ID   I6S404_ENTHA            Unreviewed;       405 AA.
AC   I6S404;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=EHR_13125 {ECO:0000313|EMBL:AFM71485.1};
OS   Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 /
OS   NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=768486 {ECO:0000313|EMBL:AFM71485.1, ECO:0000313|Proteomes:UP000002895};
RN   [1] {ECO:0000313|EMBL:AFM71485.1, ECO:0000313|Proteomes:UP000002895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB
RC   6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R
RC   {ECO:0000313|Proteomes:UP000002895};
RX   PubMed=22933757; DOI=10.1128/JB.01075-12;
RA   Gaechter T., Wunderlin C., Schmidheini T., Solioz M.;
RT   "Genome sequence of Enterococcus hirae (Streptococcus faecalis) ATCC 9790,
RT   a model organism for the study of ion transport, bioenergetics, and copper
RT   homeostasis.";
RL   J. Bacteriol. 194:5126-5127(2012).
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; CP003504; AFM71485.1; -; Genomic_DNA.
DR   RefSeq; WP_010737412.1; NZ_KB946231.1.
DR   AlphaFoldDB; I6S404; -.
DR   KEGG; ehr:EHR_13125; -.
DR   PATRIC; fig|768486.10.peg.1078; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_9; -.
DR   OrthoDB; 9802328at2; -.
DR   Proteomes; UP000002895; 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:AFM71485.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002895};
KW   Transferase {ECO:0000313|EMBL:AFM71485.1}.
FT   DOMAIN          35..387
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   405 AA;  45865 MW;  B39E8934135B6ADC CRC64;
     MREFEKSNKL EGVSYDVRGP VLEEAERMQE EGISILKLNT GNPAPFGFEA PNEVIRDLIM
     NARDSEGYSD SKGIFSARKA IEQYCQIKKF PNVTINDIYT GNGVSELITM CMQGLLDNGD
     EVLVPMPDYP LWTASVSLAG GKPVHYICDE QAEWYPDIDD IKSKITSRTK AIVIINPNNP
     TGALYPKEIL EQIVEIARQN QLIIYSDEIY DRLVMDGLEH IPIATLAPDL FVVTLNGLSK
     SHRVAGFRVG WMVLSGDKSH VKGYIEGLNM LSSMRLCSNV LSQQIIQTAL GGYQSVDELL
     LPDGRIYEQR EFIYNAINDI PGLSAVKPKA AFYIFPKIDT KRFNILDDEK FVLDFLHEHH
     ILLVHGGGFN WHQPDHFRIV YLPKMDDLKT TAVKMREFLS TYRQK
//