AC   MF_01107;
DC   Protein; auto
TR   HAMAP; MF_01107; -; 1; level=0
XX
Names: ArgD_aminotrans_3
XX
ID   ARGD
case <OC:Enterobacterales>
DE   RecName: Full=Acetylornithine/succinyldiaminopimelate aminotransferase;
DE            Short=ACOAT;
DE            Short=DapATase;
DE            Short=Succinyldiaminopimelate transferase;
DE            EC=2.6.1.11;
DE            EC=2.6.1.17;
GN   Name=argD; Synonyms=dapC;
else
DE   RecName: Full=Acetylornithine aminotransferase;
DE            Short=ACOAT;
DE            EC=2.6.1.11;
GN   Name=argD;
end case
XX
case <OC:Enterobacterales>
CC   -!- FUNCTION: Involved in both the arginine and lysine biosynthetic
CC       pathways.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-
CC         acetyl-L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:18049,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57805; EC=2.6.1.11;
case <OC:Enterobacterales>
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate =
CC         (S)-2-succinylamino-6-oxoheptanedioate + L-glutamate;
CC         Xref=Rhea:RHEA:11960, ChEBI:CHEBI:15685, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58087; EC=2.6.1.17;
end case
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC       Note=Binds 1 pyridoxal phosphate per subunit.;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 4/4.
case <OC:Enterobacterales>
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC       (succinylase route): step 2/3.
end case
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
case not <OC:Enterobacterales>
CC   -!- MISCELLANEOUS: May also have succinyldiaminopimelate aminotransferase
CC       activity, thus carrying out the corresponding step in lysine
CC       biosynthesis.
end case
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. ArgD subfamily.
XX
DR   Pfam; PF00202; Aminotran_3; 1; trigger=no
DR   NCBIfam; TIGR00707; ArgD; 1; trigger=no
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1; trigger=no
XX
KW   Cytoplasm
KW   Amino-acid biosynthesis
KW   Arginine biosynthesis
case <OC:Enterobacterales>
KW   Lysine biosynthesis
end case
KW   Transferase
KW   Aminotransferase
KW   Pyridoxal phosphate
XX
GO   GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
case <OC:Enterobacterales>
GO   GO:0009016; F:succinyldiaminopimelate transaminase activity
GO   GO:0009085; P:lysine biosynthetic process
end case
GO   GO:0006526; P:arginine biosynthetic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: ARGD_ECOLI (P18335)
FT   BINDING         108..109
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Optional; Condition: G-[TA]
FT   BINDING         226..229
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Optional; Condition: D-E-[IV]-Q
FT   BINDING         141
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Optional; Condition: F
FT   BINDING         144
FT                   /ligand="N(2)-acetyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:57805"
FT   Optional; Condition: R
FT   BINDING         283
FT                   /ligand="N(2)-acetyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:57805"
FT   Optional; Condition: [ST]
FT   BINDING         284
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Optional; Condition: T
FT   MOD_RES         255
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   Condition: K
XX
Size: 360-480;
Related: MF_01173!;
Template: P18335; P40732; O66442;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in BORBR, BORPA, BORPE, BRADU, PSESM
Plasmid: None
Comments: None
XX
# Revision 1.55 2023/06/01
//