ID A0A0M8MPL0_9MICO Unreviewed; 407 AA.
AC A0A0M8MPL0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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:KOS11744.1};
GN ORFNames=XI38_04195 {ECO:0000313|EMBL:KOS11744.1};
OS Microbacterium chocolatum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=84292 {ECO:0000313|EMBL:KOS11744.1, ECO:0000313|Proteomes:UP000037737};
RN [1] {ECO:0000313|EMBL:KOS11744.1, ECO:0000313|Proteomes:UP000037737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SIT 101 {ECO:0000313|EMBL:KOS11744.1,
RC ECO:0000313|Proteomes:UP000037737};
RA Li X., Xu Y.;
RT "Complete genome sequence of Microbacterium chocolatum SIT 101, a bacterium
RT enantioselectively hydrolyzing mesomeric diesters.";
RL Submitted (APR-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:KOS11744.1}.
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DR EMBL; LAVO01000003; KOS11744.1; -; Genomic_DNA.
DR RefSeq; WP_053547051.1; NZ_KQ440285.1.
DR AlphaFoldDB; A0A0M8MPL0; -.
DR KEGG; mcw:A8L33_02010; -.
DR PATRIC; fig|84292.3.peg.871; -.
DR OrthoDB; 9801052at2; -.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000037737; 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:KOS11744.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000037737};
KW Transferase {ECO:0000313|EMBL:KOS11744.1}.
SQ SEQUENCE 407 AA; 42453 MW; 68833A36396E5037 CRC64;
MSLPSAGEAS SAALIAAEDA HVAHNYHPLP VVVARGEGAW VTDIEGKRYL DLLAAYSAVN
FGHCHPAIVA AAQEQLARVT LTSRAFHNDR LGTFATALAD LCGKDMVLPM NTGAEAVETG
IKVARAWGYR VKGIPADRAT VIVASDNFHG RTTTIVGFSD DPQARDDFGP YAPGFVTVPF
GDAAALEAAI DATTAAVLLE PIQGEAGVII PPEGYLRAVR EITARRGVLM IADEIQSGLG
RVGTTFACQR EDVVPDVYLL GKALGGGILP VSAVVADRDV LGVIRPGEHG STFGGNPLAA
AVGTRVVEML ATGEFQTRAA ALGEHLEAKL GELVGSGVTG IRVAGLWAGV DIDPARGTGR
EVAERLLGRG VLVKDTHGQT IRIAPPLVIR ATELDWAVEQ LRHVLAG
//
