ID   ARGD_BACST              Reviewed;         385 AA.
AC   Q07907; Q9ZB64;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 2.
DT   16-JUN-2009, entry version 71.
DE   RecName: Full=Acetylornithine aminotransferase;
DE            Short=ACOAT;
DE            EC=2.6.1.11;
GN   Name=argD;
OS   Bacillus stearothermophilus (Geobacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-149.
RC   STRAIN=NCIB 8224 / CCM 2186;
RX   MEDLINE=93232760; PubMed=8473852;
RA   Sakanyan V., Charlier D.R.M., Legrain C., Kochikyan A., Mett I.,
RA   Pierard P., Glansdorff N.;
RT   "Primary structure, partial purification and regulation of key enzymes
RT   of the acetyl cycle of arginine biosynthesis in Bacillus
RT   stearothermophilus: dual function of ornithine acetyltransferase.";
RL   J. Gen. Microbiol. 139:393-402(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 148-385.
RC   STRAIN=ATCC 12980 / DSM 22 / IFO 12550 / NCIB 8923 / NCTC 10339;
RX   MEDLINE=98036119; PubMed=9370352;
RX   DOI=10.1111/j.1432-1033.1997.00443.x;
RA   Yang H., Park S.M., Nolan W.G., Lu C.-D., Abdelal A.T.;
RT   "Cloning and characterization of the arginine-specific carbamoyl-
RT   phosphate synthetase from Bacillus stearothermophilus.";
RL   Eur. J. Biochem. 249:443-449(1997).
CC   -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-
CC       acetyl-L-glutamate 5-semialdehyde + L-glutamate.
CC   -!- COFACTOR: Binds 1 pyridoxal phosphate per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 4/4.
CC   -!- SUBUNIT: Homodimer (By similarity).
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. ArgD subfamily.
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DR   EMBL; L06036; AAA22199.1; -; Genomic_DNA.
DR   EMBL; U43091; AAC78718.1; -; Genomic_DNA.
DR   PIR; I39768; I39768.
DR   HSSP; P12995; 1QJ3.
DR   BRENDA; 2.6.1.11; 266715.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-amin...; 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   Cytoplasm; Pyridoxal phosphate; Transferase.
FT   CHAIN         1    385       Acetylornithine aminotransferase.
FT                                /FTId=PRO_0000112720.
FT   REGION      207    210       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING     122    122       Pyridoxal phosphate; via carbonyl oxygen
FT                                (By similarity).
FT   BINDING     125    125       N(2)-acetyl-L-ornithine (By similarity).
FT   BINDING     264    264       N(2)-acetyl-L-ornithine (By similarity).
FT   BINDING     265    265       Pyridoxal phosphate (By similarity).
FT   MOD_RES     236    236       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   385 AA;  41304 MW;  A40E6AC2ED105604 CRC64;
     MSALFPTYNR WNIAVQSAEG TVVTDVNGKQ YLDFVSGIAV CNLGHRHPHV QKSIEQQLNQ
     YWHVSNLFTI PIQEEVASLL VAHSAGDYVF FCNSGAEANE AALKLARKHT GRHKVITFRQ
     SFHGRTFATM AATGQEKVHS GFGPLLPEFI HLPLNDVDAL KQAMSEEVAA VMLEVVQGEG
     GVRPVDPAFL QTASELCQQH GALLIIDEVQ TGIGRTGKPF AYQHFDVEPD IITAAKGLGS
     GIPVGAMIGK AFLKESFGPG VHGSTFGGNP IAMAAAKATL EVVFDPAFLQ DVQEKGRYFL
     ARLHDALASL DIVKDVRGLG LLVGIECQTD VAPLLPLIHE NGLLVLSAGP NVIRLLPLVV
     TKAEIDEAVD ILTNVLNNAN ASAVL
//