P00940 (TPIS_CHICK) 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:

TPI1

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	248 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	D-glyceraldehyde 3-phosphate = glycerone phosphate.
Pathway	Carbohydrate biosynthesis; gluconeogenesis. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the triosephosphate isomerase family.

Ontologies

Keywords
Biological process	Gluconeogenesis Glycolysis Pentose shunt
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	embryo development Inferred from electronic annotation. Source: Compara gluconeogenesis Traceable author statement. Source: Reactome glyceraldehyde-3-phosphate metabolic process Inferred from electronic annotation. Source: Compara glycolysis Traceable author statement. Source: Reactome pentose-phosphate shunt Inferred from electronic annotation. Source: UniProtKB-KW small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	triose-phosphate isomerase activity Traceable author statement. Source: Reactome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.3

Chain

2 – 248

247

Triosephosphate isomerase

PRO_0000090121

Sites

Active site

95

1

Electrophile

Active site

165

1

Proton acceptor

Binding site

13

1

Substrate

Experimental info

Mutagenesis

95

1

H → N: Reduces activity 5000-fold. Ref.5

Mutagenesis

165

1

E → D: Reduces activity 300-fold. Ref.5

Sequence conflict

17 – 18

2

DK → KR AA sequence Ref.3

Sequence conflict

29

1

N → D AA sequence Ref.3

Sequence conflict

145 – 146

2

EQ → QE AA sequence Ref.3

Sequence conflict

194

1

S → T AA sequence Ref.3

Sequence conflict

202 – 204

3

QST → VQS AA sequence Ref.3

Secondary structure

1

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248

Helix Strand Turn

Details...

Beta strand

6 – 11

6

Helix

18 – 30

13

Beta strand

37 – 42

6

Helix

45 – 47

3

Helix

48 – 54

7

Beta strand

59 – 64

6

Beta strand

68 – 73

6

Helix

80 – 85

6

Beta strand

90 – 94

5

Helix

96 – 100

5

Helix

106 – 118

13

Beta strand

122 – 127

6

Helix

131 – 135

5

Helix

139 – 151

13

Helix

157 – 159

3

Beta strand

160 – 164

5

Helix

167 – 169

3

Beta strand

170 – 173

4

Helix

178 – 195

18

Helix

198 – 203

6

Beta strand

206 – 211

6

Turn

214 – 216

3

Helix

217 – 221

5

Beta strand

228 – 232

5

Helix

233 – 236

4

Helix

240 – 244

5

Turn

245 – 247

3

Sequences

	Sequence		Length	Mass (Da)
	P00940 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: AFCC258E574DE982	FASTA	248	26,620
	10 20 30 40 50 60 MAPRKFFVGG NWKMNGDKKS LGELIHTLNG AKLSADTEVV CGAPSIYLDF ARQKLDAKIG 70 80 90 100 110 120 VAAQNCYKVP KGAFTGEISP AMIKDIGAAW VILGHSERRH VFGESDELIG QKVAHALAEG 130 140 150 160 170 180 LGVIACIGEK LDEREAGITE KVVFEQTKAI ADNVKDWSKV VLAYEPVWAI GTGKTATPQQ 190 200 210 220 230 240 AQEVHEKLRG WLKSHVSDAV AQSTRIIYGG SVTGGNCKEL ASQHDVDGFL VGGASLKPEF VDIINAKH

References

[1]	"Chicken triosephosphate isomerase complements an Escherichia coli deficiency." Straus D., Gilbert W. Proc. Natl. Acad. Sci. U.S.A. 82:2014-2018(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Genetic engineering in the Precambrian: structure of the chicken triosephosphate isomerase gene." Straus D., Gilbert W. Mol. Cell. Biol. 5:3497-3506(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Studies on the subunit structure and amino acid sequence of trisoe phosphate isomerase from chicken breast muscle." Furth A.J., Milman J.D., Priddle J.D., Offord R.E. Biochem. J. 139:11-22(1974) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-248.
[4]	"Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5-A resolution using amino acid sequence data." Banner D.W., Bloomer A.C., Petsko G.A., Phillips D.C., Pogson C.I., Wilson I.A., Corran P.H., Furth A.J., Milman J.D., Offord R.E., Priddle J.D., Waley S.G. Nature 255:609-614(1975) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SEQUENCE REVISION.
[5]	"How can a catalytic lesion be offset? The energetics of two pseudorevertant triosephosphate isomerases." Blacklow S.C., Knowles J.R. Biochemistry 29:4099-4108(1990) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), MUTAGENESIS OF HIS-95 AND GLU-165.
[6]	"Atomic coordinates for triose phosphate isomerase from chicken muscle." Banner D.W., Bloomer A.C., Petsko G.A., Phillips D.C., Wilson I.A. Biochem. Biophys. Res. Commun. 72:146-155(1976) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[7]	"Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase." Wierenga R.K., Noble M.E.M., Davenport R.C. J. Mol. Biol. 224:1115-1126(1992) [PubMed] [Europe PMC] [Abstract] Cited for: COMPARISON OF X-RAY STRUCTURES.
[8]	"Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-A resolution." Zhang Z., Sugio S., Komives E.A., Liu K.D., Knowles J.R., Petsko G.A., Ringe D. Biochemistry 33:2830-2837(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ASP-165 IN COMPLEX WITH SUBSTRATE ANALOG.
[9]	Artymiuk P.J., Taylor W.R., Phillips D.C. Submitted (AUG-1998) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M11314 mRNA. Translation: AAA49094.1.
M11941 Genomic DNA. Translation: AAA49095.1.

IPI

IPI00582452.

PIR

ISCHT. A23448.

RefSeq

NP_990782.1. NM_205451.1.

UniGene

Gga.4148.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SPQ	X-ray	2.16	A/B	2-247	[»]
1SQ7	X-ray	2.85	A/B	2-247	[»]
1SSD	X-ray	2.90	A/B	2-247	[»]
1SSG	X-ray	2.90	A/B	2-247	[»]
1SU5	X-ray	2.70	A/B	2-247	[»]
1SW0	X-ray	1.71	A/B	1-248	[»]
1SW3	X-ray	2.03	A/B	1-248	[»]
1SW7	X-ray	2.22	A/B	1-248	[»]
1TIM	X-ray	2.50	A/B	2-248	[»]
1TPB	X-ray	1.90	1/2	2-247	[»]
1TPC	X-ray	1.90	1/2	2-247	[»]
1TPH	X-ray	1.80	1/2	2-248	[»]
1TPU	X-ray	1.90	A/B	2-248	[»]
1TPV	X-ray	1.90	A/B	2-248	[»]
1TPW	X-ray	1.90	A/B	2-247	[»]
8TIM	X-ray	2.50	A/B	2-247	[»]

ProteinModelPortal

P00940.

SMR

P00940. Positions 2-248.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00940. 1 interaction.

STRING

9031.ENSGALP00000023396.

Proteomic databases

PaxDb

P00940.

PRIDE

P00940.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSGALT00000023442; ENSGALP00000023396; ENSGALG00000014526.

GeneID

396435.

KEGG

gga:396435.

Organism-specific databases

CTD

7167.

Phylogenomic databases

eggNOG

COG0149.

GeneTree

ENSGT00390000013354.

HOGENOM

HOG000226413.

HOVERGEN

HBG002599.

InParanoid

P00940.

KO

K01803.

OMA

QEVCGAI.

OrthoDB

EOG40S0GF.

Enzyme and pathway databases

Reactome

REACT_115655. Metabolism.

SABIO-RK

P00940.

UniPathway

UPA00109; UER00189.
UPA00138.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

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...

Other

EvolutionaryTrace

P00940.

NextBio

20816476.

Entry information

Entry name

TPIS_CHICK

Accession

Primary (citable) accession number: P00940

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program