219 – 223

5

Beta strand

230 – 234

5

Helix

235 – 237

3

Helix

240 – 248

9

Sequences

	Sequence		Length	Mass (Da)
	P00943-1 [UniParc]. Last modified December 1, 1992. Version 2. Checksum: 6532B5235362946C	FASTA	253	27,206
	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

References

[1]	"Cloning and overexpression of the triosephosphate isomerase genes from psychrophilic and thermophilic bacteria. Structural comparison of the predicted protein sequences." Rentier-Delrue F., Mande S.C., Moyens S., Terpstra P., Mainfroid V., Goraj K., Lion M., Hol W.G.J., Martial J.A. J. Mol. Biol. 229:85-93(1993) [PubMed: 8421318] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence of the triosephosphate isomerase-encoding gene isolated from the thermophile Bacillus stearothermophilus." Rentier-Delrue F., Moyens S., Lion M., Martial J.A. Gene 134:137-138(1993) [PubMed: 8244026] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Primary structure of triosephosphate isomerase from Bacillus stearothermophilus." Artavanis-Tsakonas S., Harris J.I. Eur. J. Biochem. 108:599-611(1980) [PubMed: 6105959] [Abstract] Cited for: PRELIMINARY PROTEIN SEQUENCE.
[4]	"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." Delboni L.F., Mande S.C., Rentier-Delrue F., Mainfroid V., Turley S., Vellieux F.M.D., Martial J.A., Hol W.G.J. Protein Sci. 4:2594-2604(1995) [PubMed: 8580851] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT.
[5]	"Lys13 plays a crucial role in the functional adaptation of the thermophilic triose-phosphate isomerase from Bacillus stearothermophilus to high temperatures." Alvarez M., Wouters J., Maes D., Mainfroid V., Rentier-Delrue F., Wyns L., Depiereux E., Martial J.A. J. Biol. Chem. 274:19181-19187(1999) [PubMed: 10383424] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X66129 Genomic DNA. Translation: CAA46920.1.

PIR

ISBSTF. JT0768.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BTM	X-ray	2.80	A/B	2-253	[»]
2BTM	X-ray	2.40	A/B	2-253	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

5.3.1.1. 266715.

Family and domain databases

HAMAP

MF_00147.
[Tree]

InterPro

IPR013785. Aldolase_TIM.
IPR000652. Triosephosphate_isomerase.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

PANTHER

PTHR21139. Triophos_ismrse. 1 hit.

Pfam

PF00121. TIM. 1 hit.
[Graphical view]

ProDom

PD001005. Triophos_ismrse. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00419. tim. 1 hit.

PROSITE

PS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

TPIS_BACST

Accession

Primary (citable) accession number: P00943

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	December 1, 1992
Last modified:	June 16, 2009
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)