ID   OAT_BRADU               Reviewed;         404 AA.
AC   Q89RB7;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 111.
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=bll2855;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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; BA000040; BAC48120.1; -; Genomic_DNA.
DR   RefSeq; NP_769495.1; NC_004463.1.
DR   RefSeq; WP_011085639.1; NC_004463.1.
DR   AlphaFoldDB; Q89RB7; -.
DR   SMR; Q89RB7; -.
DR   STRING; 224911.27351112; -.
DR   EnsemblBacteria; BAC48120; BAC48120; BAC48120.
DR   KEGG; bja:bll2855; -.
DR   PATRIC; fig|224911.5.peg.2836; -.
DR   eggNOG; COG4992; Bacteria.
DR   HOGENOM; CLU_016922_10_3_5; -.
DR   InParanoid; Q89RB7; -.
DR   OMA; GHYWSGI; -.
DR   PhylomeDB; Q89RB7; -.
DR   UniPathway; UPA00098; UER00358.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
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; IBA:GO_Central.
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; Reference proteome; Transferase.
FT   CHAIN           1..404
FT                   /note="Ornithine aminotransferase"
FT                   /id="PRO_0000112731"
FT   MOD_RES         256
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01689"
SQ   SEQUENCE   404 AA;  43444 MW;  DB38F11F8FA021D8 CRC64;
     MSSSVIDYLA TETRLGAHNY EPIGVVLSRG EGVWVWDTDG NRYLDCLSAY SAVSQGHCHP
     KILAAMVEQA HRLTLTSRAF HNDQLAPFYE EIAALTGSHK VLPMNSGAEA VESAIKSVRK
     WGYEVKGVPD DQAEIIVCAD NFHGRTLGIV GFSTDPETRG HFGPFAPGFR IIPFGDAAAL
     EQAITPNTVA FLVEPIQGEA GVIIPPAGYF TKVRELCTAN NVMLVLDEIQ TGLGRTGKLL
     AEQHEGIEAD VTLLGKALAG GFYPVSAVLS NNEVLGTLRP GQHGSTFGGN PLACAVARAA
     MRVLVEEGMI ENAARQGARL LEGLKDIRAN TVREVRGRGL MLAVELHPEA GRARRYCEAL
     QGKGILAKDT HGHTIRIAPP LVITSDEVDW ALEQFATTLT QDFS