5TVM

Crystal structure of Trypanosoma brucei AdoMetDC/prozyme heterodimer

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)
D	SAM_decarbox	e5tvmD1	A: a+b two layers	X: TBP-like	H: S-adenosylmethionine decarboxylase-related	T: S-adenosylmethionine decarboxylase	F: SAM_decarbox	ECOD (1.6)
B	SAM_decarbox	e5tvmB1	A: a+b two layers	X: TBP-like	H: S-adenosylmethionine decarboxylase-related	T: S-adenosylmethionine decarboxylase	F: SAM_decarbox	ECOD (1.6)
E	SAM_decarbox	e5tvmE1	A: a+b two layers	X: TBP-like	H: S-adenosylmethionine decarboxylase-related	T: S-adenosylmethionine decarboxylase	F: SAM_decarbox	ECOD (1.6)
F	SAM_decarbox	e5tvmF1	A: a+b two layers	X: TBP-like	H: S-adenosylmethionine decarboxylase-related	T: S-adenosylmethionine decarboxylase	F: SAM_decarbox	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
D	3.60.90.10	Alpha Beta	4-Layer Sandwich	S-adenosylmethionine decarboxylase	S-adenosylmethionine decarboxylase	CATH (4.3.0)
B	3.60.90.10	Alpha Beta	4-Layer Sandwich	S-adenosylmethionine decarboxylase	S-adenosylmethionine decarboxylase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
B, D	PF01536	Adenosylmethionine decarboxylase (SAM_decarbox)	Adenosylmethionine decarboxylase	-	Family
E, F	PF01536	Adenosylmethionine decarboxylase (SAM_decarbox)	Adenosylmethionine decarboxylase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C	S-adenosylmethionine decarboxylase beta chain	adenosylmethionine decarboxylase activity carboxy-lyase activity lyase activity catalytic activity carbon-carbon lyase activity	amine metabolic process biogenic amine biosynthetic process spermidine metabolic process biosynthetic process amine biosynthetic process polyamine biosynthetic process metabolic process spermidine biosynthetic process polyamine metabolic process biogenic amine metabolic process spermine metabolic process spermine biosynthetic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol
B, D	S-adenosylmethionine decarboxylase alpha chain	adenosylmethionine decarboxylase activity carboxy-lyase activity lyase activity catalytic activity carbon-carbon lyase activity	amine metabolic process biogenic amine biosynthetic process spermidine metabolic process biosynthetic process amine biosynthetic process polyamine biosynthetic process metabolic process spermidine biosynthetic process polyamine metabolic process biogenic amine metabolic process spermine metabolic process spermine biosynthetic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol
E, F	S-adenosylmethionine decarboxylase proenzyme-like, putative	lyase activity catalytic activity	amine metabolic process biogenic amine biosynthetic process spermidine metabolic process biosynthetic process amine biosynthetic process polyamine biosynthetic process metabolic process spermidine biosynthetic process polyamine metabolic process biogenic amine metabolic process spermine metabolic process spermine biosynthetic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C	IPR016067	S-adenosylmethionine decarboxylase, core	Homologous Superfamily
A, C	IPR001985	S-adenosylmethionine decarboxylase, eukaryotes	Family
A, C	IPR048283	S-adenosylmethionine decarboxylase-like	Family
A, C	IPR018166	S-adenosylmethionine decarboxylase, conserved site	Conserved Site
B, D	IPR016067	S-adenosylmethionine decarboxylase, core	Homologous Superfamily
B, D	IPR001985	S-adenosylmethionine decarboxylase, eukaryotes	Family
B, D	IPR048283	S-adenosylmethionine decarboxylase-like	Family
B, D	IPR018166	S-adenosylmethionine decarboxylase, conserved site	Conserved Site
E, F	IPR016067	S-adenosylmethionine decarboxylase, core	Homologous Superfamily
E, F	IPR048283	S-adenosylmethionine decarboxylase-like	Family

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
B, D	PYR	RESID: AA0127 PSI-MOD : pyruvic acid (Cys) MOD:00136 , pyruvic acid (Ser) MOD:00807 , pyruvic acid MOD:01154 , pyruvic acid (Tyr) MOD:01661

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.