3CQ9

Crystal structure of the lp_1622 protein from Lactobacillus plantarum. Northeast Structural Genomics Consortium target LpR114

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF04265	e3cq9A4	A: beta sandwiches	X: jelly-roll	H: Thiamin pyrophosphokinase, substrate-binding domain (From Topology)	T: Thiamin pyrophosphokinase, substrate-binding domain	F: PF04265	ECOD (1.6)
A	PF04263	e3cq9A3	A: a/b three-layered sandwiches	X: Thiamin pyrophosphokinase, catalytic domain (From Topology)	H: Thiamin pyrophosphokinase, catalytic domain (From Topology)	T: Thiamin pyrophosphokinase, catalytic domain	F: PF04263	ECOD (1.6)
B	PF04265	e3cq9B4	A: beta sandwiches	X: jelly-roll	H: Thiamin pyrophosphokinase, substrate-binding domain (From Topology)	T: Thiamin pyrophosphokinase, substrate-binding domain	F: PF04265	ECOD (1.6)
B	PF04263	e3cq9B3	A: a/b three-layered sandwiches	X: Thiamin pyrophosphokinase, catalytic domain (From Topology)	H: Thiamin pyrophosphokinase, catalytic domain (From Topology)	T: Thiamin pyrophosphokinase, catalytic domain	F: PF04263	ECOD (1.6)
C	PF04265	e3cq9C4	A: beta sandwiches	X: jelly-roll	H: Thiamin pyrophosphokinase, substrate-binding domain (From Topology)	T: Thiamin pyrophosphokinase, substrate-binding domain	F: PF04265	ECOD (1.6)
C	PF04263	e3cq9C3	A: a/b three-layered sandwiches	X: Thiamin pyrophosphokinase, catalytic domain (From Topology)	H: Thiamin pyrophosphokinase, catalytic domain (From Topology)	T: Thiamin pyrophosphokinase, catalytic domain	F: PF04263	ECOD (1.6)
D	PF04265	e3cq9D4	A: beta sandwiches	X: jelly-roll	H: Thiamin pyrophosphokinase, substrate-binding domain (From Topology)	T: Thiamin pyrophosphokinase, substrate-binding domain	F: PF04265	ECOD (1.6)
D	PF04263	e3cq9D3	A: a/b three-layered sandwiches	X: Thiamin pyrophosphokinase, catalytic domain (From Topology)	H: Thiamin pyrophosphokinase, catalytic domain (From Topology)	T: Thiamin pyrophosphokinase, catalytic domain	F: PF04263	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.10240	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Thiamin pyrophosphokinase, catalytic domain	CATH (4.3.0)
B	3.40.50.10240	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Thiamin pyrophosphokinase, catalytic domain	CATH (4.3.0)
C	3.40.50.10240	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Thiamin pyrophosphokinase, catalytic domain	CATH (4.3.0)
D	3.40.50.10240	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Thiamin pyrophosphokinase, catalytic domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF04265	Thiamin pyrophosphokinase, vitamin B1 binding domain (TPK_B1_binding)	Thiamin pyrophosphokinase, vitamin B1 binding domain	Family of thiamin pyrophosphokinase (EC:2.7.6.2). Thiamin pyrophosphokinase (TPK) catalyses the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamin) to form the coenzyme thiamin pyrophosphate (TPP). Thus, TPK is important for the format ...	Family of thiamin pyrophosphokinase (EC:2.7.6.2). Thiamin pyrophosphokinase (TPK) catalyses the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamin) to form the coenzyme thiamin pyrophosphate (TPP). Thus, TPK is important for the formation of a coenzyme required for central metabolic functions. The structure of thiamin pyrophosphokinase suggest that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis [1].	Domain
A, B, C, D	PF04263	Thiamin pyrophosphokinase, catalytic domain (TPK_catalytic)	Thiamin pyrophosphokinase, catalytic domain	Family of thiamin pyrophosphokinase (EC:2.7.6.2). Thiamin pyrophosphokinase (TPK) catalyses the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamin) to form the coenzyme thiamin pyrophosphate (TPP). Thus, TPK is important for the format ...	Family of thiamin pyrophosphokinase (EC:2.7.6.2). Thiamin pyrophosphokinase (TPK) catalyses the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamin) to form the coenzyme thiamin pyrophosphate (TPP). Thus, TPK is important for the formation of a coenzyme required for central metabolic functions. The structure of thiamin pyrophosphokinase suggest that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Uncharacterized protein lp_1622	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding kinase activity transferase activity catalytic activity transferase activity, transferring phosphorus-containing groups cation binding vitamin binding thiamine binding alcohol binding sulfur compound binding diphosphotransferase activity thiamine diphosphokinase activity	phosphorylation cellular metabolic process phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic process pyrimidine-containing compound metabolic process organonitrogen compound metabolic process organic hydroxy compound metabolic process thiamine-containing compound metabolic process alcohol metabolic process thiamine metabolic process vitamin metabolic process organic cyclic compound metabolic process phosphorylation cellular metabolic process phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic process pyrimidine-containing compound metabolic process organonitrogen compound metabolic process organic hydroxy compound metabolic process thiamine-containing compound metabolic process alcohol metabolic process thiamine metabolic process vitamin metabolic process organic cyclic compound metabolic process organic substance metabolic process small molecule metabolic process sulfur compound metabolic process water-soluble vitamin metabolic process primary alcohol metabolic process cellular biosynthetic process organonitrogen compound biosynthetic process vitamin biosynthetic process organic substance biosynthetic process thiamine diphosphate metabolic process pyrimidine-containing compound biosynthetic process water-soluble vitamin biosynthetic process small molecule biosynthetic process sulfur compound biosynthetic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process organic cyclic compound biosynthetic process thiamine diphosphate biosynthetic process thiamine-containing compound biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR036759	Thiamin pyrophosphokinase, catalytic domain superfamily	Homologous Superfamily
A, B, C, D	IPR006282	Thiamin pyrophosphokinase	Family
A, B, C, D	IPR007373	Thiamin pyrophosphokinase, thiamin-binding domain	Domain
A, B, C, D	IPR007371	Thiamin pyrophosphokinase, catalytic domain	Domain

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.