4YBO

Structure of Citrate Synthase from the Thermoacidophilic Euryarchaeon Thermolasma acidophilum

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005737	cellular_component	cytoplasm
A	0005975	biological_process	carbohydrate metabolic process
A	0006099	biological_process	tricarboxylic acid cycle
A	0016740	molecular_function	transferase activity
A	0036440	molecular_function	citrate synthase activity
A	0046912	molecular_function	acyltransferase activity, acyl groups converted into alkyl on transfer
B	0003824	molecular_function	catalytic activity
B	0005737	cellular_component	cytoplasm
B	0005975	biological_process	carbohydrate metabolic process
B	0006099	biological_process	tricarboxylic acid cycle
B	0016740	molecular_function	transferase activity
B	0036440	molecular_function	citrate synthase activity
B	0046912	molecular_function	acyltransferase activity, acyl groups converted into alkyl on transfer
C	0003824	molecular_function	catalytic activity
C	0005737	cellular_component	cytoplasm
C	0005975	biological_process	carbohydrate metabolic process
C	0006099	biological_process	tricarboxylic acid cycle
C	0016740	molecular_function	transferase activity
C	0036440	molecular_function	citrate synthase activity
C	0046912	molecular_function	acyltransferase activity, acyl groups converted into alkyl on transfer
D	0003824	molecular_function	catalytic activity
D	0005737	cellular_component	cytoplasm
D	0005975	biological_process	carbohydrate metabolic process
D	0006099	biological_process	tricarboxylic acid cycle
D	0016740	molecular_function	transferase activity
D	0036440	molecular_function	citrate synthase activity
D	0046912	molecular_function	acyltransferase activity, acyl groups converted into alkyl on transfer

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue BCT B 400

Chain	Residue
B	LYS286
B	PRO287
B	GLU288
B	VAL289

---

site_id	AC2
Number of Residues	3
Details	binding site for residue BCT C 400

Chain	Residue
C	LYS286
C	PRO287
C	GLU288

---

Functional Information from PROSITE/UniProt

site_id	PS00480
Number of Residues	13
Details	CITRATE_SYNTHASE Citrate synthase signature. GFGHrVy.KtyDPR

Chain	Residue	Details
A	GLY259-ARG271

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Active site: {"evidences":[{"source":"PubMed","id":"7704526","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---