ID   ARGD_MYCBO              Reviewed;         400 AA.
AC   P63569; P94990;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-NOV-2008, entry version 30.
DE   RecName: Full=Acetylornithine aminotransferase;
DE            Short=ACOAT;
DE            EC=2.6.1.11;
GN   Name=argD; OrderedLocusNames=Mb1683;
OS   Mycobacterium bovis.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=1765;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   MEDLINE=22709107; PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H.,
RA   Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S.,
RA   Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R.,
RA   Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
CC   -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-
CC       acetyl-L-glutamate 5-semialdehyde + L-glutamate.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 4/4.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- MISCELLANEOUS: May also have succinyldiaminopimelate
CC       aminotransferase activity, thus carrying out the corresponding
CC       step in lysine biosynthesis.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BX248339; CAD96350.1; -; Genomic_DNA.
DR   RefSeq; NP_855335.1; -.
DR   HSSP; P12995; 1QJ3.
DR   GeneID; 1092626; -.
DR   GenomeReviews; BX248333_GR; Mb1683.
DR   KEGG; mbo:Mb1683; -.
DR   HOGENOM; P63569; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
DR   GO; GO:0003992; F:acetylornithine transaminase activity; IEA:HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01107; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR004636; ArgD_aminotrans.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   PANTHER; PTHR11986; Aminotrans_3; 1.
DR   PANTHER; PTHR11986:SF19; ArgD_aminotrans; 1.
DR   Pfam; PF00202; Aminotran_3; 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   Complete proteome; Cytoplasm; Pyridoxal phosphate; Transferase.
FT   CHAIN         1    400       Acetylornithine aminotransferase.
FT                                /FTId=PRO_0000112757.
FT   BINDING     253    253       Pyridoxal phosphate (covalent) (By
FT                                similarity).
SQ   SEQUENCE   400 AA;  40910 MW;  833846D529795019 CRC64;
     MTGASTTTAT MRQRWQAVMM NNYGTPPIAL ASGDGAVVTD VDGRTYIDLL GGIAVNVLGH
     RHPAVIEAVT RQMSTLGHTS NLYATEPGIA LAEELVALLG ADQRTRVFFC NSGAEANEAA
     FKLSRLTGRT KLVAAHDAFH GRTMGSLALT GQPAKQTPFA PLPGDVTHVG YGDVDALAAA
     VDDHTAAVFL EPIMGESGVV VPPAGYLAAA RDITARRGAL LVLDEVQTGM GRTGAFFAHQ
     HDGITPDVVT LAKGLGGGLP IGACLAVGPA AELLTPGLHG STFGGNPVCA AAALAVLRVL
     ASDGLVRRAE VLGKSLRHGI EALGHPLIDH VRGRGLLLGI ALTAPHAKDA EATARDAGYL
     VNAAAPDVIR LAPPLIIAEA QLDGFVAALP AILDRAVGAP
//