ID   D3H6R9_STRM6            Unreviewed;       404 AA.
AC   D3H6R9;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
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:CBJ21561.1};
GN   OrderedLocusNames=smi_0289 {ECO:0000313|EMBL:CBJ21561.1};
OS   Streptococcus mitis (strain B6).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=365659 {ECO:0000313|EMBL:CBJ21561.1, ECO:0000313|Proteomes:UP000008563};
RN   [1] {ECO:0000313|EMBL:CBJ21561.1, ECO:0000313|Proteomes:UP000008563}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B6 {ECO:0000313|EMBL:CBJ21561.1,
RC   ECO:0000313|Proteomes:UP000008563};
RX   PubMed=20195536; DOI=10.1371/journal.pone.0009426;
RA   Denapaite D., Brueckner R., Nuhn M., Reichmann P., Henrich B., Maurer P.,
RA   Schaehle Y., Selbmann P., Zimmermann W., Wambutt R., Hakenbeck R.;
RT   "The genome of Streptococcus mitis B6--what is a commensal?";
RL   PLoS ONE 5:E9426-E9426(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; FN568063; CBJ21561.1; -; Genomic_DNA.
DR   RefSeq; WP_000666463.1; NC_013853.1.
DR   RefSeq; YP_003445429.1; NC_013853.1.
DR   AlphaFoldDB; D3H6R9; -.
DR   STRING; 365659.smi_0289; -.
DR   KEGG; smb:smi_0289; -.
DR   PATRIC; fig|365659.3.peg.284; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_9; -.
DR   OrthoDB; 9802328at2; -.
DR   Proteomes; UP000008563; 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:CBJ21561.1};
KW   Transferase {ECO:0000313|EMBL:CBJ21561.1}.
FT   DOMAIN          34..385
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   404 AA;  45746 MW;  657D4E8CBE65BD90 CRC64;
     MKEYNKSSKL EHVAYDIRGP VLEEAMRMRA NGEKILRLNT GNPAEFGFTA PDEVIHDLIM
     NARDSEGYSD SKGIFSARKA IMQYCQLKKF PNVDIDDIYL GNGVSELIVM SMQGLLDNGD
     EVLVPMPDYP LWTAAVSLAG GNAVHYICDE AAEWYPDIDD IKSKITSNTK AIVLINPNNP
     TGALYPKELL LEIIEIARQN DLIIFADEIY DRMVMDGHVH TPVASLAPDV FCVSMNGLSK
     SHRIAGFRVG WMVLSGPKTH VKGYIEGLNM LSNMRLCSNV LAQQVVQTSL GGHQSVDEML
     LPGGRIYEQR NFIYNAIQEI PGLSAVKPKA GLYIFPKIDR NMYRIDDDEQ FVLDFLKQEK
     VLLVHGRGFN WQEPDHFRIV YLPRVDELAQ IQEKMTRFLK QYRR
//