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5E9F

Structural insights of isocitrate lyases from Magnaporthe oryzae

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004451molecular_functionisocitrate lyase activity
A0006097biological_processglyoxylate cycle
A0006099biological_processtricarboxylic acid cycle
A0009514cellular_componentglyoxysome
A0016829molecular_functionlyase activity
A0019752biological_processcarboxylic acid metabolic process
A0046421molecular_functionmethylisocitrate lyase activity
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004451molecular_functionisocitrate lyase activity
B0006097biological_processglyoxylate cycle
B0006099biological_processtricarboxylic acid cycle
B0009514cellular_componentglyoxysome
B0016829molecular_functionlyase activity
B0019752biological_processcarboxylic acid metabolic process
B0046421molecular_functionmethylisocitrate lyase activity
B0046872molecular_functionmetal ion binding
C0003824molecular_functioncatalytic activity
C0004451molecular_functionisocitrate lyase activity
C0006097biological_processglyoxylate cycle
C0006099biological_processtricarboxylic acid cycle
C0009514cellular_componentglyoxysome
C0016829molecular_functionlyase activity
C0019752biological_processcarboxylic acid metabolic process
C0046421molecular_functionmethylisocitrate lyase activity
C0046872molecular_functionmetal ion binding
D0003824molecular_functioncatalytic activity
D0004451molecular_functionisocitrate lyase activity
D0006097biological_processglyoxylate cycle
D0006099biological_processtricarboxylic acid cycle
D0009514cellular_componentglyoxysome
D0016829molecular_functionlyase activity
D0019752biological_processcarboxylic acid metabolic process
D0046421molecular_functionmethylisocitrate lyase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue MG A 601
ChainResidue
AASP123
AASP177
AASP179

site_idAC2
Number of Residues3
Detailsbinding site for residue MG B 601
ChainResidue
BASP123
BASP177
BASP179

site_idAC3
Number of Residues4
Detailsbinding site for residue MG C 601
ChainResidue
CGLU206
CASP123
CASP177
CASP179

site_idAC4
Number of Residues4
Detailsbinding site for residue MG D 601
ChainResidue
DASP123
DASP177
DASP179
DGLU206

Functional Information from PROSITE/UniProt
site_idPS00161
Number of Residues6
DetailsISOCITRATE_LYASE Isocitrate lyase signature. KKCGHM
ChainResidueDetails
ALYS213-MET218

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P9WKK7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242500

PDB entries from 2025-10-01

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