ID   ARGD1_BORPE             Reviewed;         393 AA.
AC   Q7VTJ7;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   16-JUN-2009, entry version 44.
DE   RecName: Full=Acetylornithine aminotransferase 1;
DE            Short=ACOAT 1;
DE            EC=2.6.1.11;
GN   Name=argD1; OrderedLocusNames=BP3539;
OS   Bordetella pertussis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=520;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   MEDLINE=22827954; PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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.
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; BX640421; CAE43798.1; -; Genomic_DNA.
DR   RefSeq; NP_882054.1; -.
DR   GeneID; 2665147; -.
DR   GenomeReviews; BX470248_GR; BP3539.
DR   KEGG; bpe:BP3539; -.
DR   NMPDR; fig|257313.1.peg.3124; -.
DR   HOGENOM; Q7VTJ7; -.
DR   OMA; Q7VTJ7; YFAYQHT.
DR   BioCyc; BPER257313:BP3539-MON; -.
DR   BRENDA; 2.6.1.11; 21511.
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   Complete proteome; Cytoplasm; Pyridoxal phosphate; Transferase.
FT   CHAIN         1    393       Acetylornithine aminotransferase 1.
FT                                /FTId=PRO_0000112727.
FT   REGION      215    218       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING     131    131       N(2)-acetyl-L-ornithine (By similarity).
FT   BINDING     272    272       N(2)-acetyl-L-ornithine (By similarity).
FT   BINDING     273    273       Pyridoxal phosphate (By similarity).
FT   MOD_RES     244    244       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   393 AA;  41438 MW;  90442EA116445BD3 CRC64;
     MSSALANIYA RLPVSFTHGR GVWLWDTGER RYLDALAGIG VSCLGHGHPG LVAAISEQAA
     RLIHTSNIYE VPQQAALARR LAELSGMSEV LFNNSGSEAN EAAIKLARYY GYKQGNTHAH
     IITMDSSWHG RTLATLAATG SDKARQGFGP MPSGFIQVPY NDLPAIRAAG EAEPRVTAVL
     LEVLQGEGGI RPSDMAFLQG VRQLCTERGW LLMIDEVQSG IGRTGKWFAH QWADIRPDVM
     TLAKGLAGGV PIGAMLAAGP AAGVFAPGSH GTTFGGGPLA CAAGLAVIDA IEQEGLLGNA
     HEVGAHLHAA LASELAGAPG VIEVRGRGLM LGIELDRPCG ILATRAMEAG LLINVTRERV
     VRLLPPLILS GEEADQIVRI LVPLIKQFLA QQQ
//