ID   ARGD_STRCL              Reviewed;         400 AA.
AC   Q9LCS5;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 100.
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};
OS   Streptomyces clavuligerus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC   3585 / VKM Ac-602;
RX   PubMed=11075930;
RA   Rodriguez-Garcia A., de la Fuente A., Perez-Redondo R., Martin J.F.,
RA   Liras P.;
RT   "Characterization and expression of the arginine biosynthesis gene cluster
RT   of Streptomyces clavuligerus.";
RL   J. Mol. Microbiol. Biotechnol. 2:543-550(2000).
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; 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; Z49111; CAB82482.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9LCS5; -.
DR   SMR; Q9LCS5; -.
DR   STRING; 443255.SCLAV_0798; -.
DR   PRIDE; Q9LCS5; -.
DR   eggNOG; COG4992; Bacteria.
DR   UniPathway; UPA00068; UER00109.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01107; ArgD_aminotrans_3; 1.
DR   InterPro; IPR004636; AcOrn/SuccOrn_fam.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00707; argD; 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; Transferase.
FT   CHAIN           1..400
FT                   /note="Acetylornithine aminotransferase"
FT                   /id="PRO_0000112799"
FT   BINDING         106..107
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         132
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         135
FT                   /ligand="N(2)-acetyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:57805"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         217..220
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         274
FT                   /ligand="N(2)-acetyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:57805"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         275
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   MOD_RES         246
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
SQ   SEQUENCE   400 AA;  41968 MW;  2098C14DF9359C2C CRC64;
     MSNQEFAQRW QGVMIDSYGT PGLSFVRGEG STLWDADGTA YTDFVSGLAV NALGHAHPAV
     VGAVSRQIAS LGHISNFYSA EPTITLAERL IELFGRPGRV FFCNSGAEAN ETAFKIGRLT
     GRSRIVAAQS GFHGRTMGSL ALTGQPAKRE PFLPLPGDVT HVPYGDAEAL RAAVTEDTAM
     VILEPIQGES GVVVPPKGYL RAAREITEAT GTLLVLDEVQ TGIGRTGHWF AAQAEGVEAD
     VVTLAKGLGG GLPLGAAVAF GRAAELMTPG HHASTFGGNP VSCARTRVLD TIAADGLLDR
     VKQLGSAPDE WSVRDAAAIR WSPMSGAGLM LGIVLNEPLA PQVQLAAQKA GFLVNVPAPD
     VVRLIPPLVI EETEVDAFLQ ALPGLLDAVH ERDREGQTGE