ID   OAT_EXISA               Reviewed;         400 AA.
AC   C4L2E7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=EAT1b_2277;
OS   Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b).
OC   Bacteria; Firmicutes; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium;
OC   unclassified Exiguobacterium.
OX   NCBI_TaxID=360911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1283 / AT1b;
RX   PubMed=21460088; DOI=10.1128/jb.00303-11;
RA   Vishnivetskaya T.A., Lucas S., Copeland A., Lapidus A., Glavina del Rio T.,
RA   Dalin E., Tice H., Bruce D.C., Goodwin L.A., Pitluck S., Saunders E.,
RA   Brettin T., Detter C., Han C., Larimer F., Land M.L., Hauser L.J.,
RA   Kyrpides N.C., Ovchinnikova G., Kathariou S., Ramaley R.F., Rodrigues D.F.,
RA   Hendrix C., Richardson P., Tiedje J.M.;
RT   "Complete genome sequence of the Thermophilic Bacterium Exiguobacterium sp.
RT   AT1b.";
RL   J. Bacteriol. 193:2880-2881(2011).
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; CP001615; ACQ71199.1; -; Genomic_DNA.
DR   RefSeq; WP_015880758.1; NC_012673.1.
DR   AlphaFoldDB; C4L2E7; -.
DR   SMR; C4L2E7; -.
DR   STRING; 360911.EAT1b_2277; -.
DR   EnsemblBacteria; ACQ71199; ACQ71199; EAT1b_2277.
DR   KEGG; eat:EAT1b_2277; -.
DR   eggNOG; COG4992; Bacteria.
DR   HOGENOM; CLU_016922_10_3_9; -.
DR   OMA; DVFPRFA; -.
DR   OrthoDB; 572533at2; -.
DR   UniPathway; UPA00098; UER00358.
DR   Proteomes; UP000000716; 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; Reference proteome; Transferase.
FT   CHAIN           1..400
FT                   /note="Ornithine aminotransferase"
FT                   /id="PRO_1000215919"
FT   MOD_RES         254
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01689"
SQ   SEQUENCE   400 AA;  43690 MW;  B9134A2BC5C0DCF7 CRC64;
     MSKTHDVIEL TEKFGAHNYH PLPIVISEAK GIWVTDPEGN RYMDMLSAYS AVNQGHCHPK
     IIQALKDQAD KITLTSRAFY NDQLGRFYDK VVTLTKKQMV LPMNTGAEAV ETAVKTARRW
     AYDVKGIPGQ AEIIVCSGNF HGRTMAAVSM STEAEYQRGF GPLLPGFKVV PYGDIDAFEA
     AITENTAAFI VEPIQGEAGI IIPPAGYLKR ASELCKEHNV LFVADEIQSG LGRSGKWFAI
     EWEDVTPDMY ILGKALGGGV FPISCVAADQ EILSVFNPGS HGSTFGGNPL ASAVSVAALE
     VLEEENLPER SLELGTYFMD RLKSIDNPMI RDVRGRGLFI GIELTESARP YCEALKERGL
     LCKETHETVI RLAPPLVITK EELDQAFEAI EAVLAPAAIS