7XII

Crystal structure of the aminopropyltransferase, SpeE from hyperthermophilic crenarchaeon, Pyrobaculum calidifontis in complex with 5'-methylthioadenosine (MTA) & aminopropylagmatine

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	0016740	molecular_function	transferase activity
A	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
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	0016740	molecular_function	transferase activity
B	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
C	0003824	molecular_function	catalytic activity
C	0004766	molecular_function	spermidine synthase activity
C	0005737	cellular_component	cytoplasm
C	0006596	biological_process	polyamine biosynthetic process
C	0008295	biological_process	spermidine biosynthetic process
C	0016740	molecular_function	transferase activity
C	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
D	0003824	molecular_function	catalytic activity
D	0004766	molecular_function	spermidine synthase activity
D	0005737	cellular_component	cytoplasm
D	0006596	biological_process	polyamine biosynthetic process
D	0008295	biological_process	spermidine biosynthetic process
D	0016740	molecular_function	transferase activity
D	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL84-GLU97

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00198

Chain	Residue	Details
A	ASP164
B	ASP164
C	ASP164
D	ASP164

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site_id	SWS_FT_FI2
Number of Residues	20
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00198

Chain	Residue	Details
A	GLN36
B	ASP143
C	GLN36
C	HIS67
C	GLU91
C	ASP111
C	ASP143
D	GLN36
D	HIS67
D	GLU91
D	ASP111
A	HIS67
D	ASP143
A	GLU91
A	ASP111
A	ASP143
B	GLN36
B	HIS67
B	GLU91
B	ASP111

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