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4ADE

Structural and functional study of succinyl-ornithine transaminase from E. coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0003992molecular_functionN2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
A0006520biological_processamino acid metabolic process
A0006525biological_processarginine metabolic process
A0006527biological_processL-arginine catabolic process
A0006593biological_processL-ornithine catabolic process
A0008483molecular_functiontransaminase activity
A0016740molecular_functiontransferase activity
A0019544biological_processL-arginine catabolic process to L-glutamate
A0019545biological_processL-arginine catabolic process to succinate
A0030170molecular_functionpyridoxal phosphate binding
A0042450biological_processL-arginine biosynthetic process via ornithine
A0042802molecular_functionidentical protein binding
A0043648biological_processdicarboxylic acid metabolic process
A0043825molecular_functionsuccinylornithine transaminase activity
B0003992molecular_functionN2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
B0006520biological_processamino acid metabolic process
B0006525biological_processarginine metabolic process
B0006527biological_processL-arginine catabolic process
B0006593biological_processL-ornithine catabolic process
B0008483molecular_functiontransaminase activity
B0016740molecular_functiontransferase activity
B0019544biological_processL-arginine catabolic process to L-glutamate
B0019545biological_processL-arginine catabolic process to succinate
B0030170molecular_functionpyridoxal phosphate binding
B0042450biological_processL-arginine biosynthetic process via ornithine
B0042802molecular_functionidentical protein binding
B0043648biological_processdicarboxylic acid metabolic process
B0043825molecular_functionsuccinylornithine transaminase activity
Functional Information from PROSITE/UniProt
site_idPS00600
Number of Residues38
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIfDEVqt.GVgRtGelyaymhygvtp....DLLttAKalgGG
ChainResidueDetails
ALEU220-GLY257

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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