3PHJ

Shikimate 5-Dehydrogenase (aroE) from Helicobacter pylori in complex with 3-Dehydroshikimate

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	d3phja2	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	automated matches	automated matches	Campylobacter pylori (Helicobacter pylori 26695 ) [TaxId: 85962 ],	SCOPe (2.08)
A	d3phja1	Alpha and beta proteins (a/b)	Aminoacid dehydrogenase-like, N-terminal domain	Aminoacid dehydrogenase-like, N-terminal domain	automated matches	automated matches	Campylobacter pylori (Helicobacter pylori 26695 ) [TaxId: 85962 ],	SCOPe (2.08)
B	d3phjb2	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	automated matches	automated matches	Campylobacter pylori (Helicobacter pylori 26695 ) [TaxId: 85962 ],	SCOPe (2.08)
B	d3phjb1	Alpha and beta proteins (a/b)	Aminoacid dehydrogenase-like, N-terminal domain	Aminoacid dehydrogenase-like, N-terminal domain	automated matches	automated matches	Campylobacter pylori (Helicobacter pylori 26695 ) [TaxId: 85962 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	MtdA-like	8074752	3000046	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	MtdA-like	8074752	3000046	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	Shikimate_DH	e3phjA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: Shikimate_DH	ECOD (1.6)
A	Shikimate_dh_N	e3phjA2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Aminoacid dehydrogenase-like, N-terminal domain	F: Shikimate_dh_N	ECOD (1.6)
B	Shikimate_DH	e3phjB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: Shikimate_DH	ECOD (1.6)
B	Shikimate_dh_N	e3phjB2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Aminoacid dehydrogenase-like, N-terminal domain	F: Shikimate_dh_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.10860	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Leucine Dehydrogenase, chain A, domain 1	CATH (4.3.0)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
B	3.40.50.10860	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Leucine Dehydrogenase, chain A, domain 1	CATH (4.3.0)
B	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF08501	Shikimate dehydrogenase substrate binding domain (Shikimate_dh_N)	Shikimate dehydrogenase substrate binding domain	This domain is the substrate binding domain of shikimate dehydrogenase [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Shikimate dehydrogenase	oxidoreductase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on CH-OH group of donors shikimate 3-dehydrogenase (NADP+) activity catalytic activity binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP binding small molecule binding	oxoacid metabolic process organic hydroxy compound metabolic process cellular metabolic process carboxylic acid metabolic process organic acid metabolic process organic substance metabolic process metabolic process small molecule metabolic process cellular process shikimate metabolic process monocarboxylic acid metabolic process amino acid biosynthetic process biosynthetic process organic substance biosynthetic process oxoacid metabolic process organic hydroxy compound metabolic process cellular metabolic process carboxylic acid metabolic process organic acid metabolic process organic substance metabolic process metabolic process small molecule metabolic process cellular process shikimate metabolic process monocarboxylic acid metabolic process amino acid biosynthetic process biosynthetic process organic substance biosynthetic process amino acid metabolic process primary metabolic process small molecule biosynthetic process cellular biosynthetic process dicarboxylic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process chorismate metabolic process chorismate biosynthetic process dicarboxylic acid biosynthetic process organonitrogen compound metabolic process aromatic amino acid family biosynthetic process aromatic amino acid metabolic process organonitrogen compound biosynthetic process organic cyclic compound metabolic process organic cyclic compound biosynthetic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B	IPR046346	Aminoacid dehydrogenase-like, N-terminal domain superfamily	Homologous Superfamily
A, B	IPR022893	Shikimate dehydrogenase family	Family
A, B	IPR011342	Shikimate dehydrogenase	Family
A, B	IPR013708	Shikimate dehydrogenase substrate binding, N-terminal	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.