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5E9H

Structural insights of isocitrate lyases from Fusarium graminearum

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MN A 601
ChainResidue
AASP177
AHOH714
AHOH716
AHOH719
AHOH727
AHOH824

site_idAC2
Number of Residues12
Detailsbinding site for residue MLI A 602
ChainResidue
AASN432
ASER434
ASER436
ATHR466
ALEU467
AHOH708
AHOH714
AHOH719
AHOH824
ATRP108
ACYS215
AHIS217

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 Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P9WKK7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues19
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P9WKK7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242500

PDB entries from 2025-10-01

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