ID   OAT2_STAAR              Reviewed;         396 AA.
AC   Q6GID1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 34.
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=SAR0919;
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.
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DR   EMBL; BX571856; CAG39925.1; -; Genomic_DNA.
DR   RefSeq; YP_040341.1; -.
DR   GeneID; 2859280; -.
DR   GenomeReviews; BX571856_GR; SAR0919.
DR   KEGG; sar:SAR0919; -.
DR   HOGENOM; Q6GID1; -.
DR   OMA; Q6GID1; WAVGQLA.
DR   BioCyc; SAUR282458:SAR0919-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_0000112787.
FT   MOD_RES     255    255       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   396 AA;  43472 MW;  316DF664A635423F CRC64;
     MTKSEKIIEL TNHYGAHNYL PLPIVISEAE GVWVKDPEGN KYMDMLSAYS AVNQGHRHPK
     IIQALKDQAD KVTLVSRAFH SDNLGEWYEK ICKLAGKDKA LPMNTGAEAV ETALKAARRW
     AYDVKGIEPN KAEIIAFNGN FHGRTMAPVS LSSEAEYQRG YGPLLDGFRK VDFGDVDALK
     AAINKNTAAV LVEPIQGEAG INIPPEGYLK AIRELCDEHN VLFIADEIQA GLGRSGKLFA
     RDWDNVKPDV YILGKALGGG VFPISVVLAD KEVLDVFTPG SHGSTFGGNP LACAASIAAL
     DVIVDEDLPG RSLELGDYFK EQLKQIDHPS IKEVRGRGLF IGVELNESAR PYCEALKEEG
     LLCKETHDTV IRFAPPLIIT KEELDLALEK IRHVFQ
//