5CGE

Structure of Hydroxyethylthiazole Kinase ThiM from Staphylococcus aureus in complex with substrate analog 2-(2-methyl-1H-imidazole-1-yl)ethanol

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d5cgea1	Alpha and beta proteins (a/b)	Ribokinase-like	Ribokinase-like	automated matches	automated matches	(Staphylococcus aureus subsp. aureus MRSA252 ) [TaxId: 282458 ],	SCOPe (2.08)
A	d5cgea2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Staphylococcus aureus subsp. aureus MRSA252 ) [TaxId: 282458 ],	SCOPe (2.08)
B	d5cgeb_	Alpha and beta proteins (a/b)	Ribokinase-like	Ribokinase-like	automated matches	automated matches	(Staphylococcus aureus subsp. aureus MRSA252 ) [TaxId: 282458 ],	SCOPe (2.08)
C	d5cgec_	Alpha and beta proteins (a/b)	Ribokinase-like	Ribokinase-like	automated matches	automated matches	(Staphylococcus aureus subsp. aureus MRSA252 ) [TaxId: 282458 ],	SCOPe (2.08)
D [auth E]	d5cgee1	Alpha and beta proteins (a/b)	Ribokinase-like	Ribokinase-like	automated matches	automated matches	(Staphylococcus aureus subsp. aureus MRSA252 ) [TaxId: 282458 ],	SCOPe (2.08)
D [auth E]	d5cgee2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Staphylococcus aureus subsp. aureus MRSA252 ) [TaxId: 282458 ],	SCOPe (2.08)
E [auth D]	d5cged_	Alpha and beta proteins (a/b)	Ribokinase-like	Ribokinase-like	automated matches	automated matches	(Staphylococcus aureus subsp. aureus MRSA252 ) [TaxId: 282458 ],	SCOPe (2.08)
F	d5cgef_	Alpha and beta proteins (a/b)	Ribokinase-like	Ribokinase-like	automated matches	automated matches	(Staphylococcus aureus subsp. aureus MRSA252 ) [TaxId: 282458 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Ribokinase-like	8065921	3001268	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Ribokinase-like	8065921	3001268	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Ribokinase-like	8065921	3001268	SCOP2B (2022-06-29)
D [auth E]	SCOP2B Superfamily	Ribokinase-like	8065921	3001268	SCOP2B (2022-06-29)
E [auth D]	SCOP2B Superfamily	Ribokinase-like	8065921	3001268	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Ribokinase-like	8065921	3001268	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Carb_kinase	e5cgeA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Ribokinase-like (From Topology)	T: Ribokinase-like	F: Carb_kinase	ECOD (1.6)
B	Carb_kinase	e5cgeB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Ribokinase-like (From Topology)	T: Ribokinase-like	F: Carb_kinase	ECOD (1.6)
C	Carb_kinase	e5cgeC1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Ribokinase-like (From Topology)	T: Ribokinase-like	F: Carb_kinase	ECOD (1.6)
D [auth E]	Carb_kinase	e5cgeE1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Ribokinase-like (From Topology)	T: Ribokinase-like	F: Carb_kinase	ECOD (1.6)
E [auth D]	Carb_kinase	e5cgeD1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Ribokinase-like (From Topology)	T: Ribokinase-like	F: Carb_kinase	ECOD (1.6)
F	Carb_kinase	e5cgeF1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Ribokinase-like (From Topology)	T: Ribokinase-like	F: Carb_kinase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.1190.20	Alpha Beta	3-Layer(aba) Sandwich	UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase	Ribokinase	CATH (4.3.0)
B	3.40.1190.20	Alpha Beta	3-Layer(aba) Sandwich	UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase	Ribokinase	CATH (4.3.0)
C	3.40.1190.20	Alpha Beta	3-Layer(aba) Sandwich	UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase	Ribokinase	CATH (4.3.0)
D [auth E]	3.40.1190.20	Alpha Beta	3-Layer(aba) Sandwich	UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase	Ribokinase	CATH (4.3.0)
E [auth D]	3.40.1190.20	Alpha Beta	3-Layer(aba) Sandwich	UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase	Ribokinase	CATH (4.3.0)
F	3.40.1190.20	Alpha Beta	3-Layer(aba) Sandwich	UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase	Ribokinase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D [auth E], E [auth D], A, B, C, D [auth E], E [auth D], F	PF02110	Hydroxyethylthiazole kinase family (HK)	Hydroxyethylthiazole kinase family	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D [auth E], E [auth D], A, B, C, D [auth E], E [auth D], F	Hydroxyethylthiazole kinase	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding hydroxyethylthiazole kinase activity kinase activity transferase activity catalytic activity phosphotransferase activity, alcohol group as acceptor transferase activity, transferring phosphorus-containing groups	cellular biosynthetic process thiamine-containing compound metabolic process vitamin biosynthetic process phosphate-containing compound metabolic process thiamine diphosphate metabolic process small molecule metabolic process sulfur compound metabolic process pyrimidine-containing compound biosynthetic process water-soluble vitamin metabolic process phosphorus metabolic process pyrimidine-containing compound metabolic process water-soluble vitamin biosynthetic process small molecule biosynthetic process cellular metabolic process cellular biosynthetic process thiamine-containing compound metabolic process vitamin biosynthetic process phosphate-containing compound metabolic process thiamine diphosphate metabolic process small molecule metabolic process sulfur compound metabolic process pyrimidine-containing compound biosynthetic process water-soluble vitamin metabolic process phosphorus metabolic process pyrimidine-containing compound metabolic process water-soluble vitamin biosynthetic process small molecule biosynthetic process cellular metabolic process vitamin metabolic process sulfur compound biosynthetic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process metabolic process cellular process thiamine diphosphate biosynthetic process thiamine-containing compound biosynthetic process organic hydroxy compound metabolic process alcohol metabolic process thiamine metabolic process thiamine biosynthetic process primary alcohol biosynthetic process organic hydroxy compound biosynthetic process alcohol biosynthetic process primary alcohol metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D [auth E], E [auth D], A, B, C, D [auth E], E [auth D], F	IPR000417	Hydroxyethylthiazole kinase	Family
A, B, C, D [auth E], E [auth D], A, B, C, D [auth E], E [auth D], F	IPR029056	Ribokinase-like	Homologous Superfamily

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.