ID   OAT1_STAS1              Reviewed;         394 AA.
AC   Q4A0N2;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 34.
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=SSP0220;
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; BAE17365.1; -; Genomic_DNA.
DR   RefSeq; YP_300310.1; -.
DR   GeneID; 3617138; -.
DR   GenomeReviews; AP008934_GR; SSP0220.
DR   KEGG; ssp:SSP0220; -.
DR   NMPDR; fig|342451.4.peg.571; -.
DR   HOGENOM; Q4A0N2; -.
DR   OMA; Q4A0N2; ESELIVE.
DR   BioCyc; SSAP342451:SSP0220-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    394       Ornithine aminotransferase 1.
FT                                /FTId=PRO_0000112796.
FT   MOD_RES     252    252       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   394 AA;  43538 MW;  D4DE3FBB2D343364 CRC64;
     MLDLYEHTDK YSSKNYSPLK LALAKGRGAK VWDIEDNCYI DCISGFSVVN QGHCHPKIIK
     ALQEQSQRIT MVSRALYSDN LGKWEEKICK LANKENVLPM NTGTEAVETA IKMARKWGAD
     IKNIDESSSE IIAMNGNFHG RTLGSLSLSS QDSYKKGFGP LLNNIHYADF GDIEQLKKLI
     NNQTTAIILE PIQGEGGVNI PPTHFIQEVR QLCNEYNVLL IADEIQVGLG RTGKMFAMEW
     ENTEPDIYLL GKSLGGGLYP ISAVLANQDV MSVLTPGTHG STFGGNPLAC AVSMAALDVL
     NEEHLVQNAL DLGDRLLKHL QQIESELIVE VRGRGLFIGI ELNVAAQDYC EQMINKGVLC
     KETQGNIIRI APPLVIDKDE IDEVIRVITE VLEK
//