ID   D3HA49_STRM6            Unreviewed;       388 AA.
AC   D3HA49;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE            EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN   OrderedLocusNames=smi_1507 {ECO:0000313|EMBL:CBJ22747.1};
OS   Streptococcus mitis (strain B6).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=365659 {ECO:0000313|EMBL:CBJ22747.1, ECO:0000313|Proteomes:UP000008563};
RN   [1] {ECO:0000313|EMBL:CBJ22747.1, ECO:0000313|Proteomes:UP000008563}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B6 {ECO:0000313|EMBL:CBJ22747.1,
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-II pyridoxal-phosphate-dependent
CC       aminotransferase family. MalY/PatB cystathionine beta-lyase subfamily.
CC       {ECO:0000256|ARBA:ARBA00037974}.
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DR   EMBL; FN568063; CBJ22747.1; -; Genomic_DNA.
DR   RefSeq; WP_000521356.1; NC_013853.1.
DR   RefSeq; YP_003446609.1; NC_013853.1.
DR   AlphaFoldDB; D3HA49; -.
DR   STRING; 365659.smi_1507; -.
DR   KEGG; smb:smi_1507; -.
DR   PATRIC; fig|365659.3.peg.1517; -.
DR   eggNOG; COG1168; Bacteria.
DR   HOGENOM; CLU_017584_15_0_9; -.
DR   OrthoDB; 9802872at2; -.
DR   Proteomes; UP000008563; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; IPR027619; C-S_lyase_PatB-like.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR04350; C_S_lyase_PatB; 1.
DR   PANTHER; PTHR43525; PROTEIN MALY; 1.
DR   PANTHER; PTHR43525:SF1; PROTEIN MALY; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
FT   DOMAIN          41..381
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   388 AA;  44477 MW;  E8D20D76F82DB276 CRC64;
     MGKYDFTSLP NRLGHHTYKW KEAETDSEVL PAWIADMDFV VLPEIRQAVQ TYADQLVYGY
     TYASEELIKE VQKWEATQHG YHFDKEALVF IEGVVPAIST AIQAFTKEGE AVLINTPVYP
     PFARSVKLNN RRLITNSLVE KDGLFEIDFD QLEKDLVEED VKLYILCNPH NPGGRVWEKE
     VLEKIGQLCQ KHGVFLVSDE IHQDLALFGH KHHSFNTINP DFKEFAIVLS SATKTFNIAG
     TKNSYAVIEN PKLRLAYQKR QLANNQHEIS GLGYLATEAA YRYGKDWLEE LKQVFEDHIN
     YVVDLFGKET KIKVMKPQGT YLIWLDFSAY DLTDETLQEL LRNEAKVILN RGLDFGEEGS
     LHARLNVAMP KSLLQEVCQR IVTTFAKL
//