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Database: UniProt
Entry: A0A1I6IUA3_9MICO
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Original site: A0A1I6IUA3_9MICO 
ID   A0A1I6IUA3_9MICO        Unreviewed;       470 AA.
AC   A0A1I6IUA3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Taurine---2-oxoglutarate transaminase {ECO:0000313|EMBL:SFR69800.1};
GN   ORFNames=SAMN05428970_0792 {ECO:0000313|EMBL:SFR69800.1};
OS   Agromyces sp. CF514.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Agromyces.
OX   NCBI_TaxID=1881031 {ECO:0000313|EMBL:SFR69800.1, ECO:0000313|Proteomes:UP000199174};
RN   [1] {ECO:0000313|EMBL:SFR69800.1, ECO:0000313|Proteomes:UP000199174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF514 {ECO:0000313|EMBL:SFR69800.1,
RC   ECO:0000313|Proteomes:UP000199174};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; FOZD01000001; SFR69800.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6IUA3; -.
DR   STRING; 1881031.SAMN05428970_0792; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000199174; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
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; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}.
SQ   SEQUENCE   470 AA;  50225 MW;  0592A98F375D3B65 CRC64;
     MTDTLSPETT AVFTDRHGAV HALPAPAAEA QVRADDRGHV FHSWSAQALI DPLPIAAGEG
     STFWDYQGNA YLDFSSQLVN LNLGHQHPDL VAAIQQQAGR LATIQPSMAN DVRGELARRI
     AEVAPGDLDK VFFTNGGADA NEYAVRMARA VTGRRKVLSM YRSYHGGTAT AISLTGDPRR
     WANEPSDGSV AHFMGPYAYR SSFHADSPEQ EAERALAHLE QVIALEGPNT IAAVILETIV
     GTNGVLVPPP GYLEGVRALA DKYGIVYIAD EVMVGFGRVG EWFAVNHFGV VPDLITFAKG
     VNSGYAPLGG VVISQKIASH FDTVAFAGGL TYSGHPLACA PGVATFEVFE RDGILERVRD
     LGERVVGPRL REIAAKHPSV GEVRGLGLFW AIELVKDPET REPLVPFNAG GADAAPMGAV
     AAACKQAGLW PFVHFNRLHV APPLVITEEE LVRGLDILDE ALTVADSYVA
//
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