7KWX

Spermidine N-acetyltransferase SpeG N152L mutant from Vibrio cholerae

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004145	molecular_function	diamine N-acetyltransferase activity
A	0005737	cellular_component	cytoplasm
A	0006598	biological_process	polyamine catabolic process
A	0016746	molecular_function	acyltransferase activity
A	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
A	0046203	biological_process	spermidine catabolic process
A	0046208	biological_process	spermine catabolic process
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0004145	molecular_function	diamine N-acetyltransferase activity
B	0005737	cellular_component	cytoplasm
B	0006598	biological_process	polyamine catabolic process
B	0016746	molecular_function	acyltransferase activity
B	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
B	0046203	biological_process	spermidine catabolic process
B	0046208	biological_process	spermine catabolic process
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0004145	molecular_function	diamine N-acetyltransferase activity
C	0005737	cellular_component	cytoplasm
C	0006598	biological_process	polyamine catabolic process
C	0016746	molecular_function	acyltransferase activity
C	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
C	0046203	biological_process	spermidine catabolic process
C	0046208	biological_process	spermine catabolic process
C	0046872	molecular_function	metal ion binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P0A951

Chain	Residue	Details
B	TYR134
C	TYR134
A	TYR134

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0000269|Ref.3, ECO:0007744|PDB:4MJ8

Chain	Residue	Details
A	MET28
A	GLU84
B	MET28
B	GLU84
C	MET28
C	GLU84

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0007744|PDB:4MI4

Chain	Residue	Details
A	GLU33
B	GLU33
C	GLU33

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0007744|PDB:4MI4, ECO:0007744|PDB:4R87

Chain	Residue	Details
A	GLU41
B	GLU41
C	GLU41

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0007744|PDB:4R87

Chain	Residue	Details
A	HIS49
B	HIS49
C	HIS49

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0000269|PubMed:26410587, ECO:0007744|PDB:5CNP

Chain	Residue	Details
A	GLU75
B	GLU75
C	GLU75

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0007744|PDB:4R57, ECO:0007744|PDB:4R87

Chain	Residue	Details
A	ILE87
A	GLN94
B	ILE87
B	GLN94
C	ILE87
C	GLN94

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0007744|PDB:4R57

Chain	Residue	Details
A	ASN127
B	ASN127
C	ASN127

---

site_id	SWS_FT_FI9
Number of Residues	3
Details	SITE: Could be important for selectivity toward long polyamines => ECO:0000305|PubMed:25623305

Chain	Residue	Details
A	GLU84
B	GLU84
C	GLU84

---