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Database: UniProt
Entry: A0A117I4D0_9MYCO
LinkDB: A0A117I4D0_9MYCO
Original site: A0A117I4D0_9MYCO 
ID   A0A117I4D0_9MYCO        Unreviewed;       419 AA.
AC   A0A117I4D0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Aminotransferase class III {ECO:0000313|EMBL:GAS86762.1};
GN   ORFNames=RMCB_0858 {ECO:0000313|EMBL:GAS86762.1};
OS   Mycolicibacterium brisbanense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=146020 {ECO:0000313|EMBL:GAS86762.1, ECO:0000313|Proteomes:UP000069620};
RN   [1] {ECO:0000313|EMBL:GAS86762.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM15654 {ECO:0000313|EMBL:GAS86762.1};
RA   Katahira K., Ogura Y., Gotoh Y., Hayashi T.;
RT   "Draft Genome Sequences of Five Rapidly Growing Mycobacterium Species, M.
RT   thermoresistibile, M. fortuitum subsp. acetamidolyticum, M. canariasense,
RT   M. brisbanense, and M. novocastrense.";
RL   Genome Announc. 4:e00322-16(2016).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       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:GAS86762.1}.
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DR   EMBL; BCSX01000011; GAS86762.1; -; Genomic_DNA.
DR   RefSeq; WP_062827784.1; NZ_JACKTM010000054.1.
DR   AlphaFoldDB; A0A117I4D0; -.
DR   STRING; 146020.RMCB_0858; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000069620; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, 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:GAS86762.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:GAS86762.1}.
SQ   SEQUENCE   419 AA;  44555 MW;  C25250DA7AC2CD17 CRC64;
     MDSNSYSGGL ATDPETESLI ADRIRMLGPA YRLFYERPVH LVRGQGSHLF DADGARYLDA
     YNNVVSVGHC HPRVVDAVTR QMQTLNTHTR YVHEGIVDYS RRLLATMPDD VDQVMYACTG
     SEANDLALRV AQMHTGARGV IVTSDAYHGN TEAVTAISPS LGGATVVGPH VRTVSAQTLD
     VAAAIKDLHD SGHGVSCLIV DTIFASDGIF PDPTVLAPAV EAVRAAGGVF IADEVQPGFG
     RTGEAMWGFA RHGVVPDLVT MGKPMANGLP VAAMAARSHV LETFARGVPY FNTFGGNPVS
     MAAAAAVLDV IEDENLIDNA ARVGTALRDE IARIGADHPR IGEVRGCGLY VGVEVVTPSR
     APDRTGAHDL VNAMRDRHVL ISVCGSDGNV LKVRPPLVFT MADVDWFCTE FEGALAELS
//
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