ID   OAT2_STAAS              Reviewed;         396 AA.
AC   Q6GAW9;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 33.
DE   RecName: Full=Ornithine aminotransferase 2;
DE            Short=OAT 2;
DE            EC=2.6.1.13;
DE   AltName: Full=Ornithine--oxo-acid aminotransferase 2;
GN   Name=rocD2; OrderedLocusNames=SAS0827;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282459;
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.
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DR   EMBL; BX571857; CAG42602.1; -; Genomic_DNA.
DR   RefSeq; YP_042954.1; -.
DR   GeneID; 2864407; -.
DR   GenomeReviews; BX571857_GR; SAS0827.
DR   KEGG; sas:SAS0827; -.
DR   HOGENOM; Q6GAW9; -.
DR   OMA; Q6GAW9; WAVGQLA.
DR   BioCyc; SAUR282459:SAS0827-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:0006561; P:proline biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01689; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
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; 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    396       Ornithine aminotransferase 2.
FT                                /FTId=PRO_0000112789.
FT   MOD_RES     255    255       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   396 AA;  43418 MW;  37CCCCDC9840CCF3 CRC64;
     MTKSEKIIEL TNHYGAHNYL PLPIVISEAE GVWVKDPEGN KYMDMLSAYS AVNQGHRHPK
     IIQALKDQAD KVTLVSRAFH SDNLGEWYEK ICKLAGKDKA LPMNTGAEAV ETALKAARRW
     AYDVKGIEPN KAEIIAFNGN FHGRTMAPVS LSSEAEYQRG YGPLLDGFRK VDFGDVDALK
     AAINENTAAV LVEPIQGEAG INIPPEGYLK AIRELCDEHN VLFIADEIQA GLGRSGKLFA
     TDWDNVKPDV YILGKALGGG VFPISVVLAD KEVLDVFTPG SHGSTFGGNP LACAASIAAL
     DVIVDEDLPG RSLELGDYFK EQLKQIDHPS IKEVRGRGLF IGVELNESAR PYCEALKEEG
     LLCKETHDTV IRFAPPLIIT KEELDLALEK IRHVFQ
//