ID   OAT2_STAS1              Reviewed;         396 AA.
AC   Q49W96;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 32.
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=SSP1818;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 /
OS   DSM 20229).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K.,
RA   Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S.,
RA   Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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; AP008934; BAE18963.1; -; Genomic_DNA.
DR   RefSeq; YP_301908.1; -.
DR   GeneID; 3616473; -.
DR   GenomeReviews; AP008934_GR; SSP1818.
DR   KEGG; ssp:SSP1818; -.
DR   NMPDR; fig|342451.4.peg.1890; -.
DR   HOGENOM; Q49W96; -.
DR   OMA; Q49W96; SERLMRE.
DR   BioCyc; SSAP342451:SSP1818-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_0000112797.
FT   MOD_RES     255    255       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   396 AA;  43399 MW;  02BC20FA8B3FEE43 CRC64;
     MSRSEEIIEV TNHYGAQNYV PLPIVISEAE GVWVKDPEGN KYMDMLSAYS AVNQGHRHPK
     IIQALKEQAD KVTLVSRAFH SENLGEWYEK ICKLSGKAKA LPMNTGAEAV ETALKAARRW
     AYDVKNIQPD KAEIIAFNGN FHGRTMAPVS LSSEPEYQRG YGPLLDGFRK VDFGDIEAVK
     AAINENTAAI LIEPIQGEAG INVPPEGYLK QIRELCDEHN VLFIADEIQA GLGRSGKLFA
     TDWDNVKPDV YILGKALGGG VLPISVVLAD EEVLGVFTPG SHGSTFGGNP LACAVSNAAL
     DVIIDEDLPG RSLELGDYFK SELEKIDHPA IKEVRGRGLF IGIELNEAAR PFCESLKEQG
     LLCKETHDTV IRFAPPLIIS KEELDFALDK VRSVFE
//