galT

Functionⁱ

Miscellaneous

Iron binding is not required for protein folding or enzyme activity.1 Publication

Catalytic activityⁱ

UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose.3 Publications

Cofactorⁱ

Zn²⁺3 PublicationsNote: Binds 1 zinc ion per subunit. Zinc binding seems to play a structural role.3 Publications

Kineticsⁱ

K_M=
0.200 mM for uridine 5'-diphosphate glucose
1 Publication
Manual assertion based on experiment inⁱ
- Ref.9
  "Roles of two conserved amino acid residues in the active site of galactose-1-phosphate uridylyltransferase: an essential serine and a nonessential cysteine."
  Geeganage S., Ling V.W., Frey P.A.
  Biochemistry 39:5397-5404(2000) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, KINETIC PARAMETERS, MUTAGENESIS OF CYS-160 AND SER-161.
K_M=
0.303 mM for galactose-1-phosphate
1 Publication
Manual assertion based on experiment inⁱ
- Ref.9
  "Roles of two conserved amino acid residues in the active site of galactose-1-phosphate uridylyltransferase: an essential serine and a nonessential cysteine."
  Geeganage S., Ling V.W., Frey P.A.
  Biochemistry 39:5397-5404(2000) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, KINETIC PARAMETERS, MUTAGENESIS OF CYS-160 AND SER-161.
K_M=
0.121 mM for uridine 5'-diphosphate galactose
1 Publication
Manual assertion based on experiment inⁱ
- Ref.9
  "Roles of two conserved amino acid residues in the active site of galactose-1-phosphate uridylyltransferase: an essential serine and a nonessential cysteine."
  Geeganage S., Ling V.W., Frey P.A.
  Biochemistry 39:5397-5404(2000) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, KINETIC PARAMETERS, MUTAGENESIS OF CYS-160 AND SER-161.
K_M=
0.157 mM for glucose-1-phosphate
1 Publication
Manual assertion based on experiment inⁱ
- Ref.9
  "Roles of two conserved amino acid residues in the active site of galactose-1-phosphate uridylyltransferase: an essential serine and a nonessential cysteine."
  Geeganage S., Ling V.W., Frey P.A.
  Biochemistry 39:5397-5404(2000) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, KINETIC PARAMETERS, MUTAGENESIS OF CYS-160 AND SER-161.

V_max=
180 µmol/min/mg enzyme
1 Publication
Manual assertion based on experiment inⁱ
- Ref.9
  "Roles of two conserved amino acid residues in the active site of galactose-1-phosphate uridylyltransferase: an essential serine and a nonessential cysteine."
  Geeganage S., Ling V.W., Frey P.A.
  Biochemistry 39:5397-5404(2000) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, KINETIC PARAMETERS, MUTAGENESIS OF CYS-160 AND SER-161.

Pathwayⁱ: galactose metabolism

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

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	52	ZincCombined sources2 Publications	1
Metal bindingⁱ	55	ZincCombined sources2 Publications	1
Binding siteⁱ	61	UDP-alpha-D-glucose; via amide nitrogenCombined sources1 Publication	1
Metal bindingⁱ	115	ZincCombined sources2 Publications	1
Binding siteⁱ	153	UDP-alpha-D-glucoseCombined sources1 Publication	1
Metal bindingⁱ	164	ZincCombined sources2 Publications	1
Active siteⁱ	166	Tele-UMP-histidine intermediatePROSITE-ProRule annotation2 Publications	1
Binding siteⁱ	168	UDP-alpha-D-glucoseCombined sources1 Publication	1
Metal bindingⁱ	182	IronCombined sources2 Publications	1
Metal bindingⁱ	281	IronCombined sources2 Publications	1
Metal bindingⁱ	296	IronCombined sources2 Publications	1
Metal bindingⁱ	298	IronCombined sources2 Publications	1
Binding siteⁱ	323	UDP-alpha-D-glucoseCombined sources1 Publication	1

GO - Molecular functionⁱ

ferrous iron binding
Source: EcoCyc
Inferred from direct assayⁱ
- 7727423
galactokinase activity
Source: CACAO
Inferred from mutant phenotypeⁱ
- 18263746
UDP-glucose:hexose-1-phosphate uridylyltransferase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 5338129
zinc ion binding
Source: EcoCyc
Inferred from direct assayⁱ
- 7727423

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

galactose catabolic process via UDP-galactose
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 16590575

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Nucleotidyltransferase, Transferase
Biological process	Carbohydrate metabolism, Galactose metabolism
Ligand	Iron, Metal-binding, Zinc

Enzyme and pathway databases

BioCycⁱ	EcoCyc:GALACTURIDYLYLTRANS-MONOMER MetaCyc:GALACTURIDYLYLTRANS-MONOMER
BRENDAⁱ	2.7.7.12 2026
SABIO-RKⁱ	P09148
UniPathwayⁱ	UPA00214

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Galactose-1-phosphate uridylyltransferase (EC:2.7.7.123 Publications) Short name: Gal-1-P uridylyltransferase Alternative name(s): UDP-glucose--hexose-1-phosphate uridylyltransferase
Gene namesⁱ	Name:galT Synonyms:galB Ordered Locus Names:b0758, JW0741
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	EG10366 galT

EcoGeneⁱ

EG10366 galT

Subcellular locationⁱ

GO - Cellular componentⁱ

cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- 18304323

View the complete GO annotation on QuickGO ...

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	52	C → S: Decreases enzyme activity 3000-fold. 1 Publication	1
Mutagenesisⁱ	55	C → S: Decreases enzyme activity 600-fold. 1 Publication	1
Mutagenesisⁱ	115	H → N: Decreases enzyme activity by 98%. 1 Publication	1
Mutagenesisⁱ	160	C → S or A: Slight inhibition of enzymatic activity. 1 Publication	1
Mutagenesisⁱ	161	S → A: 7000-fold reduction in specific activity. 1 Publication	1
Mutagenesisⁱ	164	H → N: Decreases enzyme activity 10000-fold. 1 Publication	1
Mutagenesisⁱ	166	H → G: Abolishes enzymatic activity. 1 Publication	1
Mutagenesisⁱ	182	E → A: Decreases enzyme activity by about 50%. Abolishes iron binding, but has no effect on zinc binding. 1 Publication	1

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB01861 Uridine diphosphate glucose DB03435 Uridine-5'-Diphosphate DB03685 Uridine-5'-Monophosphate

DrugBankⁱ

DB01861 Uridine diphosphate glucose
DB03435 Uridine-5'-Diphosphate
DB03685 Uridine-5'-Monophosphate

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000169894	1 – 348	Galactose-1-phosphate uridylyltransferaseAdd BLAST		348

Proteomic databases

PaxDbⁱ	P09148
PRIDEⁱ	P09148

Interactionⁱ

Subunit structureⁱ

Homodimer.

Protein-protein interaction databases

BioGridⁱ	4261703, 397 interactors
Database of interacting proteins More...DIPⁱ	DIP-9735N
IntActⁱ	P09148, 1 interactor
STRINGⁱ	316385.ECDH10B_0826

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	6 – 8	Combined sources	3
Beta strandⁱ	11 – 14	Combined sources	4
Turnⁱ	16 – 18	Combined sources	3
Beta strandⁱ	21 – 24	Combined sources	4
Helixⁱ	28 – 30	Combined sources	3
Beta strandⁱ	73 – 76	Combined sources	4
Beta strandⁱ	95 – 97	Combined sources	3
Beta strandⁱ	99 – 101	Combined sources	3
Beta strandⁱ	104 – 111	Combined sources	8
Helixⁱ	119 – 121	Combined sources	3
Helixⁱ	124 – 144	Combined sources	21
Beta strandⁱ	146 – 155	Combined sources	10
Helixⁱ	156 – 158	Combined sources	3
Beta strandⁱ	164 – 174	Combined sources	11
Helixⁱ	177 – 193	Combined sources	17
Helixⁱ	197 – 208	Combined sources	12
Beta strandⁱ	212 – 215	Combined sources	4
Beta strandⁱ	217 – 222	Combined sources	6
Beta strandⁱ	233 – 239	Combined sources	7
Helixⁱ	244 – 246	Combined sources	3
Helixⁱ	249 – 270	Combined sources	22
Beta strandⁱ	276 – 281	Combined sources	6
Beta strandⁱ	285 – 288	Combined sources	4
Beta strandⁱ	296 – 300	Combined sources	5
Beta strandⁱ	305 – 308	Combined sources	4
Helixⁱ	316 – 319	Combined sources	4
Beta strandⁱ	323 – 326	Combined sources	4
Helixⁱ	328 – 336	Combined sources	9
Helixⁱ	343 – 346	Combined sources	4

Show more details

3D structure databases

ProteinModelPortalⁱ	P09148
SMRⁱ	P09148
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P09148

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	28 – 31	UDP-alpha-D-glucose binding; shared with dimeric partnerCombined sources1 Publication	4
Regionⁱ	77 – 78	UDP-alpha-D-glucose bindingCombined sources1 Publication	2
Regionⁱ	159 – 161	UDP-alpha-D-glucose bindingCombined sources1 Publication	3
Regionⁱ	311 – 312	UDP-alpha-D-glucose binding; shared with dimeric partnerCombined sources1 Publication	2
Regionⁱ	316 – 317	UDP-alpha-D-glucose binding; shared with dimeric partnerCombined sources1 Publication	2

Sequence similaritiesⁱ

Belongs to the galactose-1-phosphate uridylyltransferase type 1 family.Curated

Phylogenomic databases

eggNOGⁱ	ENOG4105F0Z Bacteria COG1085 LUCA
HOGENOMⁱ	HOG000230490
InParanoidⁱ	P09148
KEGG Orthology (KO) More...KOⁱ	K00965
PhylomeDBⁱ	P09148

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00608 GalT, 1 hit
Gene3Dⁱ	3.30.428.10, 2 hits
InterProⁱ	View protein in InterPro IPR001937 GalP_UDPtransf1 IPR019779 GalP_UDPtransf1_His-AS IPR005850 GalP_Utransf_C IPR005849 GalP_Utransf_N IPR036265 HIT-like_sf
PANTHERⁱ	PTHR11943 PTHR11943, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02744 GalP_UDP_tr_C, 1 hit PF01087 GalP_UDP_transf, 1 hit
PIRSFⁱ	PIRSF000808 GalT, 1 hit
SUPFAMⁱ	SSF54197 SSF54197, 2 hits
TIGRFAMsⁱ	TIGR00209 galT_1, 1 hit
PROSITEⁱ	View protein in PROSITE PS00117 GAL_P_UDP_TRANSF_I, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P09148-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MTQFNPVDHP HRRYNPLTGQ WILVSPHRAK RPWQGAQETP AKQVLPAHDP 
        60         70         80         90        100
DCFLCAGNVR VTGDKNPDYT GTYVFTNDFA ALMSDTPDAP ESHDPLMRCQ 
       110        120        130        140        150
SARGTSRVIC FSPDHSKTLP ELSVAALTEI VKTWQEQTAE LGKTYPWVQV 
       160        170        180        190        200
FENKGAAMGC SNPHPHGQIW ANSFLPNEAE REDRLQKEYF AEQKSPMLVD 
       210        220        230        240        250
YVQRELADGS RTVVETEHWL AVVPYWAAWP FETLLLPKAH VLRITDLTDA 
       260        270        280        290        300
QRSDLALALK KLTSRYDNLF QCSFPYSMGW HGAPFNGEEN QHWQLHAHFY 
       310        320        330        340 
PPLLRSATVR KFMVGYEMLA ETQRDLTAEQ AAERLRAVSD IHFRESGV

Length:348

Mass (Da):39,646

Last modified:November 1, 1997 - v2

Checksum:ⁱ3D55D2CB38D8C9A2

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	29 – 31	AKR → LS in CAA29574 (PubMed:3022232).Curated		3

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X06226 Genomic DNA Translation: CAA29574.1 U00096 Genomic DNA Translation: AAC73845.1 AP009048 Genomic DNA Translation: BAA35420.1 X02306 Genomic DNA Translation: CAA26171.1
PIRⁱ	S00722 XNECUD
NCBI Reference Sequences More...RefSeqⁱ	NP_415279.1, NC_000913.3 WP_000191497.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73845; AAC73845; b0758 BAA35420; BAA35420; BAA35420
GeneIDⁱ	945357
KEGGⁱ	ecj:JW0741 eco:b0758
PATRICⁱ	fig\|1411691.4.peg.1520

Protein	Similar proteins		Species	Score	Length	Source
P09148	Galactose-1-phosphate uridylyltransferase		Shigella sp.		348	UniRef100_P09148
Galactose-1-phosphate uridylyltransferase		ECOLX		348
Galactose-1-phosphate uridylyltransferase		Escherichia coli KTE108		348
Galactose-1-phosphate uridylyltransferase		SHIBO		348
Galactose-1-phosphate uridylyltransferase		SHIDY		348
+26

Protein	Similar proteins		Species	Score	Length	Source
P09148	Galactose-1-phosphate uridylyltransferase		Shigella sp.		348	UniRef90_P09148
Galactose-1-phosphate uridylyltransferase		ECOLX		348
Galactose-1-phosphate uridylyltransferase		Escherichia coli KTE108		348
Galactose-1-phosphate uridylyltransferase		SHIBO		348
Galactose-1-phosphate uridylyltransferase		SHIDY		348
+1069

Protein	Similar proteins		Species	Score	Length	Source
P09148	Probable galactose-1-phosphate uridylyltransferase		DROME		350	UniRef50_P09148
Galactose-1-phosphate uridylyltransferase		HAEIN		349
Galactose-1-phosphate uridylyltransferase		RAT		379
Probable galactose-1-phosphate uridylyltransferase		CAEEL		352
Galactose-1-phosphate uridylyltransferase		Shigella sp.		348
+4589

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X06226 Genomic DNA Translation: CAA29574.1 U00096 Genomic DNA Translation: AAC73845.1 AP009048 Genomic DNA Translation: BAA35420.1 X02306 Genomic DNA Translation: CAA26171.1
PIRⁱ	S00722 XNECUD
RefSeqⁱ	NP_415279.1, NC_000913.3 WP_000191497.1, 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
	1GUP	X-ray	1.80	A/B/C/D	1-348	[»]
	1GUQ	X-ray	1.80	A/B/C/D	1-348	[»]
	1HXP	X-ray	1.80	A/B	1-348	[»]
	1HXQ	X-ray	1.86	A/B	1-348	[»]
ProteinModelPortalⁱ	P09148
SMRⁱ	P09148
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4261703, 397 interactors
DIPⁱ	DIP-9735N
IntActⁱ	P09148, 1 interactor
STRINGⁱ	316385.ECDH10B_0826

Chemistry databases

DrugBankⁱ	DB01861 Uridine diphosphate glucose DB03435 Uridine-5'-Diphosphate DB03685 Uridine-5'-Monophosphate

DrugBankⁱ

DB01861 Uridine diphosphate glucose
DB03435 Uridine-5'-Diphosphate
DB03685 Uridine-5'-Monophosphate

Proteomic databases

PaxDbⁱ	P09148
PRIDEⁱ	P09148

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC73845; AAC73845; b0758 BAA35420; BAA35420; BAA35420
GeneIDⁱ	945357
KEGGⁱ	ecj:JW0741 eco:b0758
PATRICⁱ	fig\|1411691.4.peg.1520

Organism-specific databases

EchoBASEⁱ	EB0361
EcoGeneⁱ	EG10366 galT

Phylogenomic databases

eggNOGⁱ	ENOG4105F0Z Bacteria COG1085 LUCA
HOGENOMⁱ	HOG000230490
InParanoidⁱ	P09148
KOⁱ	K00965
PhylomeDBⁱ	P09148

Enzyme and pathway databases

UniPathwayⁱ	UPA00214
BioCycⁱ	EcoCyc:GALACTURIDYLYLTRANS-MONOMER MetaCyc:GALACTURIDYLYLTRANS-MONOMER
BRENDAⁱ	2.7.7.12 2026
SABIO-RKⁱ	P09148

Miscellaneous databases

EvolutionaryTraceⁱ	P09148
Protein Ontology More...PROⁱ	PR:P09148

Family and domain databases

CDDⁱ	cd00608 GalT, 1 hit
Gene3Dⁱ	3.30.428.10, 2 hits
InterProⁱ	View protein in InterPro IPR001937 GalP_UDPtransf1 IPR019779 GalP_UDPtransf1_His-AS IPR005850 GalP_Utransf_C IPR005849 GalP_Utransf_N IPR036265 HIT-like_sf
PANTHERⁱ	PTHR11943 PTHR11943, 1 hit
Pfamⁱ	View protein in Pfam PF02744 GalP_UDP_tr_C, 1 hit PF01087 GalP_UDP_transf, 1 hit
PIRSFⁱ	PIRSF000808 GalT, 1 hit
SUPFAMⁱ	SSF54197 SSF54197, 2 hits
TIGRFAMsⁱ	TIGR00209 galT_1, 1 hit
PROSITEⁱ	View protein in PROSITE PS00117 GAL_P_UDP_TRANSF_I, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	GAL7_ECOLI
Accessionⁱ	P09148Primary (citable) accession number: P09148 Secondary accession number(s): P78270
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
	Last sequence update:	November 1, 1997
	Last modified:	November 7, 2018
	This is version 163 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, 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

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UniProtKB - P09148 (GAL7_ECOLI)

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Galactose-1-phosphate uridylyltransferase

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 ‘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: galactose 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

<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

<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

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

Experimental Info

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

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: galactose metabolism

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ