ID   A0A0Q8LJC8_9MICO        Unreviewed;       407 AA.
AC   A0A0Q8LJC8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=ornithine aminotransferase {ECO:0000256|ARBA:ARBA00012924};
DE            EC=2.6.1.13 {ECO:0000256|ARBA:ARBA00012924};
DE   AltName: Full=Ornithine--oxo-acid aminotransferase {ECO:0000256|ARBA:ARBA00030587};
GN   Name=rocD {ECO:0000313|EMBL:KRB36699.1};
GN   ORFNames=ASD93_11690 {ECO:0000313|EMBL:KRB36699.1};
OS   Microbacterium sp. Root180.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1736483 {ECO:0000313|EMBL:KRB36699.1, ECO:0000313|Proteomes:UP000050802};
RN   [1] {ECO:0000313|EMBL:KRB36699.1, ECO:0000313|Proteomes:UP000050802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root180 {ECO:0000313|EMBL:KRB36699.1,
RC   ECO:0000313|Proteomes:UP000050802};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB36699.1, ECO:0000313|Proteomes:UP000050802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root180 {ECO:0000313|EMBL:KRB36699.1,
RC   ECO:0000313|Proteomes:UP000050802};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-ornithine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004998}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRB36699.1}.
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DR   EMBL; LMHS01000003; KRB36699.1; -; Genomic_DNA.
DR   RefSeq; WP_056122589.1; NZ_LMHS01000003.1.
DR   AlphaFoldDB; A0A0Q8LJC8; -.
DR   STRING; 1736483.ASD93_11690; -.
DR   OrthoDB; 9801052at2; -.
DR   UniPathway; UPA00098; UER00358.
DR   Proteomes; UP000050802; Unassembled WGS sequence.
DR   GO; GO:0004587; F:ornithine aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00610; OAT_like; 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   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR010164; Orn_aminotrans.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01885; Orn_aminotrans; 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; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:KRB36699.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050802};
KW   Transferase {ECO:0000313|EMBL:KRB36699.1}.
SQ   SEQUENCE   407 AA;  42671 MW;  1DCF65FA75ED7956 CRC64;
     MTTSPAVDTA MARIIADENE HVAHNYHPLP VVISRGEGAW VTDVEGKRYL DLLSAYSALN
     FGHGHPALLA AAQEQLNRLT LTSRAYHNDR LGPFAEALAE LCGKDLVLPM NTGAEAVETG
     IKVARAWGYR VKGIAPDAAT IVVANGNFHG RTTTIVGFSD DPQAREGFGP FTPGFVHVPF
     GDAAAIEAAI DENTAAVLIE PIQGEAGVVI PPEGYLRAVR ELCTKNGVLF IADEIQSGLG
     RVGATFACDR EGVVPDVYLL GKALGGGILP LSAVVADDDV LGVIRPGEHG STFGGNPLAA
     AVGLRVVEML KTGEFQTRAQ ALGEHLAAGL STLVGNGVTG VRVAGLWAGV DIDPAVGTGR
     EIAERLIARG VLVKDTHGHT IRIAPPLVVR ATELDWAVEQ LRVVLAR
//