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   03-AUG-2022, entry version 115.
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=SSP0220;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., 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. {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; AP008934; BAE17365.1; -; Genomic_DNA.
DR   RefSeq; WP_011302212.1; NZ_MTGA01000037.1.
DR   AlphaFoldDB; Q4A0N2; -.
DR   SMR; Q4A0N2; -.
DR   STRING; 342451.SSP0220; -.
DR   EnsemblBacteria; BAE17365; BAE17365; SSP0220.
DR   KEGG; ssp:SSP0220; -.
DR   PATRIC; fig|342451.11.peg.225; -.
DR   eggNOG; COG4992; Bacteria.
DR   HOGENOM; CLU_016922_10_1_9; -.
DR   OMA; PFMVPTY; -.
DR   OrthoDB; 572533at2; -.
DR   UniPathway; UPA00098; UER00358.
DR   Proteomes; UP000006371; 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; Reference proteome; Transferase.
FT   CHAIN           1..394
FT                   /note="Ornithine aminotransferase 1"
FT                   /id="PRO_0000112796"
FT   MOD_RES         252
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01689"
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