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UniProtKB - P04789 (TPIS_TRYBB)

>sp|P04789|TPIS_TRYBB Triosephosphate isomerase, glycosomal OS=Trypanosoma brucei brucei OX=5702 PE=1 SV=2
MSKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVVASTFVHLAMTKERLSHPKF
VIAAQNAIAKSGAFTGEVSLPILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASG
FMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAKVVIAYEPVWAIGTGKVATP
QQAQEAHALIRSWVSSKIGADVAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKP
EFVDIIKATQ

Entry version 147 (02 Jun 2021)
Sequence version 2 (01 Feb 1995)
Previous versions | rss

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Protein

Triosephosphate isomerase, glycosomal

Gene

N/A

Organism

Trypanosoma brucei brucei

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Miscellaneous

The enzyme contains a high proportion of positively-charged residues in beta-barrels V and VII (compared to the homologous regions in other triose isomerase sequences). Since 2 clusters of positive charges located at precise distances on the molecular surface are common to 4 glycosomal enzymes, it has been speculated that this might represent a signal for entry into glycosomes (PubMed:3015595).1 Publication

Catalytic activityⁱ

D-glyceraldehyde 3-phosphate
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
dihydroxyacetone phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
EC:
5.3.1.1
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
D-glyceraldehyde 3-phosphate
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=
dihydroxyacetone phosphate
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Pathwayⁱ: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

Pathwayⁱ: glycolysis

This protein is involved in step 1 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate from glycerone phosphate. This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate from glycerone phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	11	Substrate	1
Binding siteⁱ	13	Substrate	1
Active siteⁱ	95	Electrophile	1
Active siteⁱ	167	Proton acceptor	1

GO - Molecular functionⁱ

triose-phosphate isomerase activity
Source: GeneDB
Inferred from mutant phenotypeⁱ
- "Functional role of the conserved active site proline of triosephosphate isomerase."
  Casteleijn M.G., Alahuhta M., Groebel K., El-Sayed I., Augustyns K., Lambeir A.M., Neubauer P., Wierenga R.K.
  Biochemistry 45:15483-15494(2006) [PubMed] [Europe PMC] [Abstract]

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Isomerase
Biological process	Gluconeogenesis, Glycolysis

Enzyme and pathway databases

BRENDAⁱ	5.3.1.1, 6519
SABIO-RKⁱ	P04789
UniPathwayⁱ	UPA00109;UER00189 UPA00138

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Triosephosphate isomerase, glycosomal (EC:5.3.1.1) Short name: TIM Short name: Triose-phosphate isomerase
Organismⁱ	Trypanosoma brucei brucei
Taxonomic identifierⁱ	5702 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Discoba › Euglenozoa › Kinetoplastea › Metakinetoplastina › Trypanosomatida › Trypanosomatidae › Trypanosoma › Trypanozoon › Trypanosoma brucei

Keywords - Cellular componentⁱ

Glycosome, Peroxisome

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000090142	1 – 250	Triosephosphate isomerase, glycosomalAdd BLAST		250

Proteomic databases

PRIDEⁱ	P04789

PRIDEⁱ

P04789

Interactionⁱ

Subunit structureⁱ

Homodimer.

3 Publications

Chemistry databases

BindingDBⁱ	P04789

BindingDBⁱ

P04789

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	7 – 11	Combined sources	5
Beta strandⁱ	14 – 16	Combined sources	3
Helixⁱ	18 – 29	Combined sources	12
Beta strandⁱ	38 – 42	Combined sources	5
Helixⁱ	45 – 47	Combined sources	3
Helixⁱ	48 – 54	Combined sources	7
Beta strandⁱ	60 – 65	Combined sources	6
Beta strandⁱ	68 – 70	Combined sources	3
Helixⁱ	74 – 79	Combined sources	6
Helixⁱ	80 – 85	Combined sources	6
Beta strandⁱ	90 – 94	Combined sources	5
Helixⁱ	96 – 101	Combined sources	6
Helixⁱ	106 – 119	Combined sources	14
Beta strandⁱ	122 – 127	Combined sources	6
Helixⁱ	131 – 135	Combined sources	5
Helixⁱ	139 – 152	Combined sources	14
Helixⁱ	156 – 161	Combined sources	6
Beta strandⁱ	162 – 167	Combined sources	6
Helixⁱ	169 – 171	Combined sources	3
Beta strandⁱ	172 – 175	Combined sources	4
Helixⁱ	180 – 197	Combined sources	18
Helixⁱ	200 – 205	Combined sources	6
Beta strandⁱ	208 – 213	Combined sources	6
Turnⁱ	216 – 218	Combined sources	3
Helixⁱ	219 – 223	Combined sources	5
Beta strandⁱ	224 – 227	Combined sources	4
Beta strandⁱ	230 – 234	Combined sources	5
Helixⁱ	235 – 238	Combined sources	4
Helixⁱ	242 – 247	Combined sources	6

Show more details

3D structure databases

SMRⁱ	P04789
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P04789

EvolutionaryTraceⁱ

P04789

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the triosephosphate isomerase family.Curated

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00311, TIM, 1 hit
Gene3Dⁱ	3.20.20.70, 1 hit
HAMAPⁱ	MF_00147_B, TIM_B, 1 hit
InterProⁱ	View protein in InterPro IPR013785, Aldolase_TIM IPR035990, TIM_sf IPR022896, TrioseP_Isoase_bac/euk IPR000652, Triosephosphate_isomerase IPR020861, Triosephosphate_isomerase_AS
PANTHERⁱ	PTHR21139, PTHR21139, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00121, TIM, 1 hit
SUPFAMⁱ	SSF51351, SSF51351, 1 hit
TIGRFAMsⁱ	TIGR00419, tim, 1 hit
PROSITEⁱ	View protein in PROSITE PS00171, TIM_1, 1 hit PS51440, TIM_2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P04789-1 [UniParc]FASTA Add to basket

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        10         20         30         40         50
MSKPQPIAAA NWKCNGSQQS LSELIDLFNS TSINHDVQCV VASTFVHLAM 
        60         70         80         90        100
TKERLSHPKF VIAAQNAIAK SGAFTGEVSL PILKDFGVNW IVLGHSERRA 
       110        120        130        140        150
YYGETNEIVA DKVAAAVASG FMVIACIGET LQERESGRTA VVVLTQIAAI 
       160        170        180        190        200
AKKLKKADWA KVVIAYEPVW AIGTGKVATP QQAQEAHALI RSWVSSKIGA 
       210        220        230        240        250
DVAGELRILY GGSVNGKNAR TLYQQRDVNG FLVGGASLKP EFVDIIKATQ

Length:250

Mass (Da):26,835

Last modified:February 1, 1995 - v2

Checksum:ⁱ189D7A00632040FE

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X03921 Genomic DNA Translation: CAA27559.1

Select the link destinations:
EMBLⁱ
GenBankⁱ
DDBJⁱ

Links Updated

X03921 Genomic DNA Translation: CAA27559.1

Genome annotation databases

GeneDBⁱ	Tb927.11.5520:pep

GeneDBⁱ

Tb927.11.5520:pep

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P04789	Triosephosphate isomerase (Fragment)		Trypanosoma brucei		160	UniRef100_P04789

Protein	Similar proteins		Species	Score	Length	Source
P04789	Triosephosphate isomerase (Fragment)		Trypanosoma brucei		160	UniRef90_P04789
Triosephosphate isomerase		TRYCI		251
Triosephosphate isomerase		TRYB2		250
Triosephosphate isomerase		TRYB9		250
Triosephosphate isomerase		TRYEQ		250
+10

Protein	Similar proteins		Species	Score	Length	Source
P04789	Triosephosphate isomerase, glycosomal	)	TRYCR		251	UniRef50_P04789
Triosephosphate isomerase	)	LEIME		251
Triosephosphate isomerase (Fragment)		Trypanosoma brucei		160
Triosephosphate isomerase		TRYCI		251
Triosephosphate isomerase		Trypanosoma brucei equiperdum		250
+108

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X03921 Genomic DNA Translation: CAA27559.1

Select the link destinations:
EMBLⁱ
GenBankⁱ
DDBJⁱ

Links Updated

X03921 Genomic DNA Translation: CAA27559.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1AG1	X-ray	2.36	O/T	1-250	[»]
	1DKW	X-ray	2.65	A/B	2-250	[»]
	1IIG	X-ray	2.60	A/B	1-250	[»]
	1IIH	X-ray	2.20	A/B	1-250	[»]
	1KV5	X-ray	1.65	A/B	1-250	[»]
	1ML1	X-ray	2.60	A/C/E/G/I/K	1-250	[»]
	1MSS	X-ray	2.40	A/B	1-250	[»]
	1MTM	model	-	A	1-250	[»]
	1TPD	X-ray	2.10	A/B	1-250	[»]
	1TPE	X-ray	2.10	A	1-250	[»]
	1TPF	X-ray	1.80	A/B	1-250	[»]
	1TRD	X-ray	2.50	A/B	1-250	[»]
	1TRI	X-ray	2.40	A	1-250	[»]
	1TSI	X-ray	2.84	A/B	1-250	[»]
	1TTI	X-ray	2.40	A	1-250	[»]
	1TTJ	X-ray	2.40	A	1-250	[»]
	2J24	X-ray	2.10	A/B	1-250	[»]
	2J27	X-ray	1.15	A/B	1-250	[»]
	2V0T	X-ray	2.20	A/B/C/D/E/F/G/H	1-250	[»]
	2V2C	X-ray	1.89	A	1-250	[»]
	2V2D	X-ray	2.30	A	1-250	[»]
	2V2H	X-ray	1.18	A/B/C	1-250	[»]
	2V5L	X-ray	2.40	A/B	1-250	[»]
	2VEI	X-ray	1.89	A/B/C	2-250	[»]
	2VEK	X-ray	1.60	A/B	2-250	[»]
	2VEL	X-ray	2.30	A/B	2-250	[»]
	2VEM	X-ray	2.20	A/B	2-250	[»]
	2VEN	X-ray	2.00	A/B	2-250	[»]
	2WSQ	X-ray	2.10	A/B/C/D	2-67	[»]
				A/B/C/D	84-250	[»]
	2WSR	X-ray	1.65	A	2-67	[»]
				A	84-250	[»]
	2X16	X-ray	2.13	A/B	2-250	[»]
	2X1R	X-ray	1.98	A/B	2-250	[»]
	2X1S	X-ray	1.93	A/B	2-250	[»]
	2X1T	X-ray	1.83	A/B	2-250	[»]
	2X1U	X-ray	1.84	A/B	2-250	[»]
	2X2G	X-ray	1.90	A/B	2-250	[»]
	2Y6Z	X-ray	2.60	A	1-250	[»]
	2Y70	X-ray	2.30	A/B/C/D	1-250	[»]
	3Q37	X-ray	1.65	A/B/C/D	2-35	[»]
				A/B/C/D	92-119	[»]
	3TIM	X-ray	2.80	A/B	1-250	[»]
	4JEQ	X-ray	2.30	A/B/C/D/E/F/G/H/I/J/K/L	1-250	[»]
	4PC8	X-ray	1.55	A	1-250	[»]
	4PCF	X-ray	2.71	A/B/C	1-250	[»]
	4TIM	X-ray	2.40	A/B	1-250	[»]
	5I3F	X-ray	1.72	A/B/C/D	1-250	[»]
	5I3G	X-ray	1.96	A/B/C/D	1-250	[»]
	5I3H	X-ray	2.25	A/B	1-250	[»]
	5I3I	X-ray	2.20	A/B/C/D	1-250	[»]
	5I3J	X-ray	1.80	A/B	1-250	[»]
	5I3K	X-ray	2.21	A/B/C/D	1-250	[»]
	5TIM	X-ray	1.83	A/B	1-250	[»]
	6TIM	X-ray	2.20	A/B	1-250	[»]
SMRⁱ	P04789
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Chemistry databases

BindingDBⁱ	P04789

BindingDBⁱ

P04789

Proteomic databases

PRIDEⁱ	P04789

PRIDEⁱ

P04789

Genome annotation databases

GeneDBⁱ	Tb927.11.5520:pep

GeneDBⁱ

Tb927.11.5520:pep

Enzyme and pathway databases

UniPathwayⁱ	UPA00109;UER00189 UPA00138
BRENDAⁱ	5.3.1.1, 6519
SABIO-RKⁱ	P04789

Miscellaneous databases

EvolutionaryTraceⁱ	P04789

EvolutionaryTraceⁱ

P04789

Family and domain databases

CDDⁱ	cd00311, TIM, 1 hit
Gene3Dⁱ	3.20.20.70, 1 hit
HAMAPⁱ	MF_00147_B, TIM_B, 1 hit
InterProⁱ	View protein in InterPro IPR013785, Aldolase_TIM IPR035990, TIM_sf IPR022896, TrioseP_Isoase_bac/euk IPR000652, Triosephosphate_isomerase IPR020861, Triosephosphate_isomerase_AS
PANTHERⁱ	PTHR21139, PTHR21139, 1 hit
Pfamⁱ	View protein in Pfam PF00121, TIM, 1 hit
SUPFAMⁱ	SSF51351, SSF51351, 1 hit
TIGRFAMsⁱ	TIGR00419, tim, 1 hit
PROSITEⁱ	View protein in PROSITE PS00171, TIM_1, 1 hit PS51440, TIM_2, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	TPIS_TRYBB
Accessionⁱ	P04789Primary (citable) accession number: P04789
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
	Last sequence update:	February 1, 1995
	Last modified:	June 2, 2021
	This is version 147 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P04789 (TPIS_TRYBB)

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Triosephosphate isomerase, glycosomal

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: gluconeogenesis

Pathwayi: glycolysis

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Peroxisome

Peroxisome

Other locations

Keywords - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Chemistry databases

Proteomic databases

Genome annotation databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

Catalytic activityⁱ

Pathwayⁱ: gluconeogenesis

Pathwayⁱ: glycolysis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ