2X65

Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with mannose-1-phosphate.

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	MannoseP_isomer	e2x65A1	A: beta duplicates or obligate multimers	X: Single-stranded left-handed beta-helix	H: Guanosine diphospho-D-mannose pyrophosphorylase/mannose-6-phosphate isomerase linker domain (From Topology)	T: Guanosine diphospho-D-mannose pyrophosphorylase/mannose-6-phosphate isomerase linker domain	F: MannoseP_isomer	ECOD (1.6)
A	NTP_transferase	e2x65A2	A: a/b three-layered sandwiches	X: Nucleotide-diphospho-sugar transferases (From Topology)	H: Nucleotide-diphospho-sugar transferases (From Topology)	T: Nucleotide-diphospho-sugar transferases	F: NTP_transferase	ECOD (1.6)
B	MannoseP_isomer	e2x65B1	A: beta duplicates or obligate multimers	X: Single-stranded left-handed beta-helix	H: Guanosine diphospho-D-mannose pyrophosphorylase/mannose-6-phosphate isomerase linker domain (From Topology)	T: Guanosine diphospho-D-mannose pyrophosphorylase/mannose-6-phosphate isomerase linker domain	F: MannoseP_isomer	ECOD (1.6)
B	NTP_transferase	e2x65B2	A: a/b three-layered sandwiches	X: Nucleotide-diphospho-sugar transferases (From Topology)	H: Nucleotide-diphospho-sugar transferases (From Topology)	T: Nucleotide-diphospho-sugar transferases	F: NTP_transferase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.550.10	Alpha Beta	Alpha-Beta Complex	Spore Coat Polysaccharide Biosynthesis Protein SpsA	Chain A	CATH (4.3.0)
B	3.90.550.10	Alpha Beta	Alpha-Beta Complex	Spore Coat Polysaccharide Biosynthesis Protein SpsA	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF22640	MannoseP isomerase/GMP-like beta-helix domain (ManC_GMP_beta-helix)	MannoseP isomerase/GMP-like beta-helix domain	This entry represents a left-handed beta-helix domain found at the C-terminal of Guanosine-diphospho-d-mannose Pyrophosphorylase (GMP) from Thermotoga maritima [1] and as a linker domain in mannose-1-phosphate guanylyltransferases, alginate biosynthe ...	This entry represents a left-handed beta-helix domain found at the C-terminal of Guanosine-diphospho-d-mannose Pyrophosphorylase (GMP) from Thermotoga maritima [1] and as a linker domain in mannose-1-phosphate guanylyltransferases, alginate biosynthesis protein AlgA and xanthan biosynthesis protein XanB, among others, located between the Nucleotidyl transferase domain at the N-terminal (Pfam:PF00483) and the C-terminal isomerase cupin domain (Pfam:PF01050). This domain is composed of an alpha-helix followed by a short left-handed beta-helix. GMP forms a dimer in which two molecules associate through a tail-to-tail arrangement of this domain [1]..	Domain
A, B	PF00483	Nucleotidyl transferase (NTP_transferase)	Nucleotidyl transferase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	MANNOSE-1-PHOSPHATE GUANYLYLTRANSFERASE	guanylyltransferase activity mannose-1-phosphate guanylyltransferase (GTP) activity transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups binding guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding guanylyltransferase activity mannose-1-phosphate guanylyltransferase (GTP) activity transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups binding guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding organic cyclic compound binding purine nucleotide binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding cation binding metal ion binding	nucleoside phosphate metabolic process carbohydrate derivative biosynthetic process nucleotide-sugar metabolic process carbohydrate derivative metabolic process primary metabolic process nucleobase-containing compound biosynthetic process nucleobase-containing compound metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process nucleobase-containing small molecule metabolic process nucleoside phosphate biosynthetic process phosphate-containing compound metabolic process GDP-mannose biosynthetic process nucleoside phosphate metabolic process carbohydrate derivative biosynthetic process nucleotide-sugar metabolic process carbohydrate derivative metabolic process primary metabolic process nucleobase-containing compound biosynthetic process nucleobase-containing compound metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process nucleobase-containing small molecule metabolic process nucleoside phosphate biosynthetic process phosphate-containing compound metabolic process GDP-mannose biosynthetic process metabolic process cellular process small molecule metabolic process nucleotide-sugar biosynthetic process phosphorus metabolic process GDP-mannose metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR049577	GDP-mannose pyrophosphorylase, N-terminal domain	Domain
A, B	IPR005835	Nucleotidyl transferase domain	Domain
A, B	IPR029044	Nucleotide-diphospho-sugar transferases	Homologous Superfamily
A, B	IPR051161	Mannose-6-phosphate isomerase type 2	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.