ID   E8NBM5_MICTS            Unreviewed;       408 AA.
AC   E8NBM5;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   Name=aspC {ECO:0000313|EMBL:BAJ73485.1};
GN   OrderedLocusNames=MTES_0521 {ECO:0000313|EMBL:BAJ73485.1};
OS   Microbacterium testaceum (strain StLB037).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=979556 {ECO:0000313|EMBL:BAJ73485.1, ECO:0000313|Proteomes:UP000008975};
RN   [1] {ECO:0000313|EMBL:BAJ73485.1, ECO:0000313|Proteomes:UP000008975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StLB037 {ECO:0000313|EMBL:BAJ73485.1,
RC   ECO:0000313|Proteomes:UP000008975};
RX   PubMed=21357489; DOI=10.1128/JB.00180-11;
RA   Morohoshi T., Wang W.-Z., Someya N., Ikeda T.;
RT   "Genome sequence of Microbacterium testaceum StLB037, an N-acylhomoserine
RT   lactone-degrading bacterium isolated from potato leaves.";
RL   J. Bacteriol. 193:2072-2073(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=StLB037;
RA   Morohoshi T., Wang W.Z., Someya N., Ikeda T.;
RT   "Genome sequence of Microbacterium testaceum StLB037.";
RL   Submitted (FEB-2011) 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}.
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DR   EMBL; AP012052; BAJ73485.1; -; Genomic_DNA.
DR   RefSeq; WP_013583612.1; NC_015125.1.
DR   AlphaFoldDB; E8NBM5; -.
DR   STRING; 979556.MTES_0521; -.
DR   KEGG; mts:MTES_0521; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_11; -.
DR   OrthoDB; 9763453at2; -.
DR   Proteomes; UP000008975; Chromosome.
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:BAJ73485.1};
KW   Transferase {ECO:0000313|EMBL:BAJ73485.1}.
FT   DOMAIN          38..387
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   408 AA;  44709 MW;  BBB883DF96FEE623 CRC64;
     MSPLRPLDQS SKLKDVLYEI RGEALVEADR LEAEGHAILK LNTGNPAIFG FEAPHQIVRD
     MIAAVPNAHG YSDSRGVLSA RRAVVSRYEE EPGFPHLDPD DVYLGNGVSE LITMTMQALL
     DEGDEVLIPA PDYPLWTAMT SLGGGTPVHY LCDESREWQP DLEDIRSKVT PRTKAIVVIN
     PNNPTGAVYS REVLEGIADI AREHSLLVLA DEIYDRILFD DAVHIPMATV APDLLVLTFN
     GLSKTYRVAG YRSGWLAITG PKSHAEGFLH GINLLASTRL CPNVPAQFAV QAALSGVQSI
     DALIAPSGRL HEQRDAAWQG LEAIPGVSCV MPRGALYAFP RFDPDVYEIP DDAKFVRDFL
     VAEHVLLVQG SGFNWPATDH VRIVTLPEAR VISDAIERLG NFLASWRP
//