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   03-AUG-2022, entry version 109.
DE   RecName: Full=Ornithine aminotransferase 1 {ECO:0000255|HAMAP-Rule:MF_01689};
DE            Short=OAT 1 {ECO:0000255|HAMAP-Rule:MF_01689};
DE            EC=2.6.1.13 {ECO:0000255|HAMAP-Rule:MF_01689};
DE   AltName: Full=Ornithine--oxo-acid aminotransferase 1 {ECO:0000255|HAMAP-Rule:MF_01689};
GN   Name=rocD1 {ECO:0000255|HAMAP-Rule:MF_01689}; OrderedLocusNames=SAR0186;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
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., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   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. {ECO:0000255|HAMAP-Rule:MF_01689}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-oxocarboxylate + L-ornithine = an L-alpha-amino acid + L-
CC         glutamate 5-semialdehyde; Xref=Rhea:RHEA:13877, ChEBI:CHEBI:35179,
CC         ChEBI:CHEBI:46911, ChEBI:CHEBI:58066, ChEBI:CHEBI:59869; EC=2.6.1.13;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01689};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01689};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-ornithine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01689}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01689}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. OAT subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01689}.
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DR   EMBL; BX571856; CAG39213.1; -; Genomic_DNA.
DR   RefSeq; WP_001084444.1; NC_002952.2.
DR   AlphaFoldDB; Q6GKC1; -.
DR   SMR; Q6GKC1; -.
DR   KEGG; sar:SAR0186; -.
DR   HOGENOM; CLU_016922_10_1_9; -.
DR   OMA; PFMVPTY; -.
DR   OrthoDB; 572533at2; -.
DR   UniPathway; UPA00098; UER00358.
DR   Proteomes; UP000000596; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050155; F:ornithine(lysine) transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004587; F:ornithine-oxo-acid transaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProt.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01689; Ornith_aminotrans_3; 1.
DR   InterPro; IPR004636; AcOrn/SuccOrn_fam.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR010164; Orn_aminotrans.
DR   InterPro; IPR034757; Ornith_aminotrans_bact.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11986:SF18; PTHR11986:SF18; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; SSF53383; 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; Cytoplasm; Proline biosynthesis;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN           1..394
FT                   /note="Ornithine aminotransferase 1"
FT                   /id="PRO_0000112786"
FT   MOD_RES         252
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01689"
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