ID   B1I8U7_STRPI            Unreviewed;       404 AA.
AC   B1I8U7;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=SPH_2136 {ECO:0000313|EMBL:ACA37148.1};
OS   Streptococcus pneumoniae (strain Hungary19A-6).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=487214 {ECO:0000313|EMBL:ACA37148.1, ECO:0000313|Proteomes:UP000002163};
RN   [1] {ECO:0000313|Proteomes:UP000002163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hungary19A-6 {ECO:0000313|Proteomes:UP000002163};
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT   closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(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; CP000936; ACA37148.1; -; Genomic_DNA.
DR   RefSeq; WP_000666465.1; NC_010380.1.
DR   AlphaFoldDB; B1I8U7; -.
DR   GeneID; 66807057; -.
DR   KEGG; spv:SPH_2136; -.
DR   HOGENOM; CLU_017584_4_2_9; -.
DR   Proteomes; UP000002163; 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:ACA37148.1};
KW   Transferase {ECO:0000313|EMBL:ACA37148.1}.
FT   DOMAIN          34..385
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   404 AA;  45776 MW;  6088F5C94EA033CC CRC64;
     MKEYNKSSKL EHVAYDIRGP VLEEAMRMRA NGEKILRLNT GNPAEFGFTA PDEVIHDLIM
     NARDSEGYSD SKGIFSARKA IMQYCQLKKF PNVDIDDIYL GNGVSELIVM SMQGLLDNGD
     EVLVPMPDYP LWTAAVSLAG GNAVHYICDE AVEWYPDIDD IKSKITSNTK AIVLINPNNP
     TGALYPKEFL LEIIEIARQN DLIIFADEIY DRMVMDGHVH TPVASLAPDV FCVSMNGLSK
     SHRIAGFRVG WMVLSGPKTH VKGYIEGLNM LSNMRLCSNV LAQQVVQTSL GGHQSVDELL
     LPGGRIYEQR NFIYNAIQDI PGLSAVKPKA GLYIFPKIDR NMYRIDDDEQ FVLDFLKQEK
     VLLVHGRGFN WQEPDHFRIV YLPRVDELAQ IQEKMTRFLK QYRR
//