ID   OAT_BACC3               Reviewed;         396 AA.
AC   C1EL61;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Ornithine aminotransferase {ECO:0000255|HAMAP-Rule:MF_01689};
DE            Short=OAT {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 {ECO:0000255|HAMAP-Rule:MF_01689};
GN   Name=rocD {ECO:0000255|HAMAP-Rule:MF_01689}; OrderedLocusNames=BCA_1193;
OS   Bacillus cereus (strain 03BB102).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=572264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03BB102;
RA   Dodson R.J., Jackson P., Munk A.C., Brettin T., Bruce D., Detter C.,
RA   Tapia R., Han C., Sutton G., Sims D.;
RT   "Genome sequence of Bacillus cereus 03BB102.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001407; ACO27776.1; -; Genomic_DNA.
DR   RefSeq; WP_000616652.1; NZ_CP009318.1.
DR   AlphaFoldDB; C1EL61; -.
DR   SMR; C1EL61; -.
DR   EnsemblBacteria; ACO27776; ACO27776; BCA_1193.
DR   KEGG; bcx:BCA_1193; -.
DR   PATRIC; fig|572264.18.peg.1144; -.
DR   OMA; DVFPRFA; -.
DR   UniPathway; UPA00098; UER00358.
DR   Proteomes; UP000002210; 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: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; 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; 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..396
FT                   /note="Ornithine aminotransferase"
FT                   /id="PRO_1000187437"
FT   MOD_RES         255
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01689"
SQ   SEQUENCE   396 AA;  43300 MW;  9E2602631386FABC CRC64;
     MIQTKDIIEL TDTYGANNYH PLPIVISKAE GVWVEDPEGN RYMDLLSAYS AVNQGHRHPK
     IINALIDQAN RVTLTSRAFH SDQLGPWYEK VAKLTNKEMV LPMNTGAEAV ETAIKTARRW
     AYDVKKVEAN RAEIIVCEDN FHGRTMGAVS MSSNEEYKRG FGPMLPGIIV IPYGDLEALK
     AAITPNTAAF ILEPIQGEAG INIPPAGFLK EALEVCKKEN VLFVADEIQT GLGRTGKVFA
     CDWDNVTPDM YILGKALGGG VFPISCVAAN RDILGVFEPG SHGSTFGGNP LACAVSIAAL
     EVLEEEKLTE RSLQLGEKLV GQLKEIDNPM ITEVRGKGLF IGIELNEPAR PYCEQLKAAG
     LLCKETHENV IRIAPPLVIS EEDLEWAFQK IKAVLS