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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
A0006526biological_processarginine biosynthetic process
A0006527biological_processarginine catabolic process
A0006593biological_processornithine catabolic process
A0008483molecular_functiontransaminase activity
A0019544biological_processarginine catabolic process to glutamate
A0019545biological_processarginine catabolic process to succinate
A0030170molecular_functionpyridoxal phosphate binding
A0042450biological_processarginine biosynthetic process via ornithine
A0042802molecular_functionidentical protein binding
A0043825molecular_functionsuccinylornithine transaminase activity
B0003992molecular_functionN2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
B0006520biological_processamino acid metabolic process
B0006525biological_processarginine metabolic process
B0006526biological_processarginine biosynthetic process
B0006527biological_processarginine catabolic process
B0006593biological_processornithine catabolic process
B0008483molecular_functiontransaminase activity
B0019544biological_processarginine catabolic process to glutamate
B0019545biological_processarginine catabolic process to succinate
B0030170molecular_functionpyridoxal phosphate binding
B0042450biological_processarginine biosynthetic process via ornithine
B0042802molecular_functionidentical protein binding
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
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250
ChainResidueDetails
ALYS252
BLYS252

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PDB entries from 2024-07-24

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