1UIR

Crystal Structure of Polyamine Aminopropyltransfease from Thermus thermophilus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004766	molecular_function	spermidine synthase activity
A	0005737	cellular_component	cytoplasm
A	0006596	biological_process	polyamine biosynthetic process
A	0008295	biological_process	spermidine biosynthetic process
A	0010487	molecular_function	thermospermine synthase activity
A	0016740	molecular_function	transferase activity
A	0016768	molecular_function	spermine synthase activity
A	0043918	molecular_function	cadaverine aminopropyltransferase activity
A	0043919	molecular_function	agmatine aminopropyltransferase activity
B	0003824	molecular_function	catalytic activity
B	0004766	molecular_function	spermidine synthase activity
B	0005737	cellular_component	cytoplasm
B	0006596	biological_process	polyamine biosynthetic process
B	0008295	biological_process	spermidine biosynthetic process
B	0010487	molecular_function	thermospermine synthase activity
B	0016740	molecular_function	transferase activity
B	0016768	molecular_function	spermine synthase activity
B	0043918	molecular_function	cadaverine aminopropyltransferase activity
B	0043919	molecular_function	agmatine aminopropyltransferase activity

Functional Information from PROSITE/UniProt

site_id	PS01330
Number of Residues	14
Details	PABS_1 Polyamine biosynthesis (PABS) domain signature. VLIVGGGeGatLrE

Chain	Residue	Details
A	VAL81-GLU94

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255\|HAMAP-Rule:MF_00198

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00198, ECO:0000269\|PubMed:21458463, ECO:0007744\|PDB:3ANX

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00198