Reviewed, UniProtKB/Swiss-Prot P00940 (TPIS_CHICK)

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)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › 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	Fatty acid biosynthesis Gluconeogenesis Glycolysis Lipid synthesis Pentose shunt
Molecular function	Isomerase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW 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
Molecular function	triose-phosphate isomerase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

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

Mutagenesis

165

1

E → D: Reduces activity 300-fold

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

Turn

167 – 169

3

Helix

178 – 195

18

Helix

198 – 203

6

Beta strand

206 – 208

3

Turn

214 – 216

3

Helix

217 – 221

5

Beta strand

228 – 231

4

Helix

233 – 236

4

Helix

240 – 244

5

Turn

245 – 247

3

Sequences

	Sequence		Length	Mass (Da)
	P00940-1 [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: 3885220] [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: 3837846] [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: 4463937] [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: 1134550] [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: 2361134] [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: 985462] [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: 1569570] [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: 8130195] [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

EMBLGenBankDDBJ

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

PIR

ISCHT. A23448.

RefSeq

NP_990782.1.

UniGene

Gga.4148

3D structure databases

PDBMSD

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

ModBase

Search...

Genome annotation databases

Ensembl

ENSGALG00000014526. Gallus gallus. [Contig view]

GeneID

396435.

KEGG

gga:396435.

Phylogenomic databases

HOGENOM

P00940.

HOVERGEN

P00940.

Family and domain databases

InterPro

IPR013785. Aldolase_TIM.
IPR000652. Triophos_ismrse.
[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 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

P00940.

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:	November 25, 2008
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)