ID   I3U1B3_ENTFD            Unreviewed;       406 AA.
AC   I3U1B3;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   Name=aspC2 {ECO:0000313|EMBL:AFK58801.1};
GN   ORFNames=HMPREF0351_11177 {ECO:0000313|EMBL:AFK58801.1};
OS   Enterococcus faecium (strain ATCC BAA-472 / TX0016 / DO).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=333849 {ECO:0000313|EMBL:AFK58801.1, ECO:0000313|Proteomes:UP000005269};
RN   [1] {ECO:0000313|EMBL:AFK58801.1, ECO:0000313|Proteomes:UP000005269}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-472 / TX0016 / DO {ECO:0000313|Proteomes:UP000005269};
RX   PubMed=22769602; DOI=10.1186/1471-2180-12-135;
RA   Qin X., Galloway-Pena J.R., Sillanpaa J., Hyeob Roh J., Nallapareddy S.R.,
RA   Chowdhury S., Bourgogne A., Choudhury T., Munzy D.M., Buhay C.J., Ding Y.,
RA   Dugan-Rocha S., Liu W., Kovar C., Sodergren E., Highlander S.,
RA   Petrosino J.F., Worley K.C., Gibbs R.A., Weinstock G.M., Murray B.E.;
RT   "Complete genome sequence of Enterococcus faecium strain TX16 and
RT   comparative genomic analysis of Enterococcus faecium genomes.";
RL   BMC Microbiol. 12:135-135(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; CP003583; AFK58801.1; -; Genomic_DNA.
DR   RefSeq; YP_006375783.1; NC_017960.1.
DR   AlphaFoldDB; I3U1B3; -.
DR   KEGG; efu:HMPREF0351_11177; -.
DR   HOGENOM; CLU_017584_4_2_9; -.
DR   Proteomes; UP000005269; 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:0009042; F:valine-pyruvate transaminase activity; IEA:UniProtKB-EC.
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:AFK58801.1};
KW   Transferase {ECO:0000313|EMBL:AFK58801.1}.
FT   DOMAIN          36..388
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   406 AA;  45937 MW;  ECE2A4741060CDA7 CRC64;
     MMREFEKSNK LEGVSYDVRG PVLEEAERMQ EEGISILKLN TGNPAPFGFE APNEVIRDLI
     MNARDSEGYS DSKGIFSARK AIEQYCQLKH FPNVTINDIY TGNGVSELIT MCMQGLLDNG
     DEVLVPMPDY PLWTASIALA GGIPVHYICD EEAEWYPDID DIKSKITSRT KAIVIINPNN
     PTGALYPKEL LEEIVEVARQ NNLIIYSDEI YDRLVMDGLE HIPIATLAPD LFVVTLNGLS
     KSHRVAGFRV GWMVLSGDKS HVKGYIEGLN MLSSMRLCSN VLSQQIIQTA LGGYQSVDEL
     LLPGGRIYEQ REYIYNAIND IPGLSAVKPK AAFYIFPKID TKRFNILDDE KFVLDFLHEH
     HILLVHGGGF NWNQPDHFRI VYLPKMDDLK QTAKKMREFL ATYRQK
//