ID   OAT1_STAAR              Reviewed;         394 AA.
AC   Q6GKC1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 35.
DE   RecName: Full=Ornithine aminotransferase 1;
DE            Short=OAT 1;
DE            EC=2.6.1.13;
DE   AltName: Full=Ornithine--oxo-acid aminotransferase 1;
GN   Name=rocD1; OrderedLocusNames=SAR0186;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Catalyzes the interconversion of ornithine to glutamate
CC       semialdehyde (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-ornithine + a 2-oxo acid = L-glutamate 5-
CC       semialdehyde + an L-amino acid.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC       glutamate 5-semialdehyde from L-ornithine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. OAT 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; BX571856; CAG39213.1; -; Genomic_DNA.
DR   RefSeq; YP_039651.1; -.
DR   GeneID; 2860210; -.
DR   GenomeReviews; BX571856_GR; SAR0186.
DR   KEGG; sar:SAR0186; -.
DR   HOGENOM; Q6GKC1; -.
DR   OMA; Q6GKC1; TICAANG.
DR   BioCyc; SAUR282458:SAR0186-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004587; F:ornithine-oxo-acid transaminase activity; IEA:HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP.
DR   GO; GO:0006525; P:arginine metabolic process; IEA:InterPro.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01689; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR004636; ArgD_aminotrans.
DR   InterPro; IPR010164; Orn_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:SF18; Orn_aminotrans; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   TIGRFAMs; TIGR00707; argD; 1.
DR   TIGRFAMs; TIGR01885; Orn_aminotrans; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW   Cytoplasm; Proline biosynthesis; Pyridoxal phosphate; Transferase.
FT   CHAIN         1    394       Ornithine aminotransferase 1.
FT                                /FTId=PRO_0000112786.
FT   MOD_RES     252    252       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   394 AA;  43042 MW;  125653621113B74C CRC64;
     MNSIIELTDY YSSNNYAPLK LVITEGKGGK VWDTDGKQYI DCISGFSVAN QGHCHPTIVK
     AMTEQASKLS IISRVLYSDN LGKWEEKICH LAKKDKVLPL NSGTEAVEAA IKIARKWGSD
     VKGITDGQVE IIAMNNNFHG RTLGSLSLSN HDAYKSGFHP LLQGTKTVDF GDIEQLTQAI
     SPNTAAIILE PIQGEGGVNI PPKGYIQAVR QLCDKHQILL IADEIQVGLG RTGKWFAMEW
     EQVVPDIYIL GKALGGGLYP VSAVLANNDV MRVLTPGTHG STFGGNPLAI AISTAALDVL
     KDEQLVERSE RLGSFLLKAL LQLKHPSIKE IRGRGLFIGI ELNTDAAPFV EQLIKRGILC
     KDTHRTIIRL SPPLVIDKEE INQIVAAFQD VFKN
//