talB

Functionⁱ

Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.1 Publication

Catalytic activityⁱ

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.1 Publication

Activity regulationⁱ

Inhibited by Tris-HCl and phosphate buffer. Also competitively inhibited by sugars with L configuration at C2, such as D-arabinose-5-phosphate and L-glyceraldehyde.1 Publication

Kineticsⁱ

K_M=
38 µM for D,L-glyceraldehyde 3-phosphate (with C3 acceptor compounds at pH 8.5 and 30 degrees Celsius)
1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "Transaldolase B of Escherichia coli K-12: cloning of its gene, talB, and characterization of the enzyme from recombinant strains."
  Sprenger G.A., Schorken U., Sprenger G., Sahm H.
  J. Bacteriol. 177:5930-5936(1995) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT.
K_M=
90 µM for D-erythrose-4-phosphate (with C3 acceptor compounds at pH 8.5 and 30 degrees Celsius)
1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "Transaldolase B of Escherichia coli K-12: cloning of its gene, talB, and characterization of the enzyme from recombinant strains."
  Sprenger G.A., Schorken U., Sprenger G., Sahm H.
  J. Bacteriol. 177:5930-5936(1995) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT.
K_M=
31 mM for D-ribose-5-phosphate (with C3 acceptor compounds at pH 8.5 and 30 degrees Celsius)
1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "Transaldolase B of Escherichia coli K-12: cloning of its gene, talB, and characterization of the enzyme from recombinant strains."
  Sprenger G.A., Schorken U., Sprenger G., Sahm H.
  J. Bacteriol. 177:5930-5936(1995) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT.
K_M=
28 mM for D-glyceraldehyde (with C3 acceptor compounds at pH 8.5 and 30 degrees Celsius)
1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "Transaldolase B of Escherichia coli K-12: cloning of its gene, talB, and characterization of the enzyme from recombinant strains."
  Sprenger G.A., Schorken U., Sprenger G., Sahm H.
  J. Bacteriol. 177:5930-5936(1995) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT.
K_M=
285 µM for D-sedoheptulose-7-phosphate (with C3 donor compounds at pH 8.5 and 30 degrees Celsius)
1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "Transaldolase B of Escherichia coli K-12: cloning of its gene, talB, and characterization of the enzyme from recombinant strains."
  Sprenger G.A., Schorken U., Sprenger G., Sahm H.
  J. Bacteriol. 177:5930-5936(1995) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT.
K_M=
1200 µM for D-fructose-6-phosphate (with C3 donor compounds at pH 8.5 and 30 degrees Celsius)
1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "Transaldolase B of Escherichia coli K-12: cloning of its gene, talB, and characterization of the enzyme from recombinant strains."
  Sprenger G.A., Schorken U., Sprenger G., Sahm H.
  J. Bacteriol. 177:5930-5936(1995) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT.

pH dependenceⁱ

Optimum pH is between 8.5 and 9.5.1 Publication

Temperature dependenceⁱ

Optimum temperature is between 15 and 40 degrees Celsius. At temperatures above 50 degrees Celsius, activity is lost rapidly, and at 55 degrees Celsius, the enzyme is totally inactivated.1 Publication

Pathwayⁱ: pentose phosphate pathway

This protein is involved in step 2 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage).
Proteins known to be involved in the 3 steps of the subpathway in this organism are:

no protein annotated in this organism
Transaldolase A (talA), Transaldolase B (talB)
no protein annotated in this organism

This subpathway is part of the pathway pentose phosphate pathway, 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 and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage), the pathway pentose phosphate pathway and in Carbohydrate degradation.

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Active siteⁱ	132	Schiff-base intermediate with substrate1 Publication		1

GO - Molecular functionⁱ

sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 7592346
transferase activity, transferring aldehyde or ketonic groups
Source: EcoCyc
Inferred from direct assayⁱ
- 9883893

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

carbohydrate metabolic process Source: InterPro
pentose-phosphate shunt, non-oxidative branch
Source: EcoCyc
Inferred from direct assayⁱ
- 11298760

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Transferase
Biological process	Pentose shunt
Ligand	Schiff base

Enzyme and pathway databases

BioCycⁱ	EcoCyc:TRANSALDOLB-MONOMER MetaCyc:TRANSALDOLB-MONOMER
BRENDAⁱ	2.2.1.2 2026
UniPathwayⁱ	UPA00115;UER00414

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Transaldolase B (EC:2.2.1.2)
Gene namesⁱ	Name:talB Synonyms:yaaK Ordered Locus Names:b0008, JW0007
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG11556 talB

EcoGeneⁱ

EG11556 talB

Subcellular locationⁱ

Cytoplasm Curated

GO - Cellular componentⁱ

cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- 15911532
- 18304323
intracellular
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
membrane
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- 16858726

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cytoplasm

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed3 Publications
ChainⁱPRO_0000173593	2 – 317	Transaldolase BAdd BLAST		316

Proteomic databases

EPDⁱ	P0A870
PaxDbⁱ	P0A870
PRIDEⁱ	P0A870

2D gel databases

SWISS-2DPAGEⁱ	P0A870

SWISS-2DPAGEⁱ

P0A870

Interactionⁱ

Subunit structureⁱ

Homodimer.2 Publications

Protein-protein interaction databases

BioGridⁱ	4261939, 9 interactors
Database of interacting proteins More...DIPⁱ	DIP-31850N
IntActⁱ	P0A870, 9 interactors
STRINGⁱ	316385.ECDH10B_0008

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	4 – 8	Combined sources	5
Turnⁱ	9 – 11	Combined sources	3
Beta strandⁱ	12 – 19	Combined sources	8
Helixⁱ	21 – 27	Combined sources	7
Beta strandⁱ	30 – 33	Combined sources	4
Helixⁱ	36 – 42	Combined sources	7
Helixⁱ	46 – 48	Combined sources	3
Helixⁱ	49 – 62	Combined sources	14
Helixⁱ	66 – 86	Combined sources	21
Beta strandⁱ	93 – 96	Combined sources	4
Helixⁱ	99 – 101	Combined sources	3
Helixⁱ	105 – 121	Combined sources	17
Helixⁱ	126 – 128	Combined sources	3
Beta strandⁱ	129 – 134	Combined sources	6
Helixⁱ	137 – 148	Combined sources	12
Beta strandⁱ	153 – 158	Combined sources	6
Helixⁱ	161 – 169	Combined sources	9
Beta strandⁱ	173 – 179	Combined sources	7
Helixⁱ	180 – 189	Combined sources	10
Helixⁱ	197 – 199	Combined sources	3
Helixⁱ	201 – 215	Combined sources	15
Beta strandⁱ	221 – 225	Combined sources	5
Helixⁱ	230 – 234	Combined sources	5
Turnⁱ	235 – 238	Combined sources	4
Beta strandⁱ	239 – 244	Combined sources	6
Helixⁱ	246 – 253	Combined sources	8
Beta strandⁱ	255 – 257	Combined sources	3
Helixⁱ	278 – 286	Combined sources	9
Helixⁱ	289 – 314	Combined sources	26

Show more details

3D structure databases

ProteinModelPortalⁱ	P0A870
SMRⁱ	P0A870
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P0A870

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the transaldolase family. Type 1 subfamily.Curated

Phylogenomic databases

eggNOGⁱ	ENOG4105CW3 Bacteria COG0176 LUCA
HOGENOMⁱ	HOG000281234
InParanoidⁱ	P0A870
KEGG Orthology (KO) More...KOⁱ	K00616
PhylomeDBⁱ	P0A870

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00957 Transaldolase_TalAB, 1 hit
Gene3Dⁱ	3.20.20.70, 1 hit
HAMAPⁱ	MF_00492 Transaldolase_1, 1 hit
InterProⁱ	View protein in InterPro IPR013785 Aldolase_TIM IPR001585 TAL/FSA IPR004730 Transaldolase_1 IPR018225 Transaldolase_AS
PANTHERⁱ	PTHR10683 PTHR10683, 1 hit PTHR10683:SF20 PTHR10683:SF20, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00923 TAL_FSA, 1 hit
TIGRFAMsⁱ	TIGR00874 talAB, 1 hit
PROSITEⁱ	View protein in PROSITE PS01054 TRANSALDOLASE_1, 1 hit PS00958 TRANSALDOLASE_2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P0A870-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MTDKLTSLRQ YTTVVADTGD IAAMKLYQPQ DATTNPSLIL NAAQIPEYRK 
        60         70         80         90        100
LIDDAVAWAK QQSNDRAQQI VDATDKLAVN IGLEILKLVP GRISTEVDAR 
       110        120        130        140        150
LSYDTEASIA KAKRLIKLYN DAGISNDRIL IKLASTWQGI RAAEQLEKEG 
       160        170        180        190        200
INCNLTLLFS FAQARACAEA GVFLISPFVG RILDWYKANT DKKEYAPAED 
       210        220        230        240        250
PGVVSVSEIY QYYKEHGYET VVMGASFRNI GEILELAGCD RLTIAPALLK 
       260        270        280        290        300
ELAESEGAIE RKLSYTGEVK ARPARITESE FLWQHNQDPM AVDKLAEGIR 
       310 
KFAIDQEKLE KMIGDLL

Length:317

Mass (Da):35,219

Last modified:January 23, 2007 - v2

Checksum:ⁱ2DF03D741E576C31

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	D13161 Genomic DNA Translation: BAA21822.1 S80045 Genomic DNA Translation: AAB47022.1 U00096 Genomic DNA Translation: AAC73119.1 AP009048 Genomic DNA Translation: BAB96586.1
PIRⁱ	S40535
NCBI Reference Sequences More...RefSeqⁱ	NP_414549.1, NC_000913.3 WP_000130185.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73119; AAC73119; b0008 BAB96586; BAB96586; BAB96586
GeneIDⁱ	944748
KEGGⁱ	ecj:JW0007 eco:b0008
PATRICⁱ	fig\|1411691.4.peg.2275

Protein	Similar proteins		Species	Score	Length	Source
P0A870	Transaldolase 1		SHISS		317	UniRef100_Q3Z606
Transaldolase B		ECO57		317
Transaldolase B		SHIFL		317
Transaldolase B		ECOLX		294
Transaldolase		Shigella dysenteriae 1012		371
+67

Protein	Similar proteins		Species	Score	Length	Source
P0A870	Transaldolase	)	ECO1E		317	UniRef90_K0BE10
Transaldolase		SHIBS		317
Transaldolase 1		SHISS		317
Transaldolase B		ECO57		317
Transaldolase B		SHIFL		317
+336

Protein	Similar proteins		Species	Score	Length	Source
P0A870	Transaldolase	)	ECO1E		317	UniRef50_K0BE10
Transaldolase		SHIBS		317
Transaldolase B		ECOL6		317
Transaldolase		SHIDS		317
Transaldolase 2		PECAS		317
+402

Cross-referencesⁱ

Web resourcesⁱ

Wikipedia

Transaldolase B entry

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	D13161 Genomic DNA Translation: BAA21822.1 S80045 Genomic DNA Translation: AAB47022.1 U00096 Genomic DNA Translation: AAC73119.1 AP009048 Genomic DNA Translation: BAB96586.1
PIRⁱ	S40535
RefSeqⁱ	NP_414549.1, NC_000913.3 WP_000130185.1, NZ_LN832404.1

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
	1I2N	X-ray	2.05	A/B	2-317	[»]
	1I2O	X-ray	2.05	A/B	2-317	[»]
	1I2P	X-ray	2.05	A/B	2-317	[»]
	1I2Q	X-ray	2.05	A/B	2-317	[»]
	1I2R	X-ray	2.10	A/B	2-317	[»]
	1ONR	X-ray	1.87	A/B	2-317	[»]
	1UCW	X-ray	2.20	A/B	1-317	[»]
	3KOF	X-ray	1.90	A/B	1-317	[»]
	4RZ5	X-ray	1.80	A/B	1-317	[»]
	4RZ6	X-ray	1.80	A/B	1-317	[»]
	4S2B	X-ray	1.46	A/B	1-317	[»]
	4S2C	X-ray	2.20	A/B	1-317	[»]
ProteinModelPortalⁱ	P0A870
SMRⁱ	P0A870
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4261939, 9 interactors
DIPⁱ	DIP-31850N
IntActⁱ	P0A870, 9 interactors
STRINGⁱ	316385.ECDH10B_0008

2D gel databases

SWISS-2DPAGEⁱ	P0A870

SWISS-2DPAGEⁱ

P0A870

Proteomic databases

EPDⁱ	P0A870
PaxDbⁱ	P0A870
PRIDEⁱ	P0A870

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC73119; AAC73119; b0008 BAB96586; BAB96586; BAB96586
GeneIDⁱ	944748
KEGGⁱ	ecj:JW0007 eco:b0008
PATRICⁱ	fig\|1411691.4.peg.2275

Organism-specific databases

EchoBASEⁱ	EB1517
EcoGeneⁱ	EG11556 talB

Phylogenomic databases

eggNOGⁱ	ENOG4105CW3 Bacteria COG0176 LUCA
HOGENOMⁱ	HOG000281234
InParanoidⁱ	P0A870
KOⁱ	K00616
PhylomeDBⁱ	P0A870

Enzyme and pathway databases

UniPathwayⁱ	UPA00115;UER00414
BioCycⁱ	EcoCyc:TRANSALDOLB-MONOMER MetaCyc:TRANSALDOLB-MONOMER
BRENDAⁱ	2.2.1.2 2026

Miscellaneous databases

EvolutionaryTraceⁱ	P0A870
Protein Ontology More...PROⁱ	PR:P0A870

Family and domain databases

CDDⁱ	cd00957 Transaldolase_TalAB, 1 hit
Gene3Dⁱ	3.20.20.70, 1 hit
HAMAPⁱ	MF_00492 Transaldolase_1, 1 hit
InterProⁱ	View protein in InterPro IPR013785 Aldolase_TIM IPR001585 TAL/FSA IPR004730 Transaldolase_1 IPR018225 Transaldolase_AS
PANTHERⁱ	PTHR10683 PTHR10683, 1 hit PTHR10683:SF20 PTHR10683:SF20, 1 hit
Pfamⁱ	View protein in Pfam PF00923 TAL_FSA, 1 hit
TIGRFAMsⁱ	TIGR00874 talAB, 1 hit
PROSITEⁱ	View protein in PROSITE PS01054 TRANSALDOLASE_1, 1 hit PS00958 TRANSALDOLASE_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	TALB_ECOLI
Accessionⁱ	P0A870Primary (citable) accession number: P0A870 Secondary accession number(s): P30148
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
	Last sequence update:	January 23, 2007
	Last modified:	November 7, 2018
	This is version 126 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0A870 (TALB_ECOLI)

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Transaldolase B

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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

pH dependencei

Temperature dependencei

<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: pentose phosphate pathway

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

Organism-specific databases

<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

GO - Cellular componenti

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

2D gel 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

Protein-protein interaction 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

Phylogenomic databases

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic 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

Documents

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Functionⁱ

Kineticsⁱ

pH dependenceⁱ

Temperature dependenceⁱ

Pathwayⁱ: pentose phosphate pathway

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ