6J31

Crystal Structure Analysis of the Glycotransferase of kitacinnamycin

External Resource: Annotation

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

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	F_UNCLASSIFIED	e6j31A2	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: F_UNCLASSIFIED	ECOD (1.6)
A	PF06722	e6j31A1	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: PF06722	ECOD (1.6)
B	F_UNCLASSIFIED	e6j31B1	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: F_UNCLASSIFIED	ECOD (1.6)
B	PF06722	e6j31B2	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: PF06722	ECOD (1.6)
C	F_UNCLASSIFIED	e6j31C1	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: F_UNCLASSIFIED	ECOD (1.6)
C	PF06722	e6j31C2	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: PF06722	ECOD (1.6)
D	F_UNCLASSIFIED	e6j31D2	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: F_UNCLASSIFIED	ECOD (1.6)
D	PF06722	e6j31D1	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: PF06722	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.2000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glycogen Phosphorylase B	CATH (utative)
B	3.40.50.2000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glycogen Phosphorylase B	CATH (utative)
C	3.40.50.2000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glycogen Phosphorylase B	CATH (utative)
D	3.40.50.2000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glycogen Phosphorylase B	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF06722	Erythromycin biosynthesis protein CIII-like, C-terminal domain (EryCIII-like_C)	Erythromycin biosynthesis protein CIII-like, C-terminal domain	This domain is found at the C-terminal of Erythromycin biosynthesis protein CIII (EryCIII) from Saccharopolyspora erythraea and similar proteins found in bacteria and eukaryotes. This protein is organised into two domains, both of them with a Rossman ...	This domain is found at the C-terminal of Erythromycin biosynthesis protein CIII (EryCIII) from Saccharopolyspora erythraea and similar proteins found in bacteria and eukaryotes. This protein is organised into two domains, both of them with a Rossmann-like alpha/beta fold. The C-terminal domain contains the nucleotide disphospho-sugar (NDP-sugar) binding site [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	kcn28	glycosyltransferase activity transferase activity hexosyltransferase activity catalytic activity UDP-glycosyltransferase activity	antibiotic metabolic process biosynthetic process metabolic process antibiotic biosynthetic process	-
E, F, G, H	DBB-DSG-VAL-MEA-VAL-GLY-GLY-DVA-DLE	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR035595	UDP-glycosyltransferase family, conserved site	Conserved Site
A, B, C, D	IPR002213	UDP-glucuronosyl/UDP-glucosyltransferase	Family
A, B, C, D	IPR006326	UDP-glycosyltransferase, MGT-like	Family
A, B, C, D	IPR010610	Erythromycin biosynthesis protein CIII-like, C-terminal domain	Domain

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
E, F, G, H	DBB	RESID: AA0112 PSI-MOD : (2S,3S,2'R)-3-methyllanthionine MOD:00121
E, F, G, H	DLE	RESID: AA0112 , AA0197 PSI-MOD : (2S,3S,2'R)-3-methyllanthionine MOD:00121 , D-leucine MOD:00204
E, F, G, H	DSG	RESID: AA0112 , AA0197 , AA0196 , AA0622 PSI-MOD : (2S,3S,2'R)-3-methyllanthionine MOD:00121 , D-leucine MOD:00204 , D-asparagine MOD:00203 , 2-(L-cystein-S-yl)-D-asparagine MOD:01985
E, F, G, H	DVA	RESID: AA0112 , AA0197 , AA0196 , AA0622 , AA0200 PSI-MOD : (2S,3S,2'R)-3-methyllanthionine MOD:00121 , D-leucine MOD:00204 , D-asparagine MOD:00203 , 2-(L-cystein-S-yl)-D-asparagine MOD:01985 , D-valine MOD:00705
E, F, G, H	MEA	Parent Component: PHE RESID: AA0112 , AA0197 , AA0196 , AA0622 , AA0200 , AA0065 PSI-MOD : (2S,3S,2'R)-3-methyllanthionine MOD:00121 , D-leucine MOD:00204 , D-asparagine MOD:00203 , 2-(L-cystein-S-yl)-D-asparagine MOD:01985 , D-valine MOD:00705 , N-methyl-L-phenylalanine MOD:00074

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.