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Database: UniProt
Entry: A0A1B6ARE6_9ACTN
LinkDB: A0A1B6ARE6_9ACTN
Original site: A0A1B6ARE6_9ACTN 
ID   A0A1B6ARE6_9ACTN        Unreviewed;       454 AA.
AC   A0A1B6ARE6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Putative taurine--pyruvate aminotransferase {ECO:0000313|EMBL:GAU70080.1};
GN   Name=tpa {ECO:0000313|EMBL:GAU70080.1};
GN   ORFNames=SSP35_16_00760 {ECO:0000313|EMBL:GAU70080.1};
OS   Streptomyces sp. NBRC 110611.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1621259 {ECO:0000313|EMBL:GAU70080.1, ECO:0000313|Proteomes:UP000094479};
RN   [1] {ECO:0000313|EMBL:GAU70080.1, ECO:0000313|Proteomes:UP000094479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 110611 {ECO:0000313|EMBL:GAU70080.1,
RC   ECO:0000313|Proteomes:UP000094479};
RA   Igarashi Y., Komaki H., Ichikawa N., Hosoyama A., Fujita N., Panbangred W.;
RT   "Whole genome shotgun sequence of Streptomyces sp. NBRC 110611.";
RL   Submitted (MAR-2015) 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}.
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:GAU70080.1}.
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DR   EMBL; BBUY01000016; GAU70080.1; -; Genomic_DNA.
DR   RefSeq; WP_066936998.1; NZ_BBUY01000016.1.
DR   AlphaFoldDB; A0A1B6ARE6; -.
DR   STRING; 1621259.GCA_001590865_05405; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000094479; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
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   Aminotransferase {ECO:0000313|EMBL:GAU70080.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Pyruvate {ECO:0000313|EMBL:GAU70080.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094479};
KW   Transferase {ECO:0000313|EMBL:GAU70080.1}.
SQ   SEQUENCE   454 AA;  50100 MW;  CEB225A800BF3C1D CRC64;
     MSERDLSATA YDHLWMHFTR MSSYENAPVP TIVRGEGTHI FDDKGKRYID GLAGLFVVNA
     GHGRVELAET AFKQAQELAF FPVWSYAHPR AVELAERLAH HAPGDLNKVF FTTGGGEAVE
     TAWKLAKQYF KLTGKPTKHK VISRAVAYHG TPQGALSITG LPALKAPFEP LVPGAHKVPN
     TNIYRAPIHG DDPEAFGRWA ADQIEQQILF EGPETVAAVF LEPVQNAGGC FPPPPGYFQR
     VREICDRYDV LLVSDEVICA FGRLGTMFAC DKFGYVPDMI TCAKGMTSGY SPIGACIVSD
     RLAEPFYRGD NTFLHGYTFG GHPVSAAVGL ANLDIFEREG LNQHVLDNEG NFLSTLQKLH
     DLPIVGDVRG NGFFYGIELV KDKATKESFN EEETERVLYG FLSQALFDNG LYCRADDRGD
     PVVQLAPPLI ADQPVFDEIE QILRTVLTEA WAKL
//
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