ID   ARGD2_BORPA             Reviewed;         396 AA.
AC   Q7W2N9;
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 2;
DE            Short=ACOAT 2;
DE            EC=2.6.1.11;
GN   Name=argD2; OrderedLocusNames=BPP4365;
OS   Bordetella parapertussis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=519;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
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; BX640436; CAE39644.1; -; Genomic_DNA.
DR   RefSeq; NP_886493.1; -.
DR   GeneID; 1666162; -.
DR   GenomeReviews; BX470249_GR; BPP4365.
DR   KEGG; bpa:BPP4365; -.
DR   NMPDR; fig|257311.1.peg.4127; -.
DR   HOGENOM; Q7W2N9; -.
DR   OMA; Q7W2N9; LFAYELS.
DR   BioCyc; BPAR257311:BPP4365-MON; -.
DR   BRENDA; 2.6.1.11; 263123.
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    396       Acetylornithine aminotransferase 2.
FT                                /FTId=PRO_0000112726.
FT   REGION      219    222       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING     134    134       Pyridoxal phosphate; via carbonyl oxygen
FT                                (By similarity).
FT   BINDING     137    137       N(2)-acetyl-L-ornithine (By similarity).
FT   BINDING     276    276       Pyridoxal phosphate (By similarity).
FT   MOD_RES     248    248       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   396 AA;  42749 MW;  9CF07AF14A6378FF CRC64;
     MEFSQFKVNA LMEITACPDL VFVRGQGSWL EDHAGKRYLD FVQGWAVNTL GHCAPEMKRA
     LAEQADKLMN PSPAFYNLPS IELAQRLTSA SCFDRVFFAN SGAEANEGAI KLARKWGRVN
     RNGAYKIITM NHGFHGRTLA TMSASGKPGW DTMFAPQVEG FPKAEINDLD SVRALIDAQT
     VAVMLEPVQG EAGVIPATRE FMQGLRKLAD EHGILFIVDE VQTGMGRTGS LFAYQQFDVI
     PDIMTLAKGI GGGIPLAALL AREEVCVFAH GDQGGTYNGN PLCAAVGVAV FDTITAPGFM
     EAAQARTRQL SEGLLALSAK RGLRGERGMG LLRALVLDRD DAPAIVEAAR MLAPEGLLLN
     APRGNLLRFM PALNVTEADM ARMLEQLDGV IAAVRK
//