ID   ARGD_SHEON              Reviewed;         405 AA.
AC   P59320;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   12-FEB-2003, sequence version 1.
DT   02-SEP-2026, entry version 146.
DE   RecName: Full=Acetylornithine aminotransferase {ECO:0000255|HAMAP-Rule:MF_01107};
DE            Short=ACOAT {ECO:0000255|HAMAP-Rule:MF_01107};
DE            EC=2.6.1.11 {ECO:0000255|HAMAP-Rule:MF_01107};
GN   Name=argD {ECO:0000255|HAMAP-Rule:MF_01107};
GN   OrderedLocusNames=SO_0617;
OS   Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG
OS   19005 / NCIMB 14063 / MR-1).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Alteromonadales; Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063
RC   / MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-
CC         glutamate 5-semialdehyde + L-glutamate; Xref=Rhea:RHEA:18049,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57805; EC=2.6.1.11; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01107};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01107};
CC       Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01107};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 4/4. {ECO:0000255|HAMAP-
CC       Rule:MF_01107}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01107}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01107}.
CC   -!- MISCELLANEOUS: May also have succinyldiaminopimelate aminotransferase
CC       activity, thus carrying out the corresponding step in lysine
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01107}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. ArgD subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01107}.
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DR   EMBL; AE014299; AAN53695.1; -; Genomic_DNA.
DR   RefSeq; WP_011070947.1; NC_004347.2.
DR   AlphaFoldDB; P59320; -.
DR   SMR; P59320; -.
DR   STRING; 211586.SO_0617; -.
DR   PaxDb; 211586-SO_0617; -.
DR   KEGG; son:SO_0617; -.
DR   PATRIC; fig|211586.12.peg.595; -.
DR   eggNOG; COG4992; Bacteria.
DR   HOGENOM; CLU_016922_10_1_6; -.
DR   OrthoDB; 9801052at2; -.
DR   PhylomeDB; P59320; -.
DR   BioCyc; SONE211586:G1GMP-586-MONOMER; -.
DR   UniPathway; UPA00068; UER00109.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-transaminase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006526; P:L-arginine biosynthetic process; IBA:GO_Central.
DR   CDD; cd00610; OAT_like; 1.
DR   FunFam; 3.40.640.10:FF:000004; Acetylornithine aminotransferase; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_01107; ArgD_aminotrans_3; 1.
DR   InterPro; IPR017652; Ac/SucOrn_transaminase_bac.
DR   InterPro; IPR004636; AcOrn/SuccOrn_fam.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR050103; Class-III_PLP-dep_AT.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR03246; arg_catab_astC; 1.
DR   NCBIfam; TIGR00707; argD; 1.
DR   NCBIfam; NF002325; PRK01278.1; 1.
DR   NCBIfam; NF003468; PRK05093.1; 1.
DR   NCBIfam; NF009047; PRK12381.1; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF113; SUCCINYLORNITHINE TRANSAMINASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis;
KW   Cytoplasm; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..405
FT                   /note="Acetylornithine aminotransferase"
FT                   /id="PRO_0000112778"
FT   BINDING         107..108
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         140
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         143
FT                   /ligand="N(2)-acetyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:57805"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         225..228
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         282
FT                   /ligand="N(2)-acetyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:57805"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         283
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   MOD_RES         254
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
SQ   SEQUENCE   405 AA;  43214 MW;  5EF6879ED99283E0 CRC64;
     MSVDMKLNRA QFDAVMVPNY APAAVIPVRG EGSRVWDQEG NEFIDFAGGI AVNCLGHCHP
     ALVNALKTQG EKLWHLSNVM TNEPALELAT KLVNSTFAER VYFANSGAEA NEAALKLARR
     YALEKHGVEK DEIIAFDKAF HGRTFFTVSV GGQAAYSDGF GPKPQSITHL PFNDVAALEA
     AVSDKTCAIM LEPLQGEGGI IDADPAFLKA VRELANKHNA LVIFDEVQTG VGRTGELYAY
     MGTDIVPDIL TTAKALGGGF PIAAMLTTTE IAEHLKVGTH GSTYGGNPLA CAIGNAVLDV
     VNTPEVLNGV KHREQLLRDG LNKINEKYHV FSEVRGKGLL LGAVLNEQYQ GRSRDFLVAS
     VAEGLMSLMA GANVVRFAPS LVIPEADIAE GLARFERAVA SIAAA
//