eda

Functionⁱ

Involved in the degradation of glucose via the Entner-Doudoroff pathway. Catalyzes the reversible, stereospecific retro-aldol cleavage of 2-Keto-3-deoxy-6-phosphogluconate (KDPG) to pyruvate and D-glyceraldehyde-3-phosphate. In the synthetic direction, it catalyzes the addition of pyruvate to electrophilic aldehydes with si-facial selectivity. It accepts some nucleophiles other than pyruvate, including 2-oxobutanoate, phenylpyruvate, and fluorobutanoate. It has a preference for the S-configuration at C2 of the electrophile.2 Publications

Catalytic activityⁱ

4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate.1 Publication

2-dehydro-3-deoxy-6-phosphate-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate.1 Publication

Kineticsⁱ

Kcat is 80 sec(-1) for KDPG, 0.012 sec(-1) for pyruvate and 0.0004 sec(-1) for 2-oxobutyrate.

Pathwayⁱ: 2-dehydro-3-deoxy-D-gluconate degradation

This protein is involved in step 2 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-3-deoxy-D-gluconate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:

2-dehydro-3-deoxygluconokinase (kdgK)
KHG/KDPG aldolase (eda)

This subpathway is part of the pathway 2-dehydro-3-deoxy-D-gluconate degradation, which is itself part of Carbohydrate acid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-3-deoxy-D-gluconate, the pathway 2-dehydro-3-deoxy-D-gluconate degradation and in Carbohydrate acid metabolism.

Pathwayⁱ: glyoxylate and dicarboxylate metabolism

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

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	45	Proton acceptor	1
Active siteⁱ	49		1
Binding siteⁱ	49	Substrate1 Publication	1
Binding siteⁱ	73	Substrate1 Publication	1
Active siteⁱ	133	Schiff-base intermediate with substrate	1
Binding siteⁱ	133	Substrate (covalent)1 Publication	1
Binding siteⁱ	161	Substrate1 Publication	1
Siteⁱ	161	Plays a major role in determining the stereoselectivity	1
Binding siteⁱ	163	Substrate; via amide nitrogen1 Publication	1
Binding siteⁱ	184	Substrate1 Publication	1

GO - Molecular functionⁱ

(4S)-4-hydroxy-2-oxoglutarate aldolase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 4560498
2-dehydro-3-deoxy-phosphogluconate aldolase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 11094340
4-hydroxy-2-oxoglutarate aldolase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 17981470
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 16858726
- 24561554
oxaloacetate decarboxylase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 4560498
oxo-acid-lyase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 1339418
- 4560498

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

metabolic process Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Lyase, Multifunctional enzyme
Ligand	Schiff base

Enzyme and pathway databases

BioCycⁱ	EcoCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-MONOMER MetaCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-MONOMER
BRENDAⁱ	4.1.2.14 2026 4.1.3.42 2026
UniPathwayⁱ	UPA00227 UPA00856;UER00829

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: KHG/KDPG aldolase Including the following 2 domains: 4-hydroxy-2-oxoglutarate aldolase (EC:4.1.3.16) Alternative name(s): 2-keto-4-hydroxyglutarate aldolase Short name: KHG-aldolase 2-dehydro-3-deoxy-phosphogluconate aldolase (EC:4.1.2.14) Alternative name(s): 2-keto-3-deoxy-6-phosphogluconate aldolase Short name: KDPG-aldolase Phospho-2-dehydro-3-deoxygluconate aldolase Phospho-2-keto-3-deoxygluconate aldolase
Gene namesⁱ	Name:eda Synonyms:hga, kdgA Ordered Locus Names:b1850, JW1839
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	EG10256 eda

EcoGeneⁱ

EG10256 eda

Subcellular locationⁱ

Cytoplasm By similarity

GO - Cellular componentⁱ

cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- 15911532
- 18304323
membrane
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- 16858726

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Disruption phenotypeⁱ

Cells lacking this gene lose KHG aldolase activity.1 Publication

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	45	E → N: 50-fold decrease in catalytic efficiency and 6-fold decrease of binding affinity. 2 Publications	1
Mutagenesisⁱ	133	K → Q: Absence of aldolase activity. Shows a markedly altered substrate specificity relative to the wild-type, with an enhanced activity against pyridine carboxaldehyde, benzaldehyde, and alpha-ketobutyrate; when associated with k-161. 1 Publication	1
Mutagenesisⁱ	161	T → K: Shows activity significantly greater than wild-type. Shows a markedly altered substrate specificity relative to the wild-type, with an enhanced activity against pyridine carboxaldehyde, benzaldehyde, and alpha-ketobutyrate; when associated with Q-133. 2 Publications	1
Mutagenesisⁱ	161	T → V: Little stereoselectivity, accepting KDPG and KDPGal as substrate with roughly equal efficacy. It strongly diminishes the activity against KDPG and slightly increases activity against KDPGal. 2 Publications	1
Mutagenesisⁱ	168	N → S: Shows activity significantly greater than wild-type. 1 Publication	1

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB04272 Citric Acid

DrugBankⁱ

DB04272 Citric Acid

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000201037	1 – 213	KHG/KDPG aldolaseAdd BLAST		213

Proteomic databases

EPDⁱ	P0A955
PaxDbⁱ	P0A955
PRIDEⁱ	P0A955

2D gel databases

SWISS-2DPAGEⁱ	P0A955

SWISS-2DPAGEⁱ

P0A955

Expressionⁱ

Inductionⁱ

Constitutive, three-fold induction occurs for growth on gluconate and two-fold for growth on hexuronic acids.1 Publication

Interactionⁱ

Subunit structureⁱ

Homotrimer.3 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-558114,EBI-558114

With

Entry

#Exp.

IntAct

Notes

itself

3

EBI-558114,EBI-558114

GO - Molecular functionⁱ

identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 16858726
- 24561554

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	4259153, 29 interactors
Database of interacting proteins More...DIPⁱ	DIP-36196N
IntActⁱ	P0A955, 10 interactors
STRINGⁱ	316385.ECDH10B_1991

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	8 – 13	Combined sources	6
Beta strandⁱ	16 – 21	Combined sources	6
Helixⁱ	26 – 28	Combined sources	3
Helixⁱ	29 – 38	Combined sources	10
Beta strandⁱ	43 – 48	Combined sources	6
Helixⁱ	53 – 63	Combined sources	11
Beta strandⁱ	67 – 73	Combined sources	7
Helixⁱ	77 – 86	Combined sources	10
Beta strandⁱ	91 – 95	Combined sources	5
Helixⁱ	98 – 106	Combined sources	9
Beta strandⁱ	107 – 109	Combined sources	3
Beta strandⁱ	111 – 117	Combined sources	7
Helixⁱ	118 – 126	Combined sources	9
Beta strandⁱ	131 – 134	Combined sources	4
Turnⁱ	135 – 141	Combined sources	7
Helixⁱ	142 – 150	Combined sources	9
Beta strandⁱ	157 – 163	Combined sources	7
Turnⁱ	166 – 168	Combined sources	3
Helixⁱ	169 – 173	Combined sources	5
Beta strandⁱ	181 – 183	Combined sources	3
Helixⁱ	184 – 186	Combined sources	3
Helixⁱ	189 – 194	Combined sources	6
Helixⁱ	197 – 210	Combined sources	14

Show more details

3D structure databases

ProteinModelPortalⁱ	P0A955
SMRⁱ	P0A955
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P0A955

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	8 – 9	Substrate binding		2

Sequence similaritiesⁱ

Belongs to the KHG/KDPG aldolase family.Curated

Phylogenomic databases

eggNOGⁱ	ENOG4108UHU Bacteria COG0800 LUCA
HOGENOMⁱ	HOG000233114
InParanoidⁱ	P0A955
KEGG Orthology (KO) More...KOⁱ	K01625
OMAⁱ	NVGCVGG
PhylomeDBⁱ	P0A955

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00452 KDPG_aldolase, 1 hit
Gene3Dⁱ	3.20.20.70, 1 hit
InterProⁱ	View protein in InterPro IPR000887 Aldlse_KDPG_KHG IPR013785 Aldolase_TIM IPR031337 KDPG/KHG_AS_1 IPR031338 KDPG/KHG_AS_2
PANTHERⁱ	PTHR30246 PTHR30246, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01081 Aldolase, 1 hit
TIGRFAMsⁱ	TIGR01182 eda, 1 hit
PROSITEⁱ	View protein in PROSITE PS00159 ALDOLASE_KDPG_KHG_1, 1 hit PS00160 ALDOLASE_KDPG_KHG_2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P0A955-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MKNWKTSAES ILTTGPVVPV IVVKKLEHAV PMAKALVAGG VRVLEVTLRT 
        60         70         80         90        100
ECAVDAIRAI AKEVPEAIVG AGTVLNPQQL AEVTEAGAQF AISPGLTEPL 
       110        120        130        140        150
LKAATEGTIP LIPGISTVSE LMLGMDYGLK EFKFFPAEAN GGVKALQAIA 
       160        170        180        190        200
GPFSQVRFCP TGGISPANYR DYLALKSVLC IGGSWLVPAD ALEAGDYDRI 
       210 
TKLAREAVEG AKL

Length:213

Mass (Da):22,284

Last modified:July 19, 2005 - v1

Checksum:ⁱCC8D51B50480D0B7

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X68871 Genomic DNA Translation: CAA48732.1 M87458 Genomic DNA Translation: AAA23723.1 L20897 Genomic DNA Translation: AAA23862.1 X63694 Genomic DNA Translation: CAA45222.1 U00096 Genomic DNA Translation: AAC74920.1 AP009048 Genomic DNA Translation: BAA15658.1
PIRⁱ	B42986 ADECOG
NCBI Reference Sequences More...RefSeqⁱ	NP_416364.1, NC_000913.3 WP_000800512.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC74920; AAC74920; b1850 BAA15658; BAA15658; BAA15658
GeneIDⁱ	946367
KEGGⁱ	ecj:JW1839 eco:b1850
PATRICⁱ	fig\|1411691.4.peg.399

Protein	Similar proteins		Species	Score	Length	Source
P0A955	KHG/KDPG aldolase		ECO57		213	UniRef100_P0A957
KHG/KDPG aldolase		ECOL6		213
KHG/KDPG aldolase		SHIFL		213
Aldolase domain containing protein		TRITR		213
Multifunctional 2-keto-3-deoxygluconate 6-phosphate aldolase and 2-keto-4-hydroxyglutarate aldolase and oxaloacetate decarboxylase		Escherichia coli NCCP15648		213
+170

Protein	Similar proteins		Species	Score	Length	Source
P0A955	KHG/KDPG aldolase		ECO57		213	UniRef90_P0A957
KHG/KDPG aldolase		ECOL6		213
KHG/KDPG aldolase		SHIFL		213
Aldolase domain containing protein		TRITR		213
Multifunctional 2-keto-3-deoxygluconate 6-phosphate aldolase and 2-keto-4-hydroxyglutarate aldolase and oxaloacetate decarboxylase		Escherichia coli NCCP15648		213
+858

Protein	Similar proteins		Species	Score	Length	Source
P0A955	KHG/KDPG aldolase	)	ZYMMO		208	UniRef50_Q00384
KHG/KDPG aldolase		ECO57		213
KHG/KDPG aldolase		ECOL6		213
KHG/KDPG aldolase		SHIFL		213
2-dehydro-3-deoxyphosphogluconate aldolase/4-hydroxy-2-oxoglutarate aldolase		Zymomonas mobilis subsp. mobilis		208
+2503

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X68871 Genomic DNA Translation: CAA48732.1 M87458 Genomic DNA Translation: AAA23723.1 L20897 Genomic DNA Translation: AAA23862.1 X63694 Genomic DNA Translation: CAA45222.1 U00096 Genomic DNA Translation: AAC74920.1 AP009048 Genomic DNA Translation: BAA15658.1
PIRⁱ	B42986 ADECOG
RefSeqⁱ	NP_416364.1, NC_000913.3 WP_000800512.1, 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
	1EUA	X-ray	1.95	A/B/C	1-213	[»]
	1EUN	X-ray	2.00	A/B/C	1-213	[»]
	1FQ0	X-ray	2.10	A/B/C	1-213	[»]
	1FWR	X-ray	2.70	A/B/C	1-213	[»]
	1WAU	X-ray	2.80	A	1-213	[»]
	1WBH	X-ray	1.55	A/B/C	1-213	[»]
	2C0A	X-ray	1.55	A/B/C	1-213	[»]
ProteinModelPortalⁱ	P0A955
SMRⁱ	P0A955
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4259153, 29 interactors
DIPⁱ	DIP-36196N
IntActⁱ	P0A955, 10 interactors
STRINGⁱ	316385.ECDH10B_1991

Chemistry databases

DrugBankⁱ	DB04272 Citric Acid

DrugBankⁱ

DB04272 Citric Acid

2D gel databases

SWISS-2DPAGEⁱ	P0A955

SWISS-2DPAGEⁱ

P0A955

Proteomic databases

EPDⁱ	P0A955
PaxDbⁱ	P0A955
PRIDEⁱ	P0A955

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC74920; AAC74920; b1850 BAA15658; BAA15658; BAA15658
GeneIDⁱ	946367
KEGGⁱ	ecj:JW1839 eco:b1850
PATRICⁱ	fig\|1411691.4.peg.399

Organism-specific databases

EchoBASEⁱ	EB0252
EcoGeneⁱ	EG10256 eda

Phylogenomic databases

eggNOGⁱ	ENOG4108UHU Bacteria COG0800 LUCA
HOGENOMⁱ	HOG000233114
InParanoidⁱ	P0A955
KOⁱ	K01625
OMAⁱ	NVGCVGG
PhylomeDBⁱ	P0A955

Enzyme and pathway databases

UniPathwayⁱ	UPA00227 UPA00856;UER00829
BioCycⁱ	EcoCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-MONOMER MetaCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-MONOMER
BRENDAⁱ	4.1.2.14 2026 4.1.3.42 2026

Miscellaneous databases

EvolutionaryTraceⁱ	P0A955
Protein Ontology More...PROⁱ	PR:P0A955

Family and domain databases

CDDⁱ	cd00452 KDPG_aldolase, 1 hit
Gene3Dⁱ	3.20.20.70, 1 hit
InterProⁱ	View protein in InterPro IPR000887 Aldlse_KDPG_KHG IPR013785 Aldolase_TIM IPR031337 KDPG/KHG_AS_1 IPR031338 KDPG/KHG_AS_2
PANTHERⁱ	PTHR30246 PTHR30246, 1 hit
Pfamⁱ	View protein in Pfam PF01081 Aldolase, 1 hit
TIGRFAMsⁱ	TIGR01182 eda, 1 hit
PROSITEⁱ	View protein in PROSITE PS00159 ALDOLASE_KDPG_KHG_1, 1 hit PS00160 ALDOLASE_KDPG_KHG_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ALKH_ECOLI
Accessionⁱ	P0A955Primary (citable) accession number: P0A955 Secondary accession number(s): P10177
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
	Last sequence update:	July 19, 2005
	Last modified:	July 18, 2018
	This is version 108 of the entry and version 1 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

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0A955 (ALKH_ECOLI)

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KHG/KDPG aldolase

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

<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: 2-dehydro-3-deoxy-D-gluconate degradation

Pathwayi: glyoxylate and dicarboxylate metabolism

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 provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Chemistry databases

<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 expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<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

GO - Molecular functioni

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

Region

<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

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry 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

Pathwayⁱ: 2-dehydro-3-deoxy-D-gluconate degradation

Pathwayⁱ: glyoxylate and dicarboxylate metabolism

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ