Q8NKN9 (TPIS_THETE) Reviewed, UniProtKB/Swiss-Prot

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

Thermoproteus tenax

Taxonomic identifier

2271 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermoproteaceae › Thermoproteus

Protein attributes

Sequence length	226 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	D-glyceraldehyde 3-phosphate = glycerone phosphate. HAMAP MF_00147_A
Pathway	Carbohydrate biosynthesis; gluconeogenesis. HAMAP MF_00147_A Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. HAMAP MF_00147_A
Subunit structure	Homotetramer. Ref.3
Subcellular location	Cytoplasm Probable HAMAP MF_00147_A.
Sequence similarities	Belongs to the triosephosphate isomerase family.

Ontologies

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 226

226

Triosephosphate isomerase HAMAP MF_00147_A

PRO_0000090349

Sites

Active site

93

1

Electrophile By similarity

Active site

141

1

Proton acceptor By similarity

Binding site

9

1

Substrate By similarity

Binding site

11

1

Substrate By similarity

Secondary structure

1

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226

Helix Strand Turn

Details...

Beta strand

3 – 9

7

Helix

14 – 16

3

Helix

19 – 35

17

Beta strand

38 – 42

5

Helix

45 – 47

3

Helix

48 – 52

5

Beta strand

59 – 62

4

Beta strand

65 – 68

4

Helix

78 – 84

7

Beta strand

88 – 91

4

Helix

100 – 112

13

Beta strand

116 – 123

8

Helix

124 – 132

9

Beta strand

136 – 140

5

Helix

143 – 145

3

Turn

146 – 148

3

Helix

152 – 155

4

Helix

157 – 170

14

Beta strand

174 – 181

8

Helix

185 – 193

9

Beta strand

197 – 201

5

Helix

203 – 206

4

Helix

211 – 224

14

Sequences

	Sequence		Length	Mass (Da)
	Q8NKN9 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 53BE6A0A5F492857	FASTA	226	23,283
	10 20 30 40 50 60 MRLPILIINF KAYGEAAGKR AVELAKAAER AARELGVNIV VAPNHLELGL VSQSVDIPVY 70 80 90 100 110 120 AQGADVEAGG AHTAHVSLEN IKEAGGSGVI LNHSEAPLKL NDLARLVAKA KSLGLDVVVC 130 140 150 160 170 180 APDPRTSLAA AALGPHAVAV EPPELIGTGR AVSRYKPEAI VETVGLVSRH FPEVSVITGA 190 200 210 220 GIESGDDVAA ALRLGTRGVL LASAAVKAKD PYAKIVELAK PLSELR

References

[1]	Schramm A. Thesis (1998), Universitaet-GH Essen, Germany Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Kra 1 / DSM 2078.
[2]	"Regulation of the carbohydrate metabolism of the hyperthermophilic crenarchaeote Thermoproteus tenax." Tjaden B. Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Kra 1 / DSM 2078.
[3]	"Structure and function of a regulated archaeal triosephosphate isomerase adapted to high temperature." Walden H., Taylor G.L., Lorentzen E., Pohl E., Lilie H., Schramm A., Knura T., Stubbe K., Tjaden B., Hensel R. J. Mol. Biol. 342:861-875(2004) [PubMed: 15342242] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ012066 Genomic DNA. Translation: CAB66162.1.
AJ515539 Genomic DNA. Translation: CAD56500.1.

RefSeq

YP_004892241.1. NC_016070.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W0M	X-ray	2.50	A/B/C/D/E/F/G/H	1-226	[»]

ProteinModelPortal

Q8NKN9.

SMR

Q8NKN9. Positions 1-225.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

11263496.

Family and domain databases

HAMAP

MF_00147_A. TIM_A.
[Tree]

InterPro

IPR013785. Aldolase_TIM.
IPR000652. Triosephosphate_isomerase.
IPR022891. Triosephosphate_isomerase_arc.
IPR020861. Triosephosphate_isomerase_AS.
[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]

SUPFAM

SSF51351. Triophos_ismrse. 1 hit.

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_THETE

Accession

Primary (citable) accession number: Q8NKN9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2003
Last sequence update:	October 1, 2002
Last modified:	December 14, 2011
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program