ID   A0A199AUI0_9ACTN        Unreviewed;       417 AA.
AC   A0A199AUI0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=AYO52_06890 {ECO:0000313|EMBL:OAV76697.1};
OS   Dietzia sp. 111N12-1.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC   Dietzia.
OX   NCBI_TaxID=1785156 {ECO:0000313|EMBL:OAV76697.1, ECO:0000313|Proteomes:UP000092558};
RN   [1] {ECO:0000313|EMBL:OAV76697.1, ECO:0000313|Proteomes:UP000092558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=111N12-1 {ECO:0000313|EMBL:OAV76697.1,
RC   ECO:0000313|Proteomes:UP000092558};
RA   Yu M.;
RT   "Draft genome sequence of Dietzia sp.111N12-1 isolated from South China Sea
RT   with petroleum hydrocarbons degradation activity.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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:OAV76697.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LSSV01000082; OAV76697.1; -; Genomic_DNA.
DR   RefSeq; WP_067719484.1; NZ_LSSV01000082.1.
DR   AlphaFoldDB; A0A199AUI0; -.
DR   STRING; 1785156.AYO52_06890; -.
DR   GeneID; 84688321; -.
DR   Proteomes; UP000092558; 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:InterPro.
DR   CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43488; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR   PANTHER; PTHR43488:SF2; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:OAV76697.1};
KW   Transferase {ECO:0000313|EMBL:OAV76697.1}.
FT   DOMAIN          47..407
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   417 AA;  46059 MW;  E2E0AD79B2ECA553 CRC64;
     MTPETTGRTL HQLRTLDQSS KLKDVLYEIR GPVLARANQL EAEGHRILKL NIGNPAPFGF
     EAPDVIMRDM IAALPHAQGY SESKGILSAR RAIFTRYELV PDFPRLSVDD IYLGNGVSEL
     ITMTMQALLD DGDEVLIPAP DYPLWTAMTS LAGGRPVHYL ADEQDDWNPS LEDIASKITP
     RTKAIVVINP NNPTGAVYSR EVLQGIVDLA REHSLLILAD EIYDRIVYDE AEHTSIATLA
     HDLLVLTFNG LSKTYRVAGY RAGWLAITGP KAHAAGFLEG LELLASTRLC PNVPAQHAIQ
     VALGGYQSIN ELIEPGGRLH EQRGIAWEKL NTIPGVSCVK PMGALYAFPK LDPNVHEIHD
     DRLFALDLLE QERILVTQGT GFNWPDPDHF RVVTLPASRD LGVAIERIGN FLASYRQ
//