9S1Q

Crystal structure of the DABA transaminase EctB from the halophilic and cold-adapted Marinobacter sp. CK1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008483	molecular_function	transaminase activity
A	0009058	biological_process	biosynthetic process
A	0019491	biological_process	ectoine biosynthetic process
A	0030170	molecular_function	pyridoxal phosphate binding
A	0045303	molecular_function	L-2,4-diaminobutyrate:2-oxoglutarate transaminase activity
A	0047307	molecular_function	L-2,4-diaminobutyrate:pyruvate transaminase activity
B	0008483	molecular_function	transaminase activity
B	0009058	biological_process	biosynthetic process
B	0019491	biological_process	ectoine biosynthetic process
B	0030170	molecular_function	pyridoxal phosphate binding
B	0045303	molecular_function	L-2,4-diaminobutyrate:2-oxoglutarate transaminase activity
B	0047307	molecular_function	L-2,4-diaminobutyrate:pyruvate transaminase activity
C	0008483	molecular_function	transaminase activity
C	0009058	biological_process	biosynthetic process
C	0019491	biological_process	ectoine biosynthetic process
C	0030170	molecular_function	pyridoxal phosphate binding
C	0045303	molecular_function	L-2,4-diaminobutyrate:2-oxoglutarate transaminase activity
C	0047307	molecular_function	L-2,4-diaminobutyrate:pyruvate transaminase activity
D	0008483	molecular_function	transaminase activity
D	0009058	biological_process	biosynthetic process
D	0019491	biological_process	ectoine biosynthetic process
D	0030170	molecular_function	pyridoxal phosphate binding
D	0045303	molecular_function	L-2,4-diaminobutyrate:2-oxoglutarate transaminase activity
D	0047307	molecular_function	L-2,4-diaminobutyrate:pyruvate transaminase activity

Functional Information from PROSITE/UniProt

site_id	PS00599
Number of Residues	10
Details	AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TVSKSLSGYG

Chain	Residue	Details
A	THR261-GLY270

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site_id	PS00600
Number of Residues	37
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIlDDIqa.GNgRtGeffsfefagitp....DIVtvSKsl.SG

Chain	Residue	Details
A	LEU232-GLY268

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