ID   D7GED9_PROFC            Unreviewed;       404 AA.
AC   D7GED9;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   Name=got {ECO:0000313|EMBL:CBL56900.1};
GN   OrderedLocusNames=PFREUD_14000 {ECO:0000313|EMBL:CBL56900.1};
OS   Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM
OS   4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Propionibacterium.
OX   NCBI_TaxID=754252 {ECO:0000313|EMBL:CBL56900.1, ECO:0000313|Proteomes:UP000000936};
RN   [1] {ECO:0000313|EMBL:CBL56900.1, ECO:0000313|Proteomes:UP000000936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1
RC   {ECO:0000313|Proteomes:UP000000936};
RX   PubMed=20668525; DOI=10.1371/journal.pone.0011748;
RA   Falentin H., Deutsch S.M., Jan G., Loux V., Thierry A., Parayre S.,
RA   Maillard M.B., Dherbecourt J., Cousin F.J., Jardin J., Siguier P.,
RA   Couloux A., Barbe V., Vacherie B., Wincker P., Gibrat J.F., Gaillardin C.,
RA   Lortal S.;
RT   "The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a hardy
RT   actinobacterium with food and probiotic applications.";
RL   PLoS ONE 5:E11748-E11748(2010).
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; FN806773; CBL56900.1; -; Genomic_DNA.
DR   RefSeq; WP_013161268.1; NC_014215.1.
DR   AlphaFoldDB; D7GED9; -.
DR   STRING; 754252.PFREUD_14000; -.
DR   KEGG; pfr:PFREUD_14000; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_11; -.
DR   Proteomes; UP000000936; Chromosome.
DR   GO; GO:0004069; F:L-aspartate: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:CBL56900.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000936};
KW   Transferase {ECO:0000313|EMBL:CBL56900.1}.
FT   DOMAIN          34..394
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   404 AA;  44568 MW;  DE3CDE61DF9193FE CRC64;
     MTGFHQATRL QGVRYDVRGK NMVEAQAMEA RGEHILKLNI GNLAPFGFAT PDSVVRSVAT
     HLPESEGYSD ARGVPSARAA VAEYYQSKHL DVDPQQVLIG NGVSELISLT LSAILNHGDE
     VLVPAPDYPL WTAQITLCDG KAVHYLCDET RGWNPDPDDI AAHITARTKA IVLINPNNPT
     GAVYSADTVR AIVQLAREHD LIVLSDEIYE KIIYHGTHTY TAHETGDDVL CLTYSGLSKA
     YRACGFRAGW VVFTGSLQRA HNLLEGVDLL ANMRMCANVP AQYAIEACLS GYQSIDELTA
     PGGRFEEQLR LSHDLLDQIP GVNCVPAAGA LYLFPQLDPE RYPITDDEDW ALGLLREKKI
     LISHGRGFNW PNPDHFRLVA LPEDAVLREA LGRLAEYCEE TRRD
//