ID   A0A0G3UEA8_9ACTN        Unreviewed;       404 AA.
AC   A0A0G3UEA8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=M444_00405 {ECO:0000313|EMBL:AKL64173.1};
OS   Streptomyces sp. Mg1.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=465541 {ECO:0000313|EMBL:AKL64173.1, ECO:0000313|Proteomes:UP000035653};
RN   [1] {ECO:0000313|EMBL:AKL64173.1, ECO:0000313|Proteomes:UP000035653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mg1 {ECO:0000313|EMBL:AKL64173.1,
RC   ECO:0000313|Proteomes:UP000035653};
RX   PubMed=23908282;
RA   Hoefler B.C., Konganti K., Straight P.D.;
RT   "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using PacBio
RT   Single-Molecule Sequencing.";
RL   Genome Announc. 1:e00535-13(2013).
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}.
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DR   EMBL; CP011664; AKL64173.1; -; Genomic_DNA.
DR   RefSeq; WP_037796816.1; NZ_CP011664.1.
DR   AlphaFoldDB; A0A0G3UEA8; -.
DR   KEGG; strm:M444_00405; -.
DR   PATRIC; fig|465541.12.peg.114; -.
DR   OrthoDB; 9763453at2; -.
DR   Proteomes; UP000035653; Chromosome.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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:AKL64173.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035653};
KW   Transferase {ECO:0000313|EMBL:AKL64173.1}.
FT   DOMAIN          35..394
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   404 AA;  44040 MW;  C2BF251D8CD5A1FA CRC64;
     MQVNQSSKLA GVCYDIRGPV LEEATRLENE GHRILKLHTG NPAAFGFEAP TEILREITGN
     LAGAHGYGDA KGLPAARRAI TDYYLQRGVT GLTAEDIYLG NGASELIQMS MQALLDNGDE
     VLIPAPDYPL WTASVSLAGG TAVHYRCDEQ AGWFPDLADV EAKITPRTRA LVLINPNNPT
     GAVYSTALLH GLMEIARRHQ LIVCSDEIYD KILYDGLAHT CTASLAPDLL CLTFNGLSKA
     YRVAGYRSGW MAVSGPKAHA TSYIEGLNIL ANMRLCASMP AQYAINAALG GPQSINDLLL
     PDGRLTQQRD TAWKLLNDIP GVSCVKPQGA LYAFPRLDPK VYKINDDARL VLDLLRAQRL
     LIVQGTGFNW PDPDHFRLVT LPRTEELTDA VTRIATFLDG YSQH
//