1PMI

Candida Albicans Phosphomannose Isomerase

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1pmia_	All beta proteins	Double-stranded beta-helix	RmlC-like cupins	Type I phosphomannose isomerase	Phosphomannose isomerase	(Candida albicans ) [TaxId: 5476 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Type I phosphomannose isomerase	8030663	4002872	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	RmlC-like cupins	8043042	3001825	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)
A	PF01238	e1pmiA3	A: beta sandwiches	X: jelly-roll	H: Double-stranded beta-helix (From Topology)	T: Double-stranded beta-helix	F: PF01238	ECOD (1.6)
A	PF20511	e1pmiA2	A: beta sandwiches	X: jelly-roll	H: Double-stranded beta-helix (From Topology)	T: Double-stranded beta-helix	F: PF20511	ECOD (1.6)
A	PF20512	e1pmiA4	A: alpha arrays	X: Phosphomannose isomerase helical insertion domain (From Topology)	H: Phosphomannose isomerase helical insertion domain (From Topology)	T: Phosphomannose isomerase helical insertion domain	F: PF20512	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.120.10	Mainly Beta	Sandwich	Jelly Rolls	Jelly Rolls	CATH (4.3.0)
A	1.10.441.10	Mainly Alpha	Orthogonal Bundle	Phosphomannose Isomerase	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01238	Phosphomannose isomerase type I C-terminal (PMI_typeI_C)	Phosphomannose isomerase type I C-terminal	This is the C-terminal domain of Phosphomannose isomerase type I enzymes (EC 5.3.1.8), which contains antiparallel beta-strands in an extended jelly roll topology with short loops connecting the strands [1].	Domain
A	PF20511	Phosphomannose isomerase type I, catalytic domain (PMI_typeI_cat)	Phosphomannose isomerase type I, catalytic domain	This entry represents the catalytic domain of Phosphomannose isomerase type I enzymes (EC 5.3.1.8) which contains a zinc-binding site. It is composed of beta-strands connected by long loops in a jelly roll conformation [1].	Domain
A	PF20512	Phosphomannose isomerase type I, helical insertion domain (PMI_typeI_hel)	Phosphomannose isomerase type I, helical insertion domain	This entry represents the alpha-helical insertion domain of Phosphomannose isomerase type I enzymes (EC 5.3.1.8), in which the helices are packed closely, connected by short turns and loops. This domain packs closely against the catalytic domain, int ...	This entry represents the alpha-helical insertion domain of Phosphomannose isomerase type I enzymes (EC 5.3.1.8), in which the helices are packed closely, connected by short turns and loops. This domain packs closely against the catalytic domain, interrupting it [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	PHOSPHOMANNOSE ISOMERASE	isomerase activity intramolecular oxidoreductase activity, interconverting aldoses and ketoses intramolecular oxidoreductase activity mannose-6-phosphate isomerase activity catalytic activity cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding	carbohydrate derivative biosynthetic process organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process organonitrogen compound biosynthetic process glycoprotein biosynthetic process carbohydrate derivative metabolic process primary metabolic process glycoprotein metabolic process protein glycosylation macromolecule biosynthetic process organic substance metabolic process biosynthetic process glycosylation macromolecule modification carbohydrate derivative biosynthetic process organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process organonitrogen compound biosynthetic process glycoprotein biosynthetic process carbohydrate derivative metabolic process primary metabolic process glycoprotein metabolic process protein glycosylation macromolecule biosynthetic process organic substance metabolic process biosynthetic process glycosylation macromolecule modification macromolecule glycosylation organic substance biosynthetic process metabolic process cellular process protein metabolic process macromolecule metabolic process protein modification process carbohydrate metabolic process nucleotide-sugar metabolic process nucleobase-containing compound biosynthetic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process nucleobase-containing small molecule metabolic process organic cyclic compound biosynthetic process GDP-mannose biosynthetic process small molecule metabolic process nucleotide-sugar biosynthetic process GDP-mannose metabolic process fungal-type cell wall organization cellular component organization fungal-type cell wall organization or biogenesis cell wall organization or biogenesis cell wall organization cellular component organization or biogenesis external encapsulating structure organization mannoprotein biosynthetic process cell wall mannoprotein biosynthetic process mannoprotein metabolic process cell wall glycoprotein biosynthetic process cell wall macromolecule metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR018050	Phosphomannose isomerase, type I, conserved site	Conserved Site
A	IPR046457	Phosphomannose isomerase type I, catalytic domain	Domain
A	IPR014710	RmlC-like jelly roll fold	Homologous Superfamily
A	IPR001250	Mannose-6-phosphate isomerase, type I	Family
A	IPR016305	Mannose-6-phosphate isomerase	Family
A	IPR011051	RmlC-like cupin domain superfamily	Homologous Superfamily
A	IPR046458	Phosphomannose isomerase type I, helical insertion domain	Domain
A	IPR046456	Phosphomannose isomerase type I, C-terminal domain	Domain

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	mannose-6-phosphate isomerase (type I) M-CSA #880	Mannose-6-phosphate isomerase or phosphomannose isomerase (EC:5.3.1.8) (PMI) is the enzyme that catalyses the interconversion of mannose-6-phosphate and fructose-6-phosphate. In eukaryotes PMI is involved in the synthesis of GDP-mannose, a constituent of N- and O-linked glycans and GPI anchors and in prokaryotes it participates in a variety of pathways, including capsular polysaccharide biosynthesis and D-mannose metabolism. PMIs in this entry belong to the cupin superfamily whose functions range from isomerase and epimerase activities involved in the modification of cell wall carbohydrates in bacteria and plants, to non-enzymatic storage proteins in plant seeds, and transcription factors linked to congenital baldness in mammals [PMID: 11165500].	Defined by 8 residues: SER:A-108 [auth A-109]GLN:A-110 [auth A-111]HIS:A-112 [auth A-113]LYS:A-135 [auth A-136]GLU:A-137 [auth A-138]HIS:A-284 [auth A-285]ARG:A-303 [auth A-304]LYS:A-309 [auth A-310] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 5.3.1.8 (PDB Primary Data) Search M-CSA Motif + EC 5.3.1.8

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 R01GM133198.