5U4H

1.05 Angstrom Resolution Crystal Structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase from Acinetobacter baumannii in Covalently Bound Complex with (2R)-2-(phosphonooxy)propanoic Acid.

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)
B	d5u4hb1	Alpha and beta proteins (a+b)	IF3-like	EPT/RTPC-like	automated matches	automated matches	(Acinetobacter baumannii ) [TaxId: 470 ],	SCOPe (2.08)
B	d5u4hb2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Acinetobacter baumannii ) [TaxId: 470 ],	SCOPe (2.08)
A	d5u4ha1	Alpha and beta proteins (a+b)	IF3-like	EPT/RTPC-like	automated matches	automated matches	(Acinetobacter baumannii ) [TaxId: 470 ],	SCOPe (2.08)
A	d5u4ha2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Acinetobacter baumannii ) [TaxId: 470 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	EPT/RTPC-like	8074714	3001530	SCOP2B (2022-06-29)
A	SCOP2 Family	Enolpyruvate transferase, EPT	8074713	4001425	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	EPT/RTPC-like	8074714	3001530	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	EPSP_synthase_C_1	e5u4hB1	A: a+b two layers	X: IF3-like	H: EPT/RTPC-like (From Topology)	T: EPT/RTPC-like	F: EPSP_synthase_C_1	ECOD (1.6)
B	EPSP_synthase_N	e5u4hB2	A: a+b two layers	X: IF3-like	H: EPT/RTPC-like (From Topology)	T: EPT/RTPC-like	F: EPSP_synthase_N	ECOD (1.6)
A	EPSP_synthase_C_1	e5u4hA2	A: a+b two layers	X: IF3-like	H: EPT/RTPC-like (From Topology)	T: EPT/RTPC-like	F: EPSP_synthase_C_1	ECOD (1.6)
A	EPSP_synthase_N	e5u4hA1	A: a+b two layers	X: IF3-like	H: EPT/RTPC-like (From Topology)	T: EPT/RTPC-like	F: EPSP_synthase_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.65.10.10	Alpha Beta	Alpha-beta prism	UDP-n-acetylglucosamine1-carboxyvinyl-transferase	Chain	CATH (4.3.0)
A	3.65.10.10	Alpha Beta	Alpha-beta prism	UDP-n-acetylglucosamine1-carboxyvinyl-transferase	Chain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00275	EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase) (EPSP_synthase)	EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase)	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	UDP-N-acetylglucosamine 1-carboxyvinyltransferase	UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups catalytic activity	developmental process regulation of biological process regulation of developmental process biological regulation regulation of cell shape cell morphogenesis regulation of cell morphogenesis anatomical structure morphogenesis anatomical structure development regulation of biological quality regulation of anatomical structure morphogenesis amino sugar biosynthetic process carbohydrate derivative metabolic process nucleobase-containing compound metabolic process developmental process regulation of biological process regulation of developmental process biological regulation regulation of cell shape cell morphogenesis regulation of cell morphogenesis anatomical structure morphogenesis anatomical structure development regulation of biological quality regulation of anatomical structure morphogenesis amino sugar biosynthetic process carbohydrate derivative metabolic process nucleobase-containing compound metabolic process UDP-N-acetylgalactosamine metabolic process nucleobase-containing small molecule metabolic process amino sugar metabolic process phosphate-containing compound metabolic process small molecule metabolic process phosphorus metabolic process nucleotide-sugar biosynthetic process nucleoside phosphate metabolic process carbohydrate derivative biosynthetic process nucleotide-sugar metabolic process cellular metabolic process primary metabolic process nucleobase-containing compound biosynthetic process biosynthetic process UDP-N-acetylgalactosamine biosynthetic process organophosphate metabolic process organophosphate biosynthetic process nucleoside phosphate biosynthetic process metabolic process cellular process cell division cellular component organization cell wall organization or biogenesis cell wall organization cellular component organization or biogenesis external encapsulating structure organization peptidoglycan-based cell wall biogenesis cellular biosynthetic process glycosaminoglycan metabolic process macromolecule biosynthetic process cellular component biogenesis peptidoglycan biosynthetic process cell wall biogenesis cell wall macromolecule biosynthetic process aminoglycan metabolic process peptidoglycan metabolic process aminoglycan biosynthetic process glycosaminoglycan biosynthetic process macromolecule metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR002110	Ankyrin repeat	Repeat
A, B	IPR001986	Enolpyruvate transferase domain	Domain
A, B	IPR005750	UDP-N-acetylglucosamine 1-carboxyvinyltransferase	Family
A, B	IPR036968	Enolpyruvate transferase domain superfamily	Homologous Superfamily
A, B	IPR013792	RNA 3'-terminal phosphate cyclase/enolpyruvate transferase, alpha/beta	Homologous Superfamily
A, B	IPR050068	UDP-N-acetylglucosamine 1-carboxyvinyltransferase MurA subfamily	Family

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.