ID   OAT1_STAAM              Reviewed;         394 AA.
AC   P60295; Q99X36;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 1.
DT   02-SEP-2026, entry version 135.
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};
GN   OrderedLocusNames=SAV0185;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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 = L-glutamate 5-semialdehyde
CC         + an L-alpha-amino acid; 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; BA000017; BAB56347.1; -; Genomic_DNA.
DR   RefSeq; WP_001084442.1; NC_002758.2.
DR   AlphaFoldDB; P60295; -.
DR   SMR; P60295; -.
DR   KEGG; sav:SAV0185; -.
DR   HOGENOM; CLU_016922_10_1_9; -.
DR   PhylomeDB; P60295; -.
DR   UniPathway; UPA00098; UER00358.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IEA:TreeGrafter.
DR   GO; GO:0004587; F:L-ornithine transaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006526; P:L-arginine biosynthetic process; IEA:UniProtKB-ARBA.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00610; OAT_like; 1.
DR   FunFam; 3.40.640.10:FF:000011; Ornithine aminotransferase; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_01689; Ornith_aminotrans_3; 1.
DR   InterPro; IPR004636; AcOrn/SuccOrn_fam.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR050103; Class-III_PLP-dep_AT.
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   NCBIfam; TIGR00707; argD; 1.
DR   NCBIfam; TIGR01885; Orn_aminotrans; 1.
DR   NCBIfam; NF002325; PRK01278.1; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF18; ORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 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_0000112782"
FT   MOD_RES         252
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01689"
SQ   SEQUENCE   394 AA;  43057 MW;  D74BFF1F623D9396 CRC64;
     MNSIIELTDY YSSNNYAPLK LVISKGKGVK VWDTDGKQYI DCISGFSVAN QGHCHPTIVK
     AMTEQASKLS IISRVLYSDN LGKWEEKICH LAKKDKVLSL NSGTEAVEAA IKIARKWGSE
     VKGITDGQVE IIAMNNNFHG RTLGSLSLSN HDAYKAGFHP LLQGTTTVDF GDIEQLTQAI
     SPNTAAIILE PIQGEGGVNI PPKGYIQAVR QLCDKHQILM IADEIQVGLG RTGKWFAMEW
     EQVVPDIYIL GKALGGGLYP VSAVLANNDV MRVLTPGTHG STFGGNPLAI AISTAALDVL
     KDEQLVERSE RLGSFLLKAL LQLKHPSIKE IRGRGLFIGI ELNTDAAPFV DQLIQRGILC
     KDTHRTIIRL SPPLVIDKEE IHQIVAAFQD VFKN
//