B1XB85 (TPIS_ECODH) 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
Ordered Locus Names:	ECDH10B_4108

Organism

Escherichia coli (strain K12 / DH10B) [Complete proteome] [HAMAP]

Taxonomic identifier

316385 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli › Escherichia coli (strain K12)

Protein attributes

Sequence length	255 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	D-glyceraldehyde 3-phosphate = glycerone phosphate. HAMAP-Rule MF_00147
Pathway	Carbohydrate biosynthesis; gluconeogenesis. HAMAP-Rule MF_00147 Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. HAMAP-Rule MF_00147
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
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 Complete proteome
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 – 255

255

Triosephosphate isomerase HAMAP-Rule MF_00147

PRO_1000096495

Sites

Active site

95

1

Electrophile By similarity

Active site

167

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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255

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Helix

16 – 30

15

Beta strand

35 – 41

7

Helix

44 – 46

3

Helix

47 – 54

8

Beta strand

57 – 64

8

Beta strand

70 – 73

4

Helix

80 – 86

7

Beta strand

88 – 94

7

Helix

96 – 101

6

Helix

106 – 118

13

Beta strand

122 – 127

6

Helix

131 – 135

5

Helix

139 – 154

16

Helix

156 – 159

4

Beta strand

163 – 166

4

Helix

169 – 171

3

Beta strand

172 – 175

4

Helix

180 – 195

16

Helix

199 – 204

6

Beta strand

206 – 209

4

Turn

215 – 217

3

Helix

218 – 222

5

Beta strand

229 – 233

5

Helix

234 – 237

4

Helix

239 – 253

15

Sequences

	Sequence		Length	Mass (Da)
	B1XB85 [UniParc]. Last modified May 20, 2008. Version 1. Checksum: E398251020012D94	FASTA	255	26,972
	10 20 30 40 50 60 MRHPLVMGNW KLNGSRHMVH ELVSNLRKEL AGVAGCAVAI APPEMYIDMA KREAEGSHIM 70 80 90 100 110 120 LGAQNVDLNL SGAFTGETSA AMLKDIGAQY IIIGHSERRT YHKESDELIA KKFAVLKEQG 130 140 150 160 170 180 LTPVLCIGET EAENEAGKTE EVCARQIDAV LKTQGAAAFE GAVIAYEPVW AIGTGKSATP 190 200 210 220 230 240 AQAQAVHKFI RDHIAKVDAN IAEQVIIQYG GSVNASNAAE LFAQPDIDGA LVGGASLKAD 250 AFAVIVKAAE AAKQA

References

[1]

"The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse." Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B., Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B., Posfai G., Weinstock G.M., Blattner F.R. J. Bacteriol. 190:2597-2606(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / DH10B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

CP000948 Genomic DNA. Translation: ACB04931.1.

RefSeq

YP_001732709.1. NC_010473.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4IOT	X-ray	1.85	A/B	1-255	[»]

ProteinModelPortal

B1XB85.

SMR

B1XB85. Positions 1-255.

ModBase

Search...

Protein-protein interaction databases

STRING

316385.ECDH10B_4108.

Proteomic databases

PRIDE

B1XB85.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

ACB04931; ACB04931; ECDH10B_4108.

GeneID

6061229.

KEGG

ecd:ECDH10B_4108.

PATRIC

18468207. VBIEscCol59506_4140.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG0149.

HOGENOM

HOG000226413.

KO

K01803.

OMA

QEVCGAI.

ProtClustDB

PRK00042.

Enzyme and pathway databases

BioCyc

ECOL316385:GJ8B-3929-MONOMER.

UniPathway

UPA00109; UER00189.
UPA00138.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

HAMAP

MF_00147_B. TIM_B.

InterPro

IPR013785. Aldolase_TIM.
IPR022896. TrioseP_Isoase_bac/euk.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]

PANTHER

PTHR21139. PTHR21139. 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_ECODH

Accession

Primary (citable) accession number: B1XB85

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	May 20, 2008
Last modified:	May 1, 2013
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program