ID A0A0M2H5P2_9MICO Unreviewed; 408 AA.
AC A0A0M2H5P2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:KJL41810.1};
GN ORFNames=RS82_02426 {ECO:0000313|EMBL:KJL41810.1};
OS Microbacterium trichothecenolyticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=69370 {ECO:0000313|EMBL:KJL41810.1, ECO:0000313|Proteomes:UP000034098};
RN [1] {ECO:0000313|EMBL:KJL41810.1, ECO:0000313|Proteomes:UP000034098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8608 {ECO:0000313|EMBL:KJL41810.1,
RC ECO:0000313|Proteomes:UP000034098};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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:KJL41810.1}.
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DR EMBL; JYJA01000036; KJL41810.1; -; Genomic_DNA.
DR RefSeq; WP_045299729.1; NZ_JYJA01000036.1.
DR AlphaFoldDB; A0A0M2H5P2; -.
DR PATRIC; fig|69370.6.peg.2471; -.
DR OrthoDB; 9801052at2; -.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000034098; 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:KJL41810.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000034098};
KW Transferase {ECO:0000313|EMBL:KJL41810.1}.
SQ SEQUENCE 408 AA; 42943 MW; 6C4C1A24BAD940DF CRC64;
MTAASTSLDA AMSQIIAAEE QHVAHNYHPL PVVISRGEGA WVTDVEGKRY LDLLSAYSAL
NFGHGHPAIV AAAQEQLNRL TLTSRAYHND RLGPFAAALA ELCGKDLVLP MNTGAEAVET
GIKVARAWGY RVKGVAADAA KIVVAHGNFH GRTTTIVGFS DDPQARADFG PFTPGFVSVP
FGDAAVIDAA ITADTVAVLI EPIQGEAGVI LPPEGYLKKV REICTRRGVL FIADEIQSGL
GRVGETFACD REGVVPDIYL LGKALGGGIL PLSAVVADRD VLGVIHPGEH GSTFGGNPLA
AAVGLRVVEM LQTGEFQGRA KLLGDHLEAK LQELVGHGVT AVRVAGLWAG IDIDPEVGTG
REIAERLIGR GVLAKDTHGQ TIRIAPPLVV RATELDWAVE QLRFVLAA
//
