ID   F5X364_STRPX            Unreviewed;       404 AA.
AC   F5X364;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=SGPB_1707 {ECO:0000313|EMBL:BAK30723.1};
OS   Streptococcus pasteurianus (strain ATCC 43144 / JCM 5346 / CDC 1723-81).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=981540 {ECO:0000313|EMBL:BAK30723.1, ECO:0000313|Proteomes:UP000007946};
RN   [1] {ECO:0000313|EMBL:BAK30723.1, ECO:0000313|Proteomes:UP000007946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43144 / JCM 5346 / CDC 1723-81
RC   {ECO:0000313|Proteomes:UP000007946};
RX   PubMed=21633709; DOI=10.1371/journal.pone.0020519;
RA   Lin I.-H., Liu T.-T., Teng Y.-T., Wu H.-L., Liu Y.-M., Wu K.-M.,
RA   Chang C.-H., Hsu M.-T.;
RT   "Sequencing and comparative genome analysis of two pathogenic Streptococcus
RT   gallolyticus subspecies: genome plasticity, adaptation and virulence.";
RL   PLoS ONE 6:E20519-E20519(2011).
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; AP012054; BAK30723.1; -; Genomic_DNA.
DR   RefSeq; WP_003066271.1; NC_015600.1.
DR   AlphaFoldDB; F5X364; -.
DR   STRING; 981540.SGPB_1707; -.
DR   GeneID; 76468358; -.
DR   KEGG; stb:SGPB_1707; -.
DR   HOGENOM; CLU_017584_4_2_9; -.
DR   Proteomes; UP000007946; 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:BAK30723.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007946};
KW   Transferase {ECO:0000313|EMBL:BAK30723.1}.
FT   DOMAIN          34..388
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   404 AA;  45352 MW;  26DDD9F275896B07 CRC64;
     MKIFDKSSKL EHVSYDIRGP ILDEATRMIA NGEKILRLNT GNPAEFGFTA PDEVIRDLIA
     NARNSEAYSD SKGIFSARKA IMQYCQLKGF PHVDIDDIYL GNGVSELISI SLQALLDDGD
     EVLVPMPDYP LWTACVSLAG GNAVHYLCDE KANWYPDIDD IKSKITSNTK AIVVINPNNP
     TGALYPDELL KEIVEIARQN DLIIFADEIY DRLVMDGKKH TAIASLAPDV FCVSMNGLSK
     SHRICGFRVG WMVLSGPKNN VKGYIEGLNM LANMRLCANV LGQHVVQTSL GGYQSVDELL
     IPGGRIYEQR NFIYKAVNEV PGLSAVKPDA GLYIFPKIDR DMYQIDDDEQ FCLELLKQEK
     VMLVPGKGFN WNEPDHFRIV YLPRVEELAE VQEKLTRVLN QYRR
//