ID   Q8DUR2_STRMU            Unreviewed;       380 AA.
AC   Q8DUR2;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:AAN58557.1};
GN   OrderedLocusNames=SMU_841 {ECO:0000313|EMBL:AAN58557.1};
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN58557.1, ECO:0000313|Proteomes:UP000002512};
RN   [1] {ECO:0000313|EMBL:AAN58557.1, ECO:0000313|Proteomes:UP000002512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512};
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H.,
RA   Najar F., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR   EMBL; AE014133; AAN58557.1; -; Genomic_DNA.
DR   RefSeq; NP_721251.1; NC_004350.2.
DR   RefSeq; WP_002352252.1; NC_004350.2.
DR   AlphaFoldDB; Q8DUR2; -.
DR   STRING; 210007.SMU_841; -.
DR   KEGG; smu:SMU_841; -.
DR   PATRIC; fig|210007.7.peg.748; -.
DR   eggNOG; COG1104; Bacteria.
DR   HOGENOM; CLU_003433_0_0_9; -.
DR   OrthoDB; 9808002at2; -.
DR   PhylomeDB; Q8DUR2; -.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.260.50; -; 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; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR016454; Cysteine_dSase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11601:SF50; CYSTEINE DESULFURASE ISCS 2-RELATED; 1.
DR   PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000313|EMBL:AAN58557.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002512};
KW   Transferase {ECO:0000313|EMBL:AAN58557.1}.
FT   DOMAIN          2..365
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   380 AA;  41817 MW;  40F1CA7A7C9534C3 CRC64;
     MIYFDNSATT LPYPEAIKTY EEVATKIFGN PSSLHQLGSQ SSRILQASRQ QIAELLGKRT
     DEVFFTSGGT EGDNWVIKGL AFEKQRYGKH IIVSDIEHPA VKESAKWLQT QGFEVDFAPV
     DKKGFVKVDV LAKLLRPDTI LVSIMAVNNE IGSVQPIKAI SKLLADKASI SFHVDAVQAI
     GKIATDDYLT DRVDFATFSG HKFHSVRGVG FIYKKAGKKI SPLLNGGGQE AGFRSTTENV
     AGIAATVKAL RIVLDKAKIG QKQLLAMKRI LFDSLSHYDD VILFSEMEYF APNILTFGIK
     GVRGEVLVHA FEEHDIYIST TSACSSKAGK PAGTLISMGI SSKLAQTAVR LSLDEDNDMS
     QVEQFLTIFK QIYEKTKKVR
//