7XQN

InDel-mutant malate dehydrogenase from E. coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006096	biological_process	glycolytic process
A	0006099	biological_process	tricarboxylic acid cycle
A	0006108	biological_process	malate metabolic process
A	0009061	biological_process	anaerobic respiration
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0016615	molecular_function	malate dehydrogenase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0019752	biological_process	carboxylic acid metabolic process
A	0019898	cellular_component	extrinsic component of membrane
A	0030060	molecular_function	L-malate dehydrogenase (NAD+) activity
A	0042803	molecular_function	protein homodimerization activity
B	0003824	molecular_function	catalytic activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006096	biological_process	glycolytic process
B	0006099	biological_process	tricarboxylic acid cycle
B	0006108	biological_process	malate metabolic process
B	0009061	biological_process	anaerobic respiration
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0016615	molecular_function	malate dehydrogenase activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0019752	biological_process	carboxylic acid metabolic process
B	0019898	cellular_component	extrinsic component of membrane
B	0030060	molecular_function	L-malate dehydrogenase (NAD+) activity
B	0042803	molecular_function	protein homodimerization activity

Functional Information from PROSITE/UniProt

site_id	PS00068
Number of Residues	13
Details	MDH Malate dehydrogenase active site signature. VTTLDiiRSntfV

Chain	Residue	Details
A	VAL143-VAL155

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01516","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11389141","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01516","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11389141","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8331658","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01516","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1507230","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8331658","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 527

Chain	Residue	Details
A	ASP147	modifies pKa
A	HIS174	proton acceptor, proton donor

---

site_id	MCSA2
Number of Residues	2
Details	M-CSA 527

Chain	Residue	Details
B	ASP147	modifies pKa
B	HIS174	proton acceptor, proton donor

---