ID   E1LR72_STRMT            Unreviewed;       388 AA.
AC   E1LR72;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE            EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN   ORFNames=SMSK597_0470 {ECO:0000313|EMBL:EFO00998.1};
OS   Streptococcus mitis SK597.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=585204 {ECO:0000313|EMBL:EFO00998.1, ECO:0000313|Proteomes:UP000003316};
RN   [1] {ECO:0000313|EMBL:EFO00998.1, ECO:0000313|Proteomes:UP000003316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK597 {ECO:0000313|EMBL:EFO00998.1,
RC   ECO:0000313|Proteomes:UP000003316};
RA   Daugherty S.C., Tallon L.J., Jones K.M., Liu X., Kilian M., Tettelin H.;
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFO00998.1}.
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DR   EMBL; AEDV01000025; EFO00998.1; -; Genomic_DNA.
DR   RefSeq; WP_000521352.1; NZ_AEDV01000025.1.
DR   AlphaFoldDB; E1LR72; -.
DR   eggNOG; COG1168; Bacteria.
DR   Proteomes; UP000003316; Unassembled WGS sequence.
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; 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;
KW   Aminotransferase {ECO:0000313|EMBL:EFO00998.1};
KW   Transferase {ECO:0000313|EMBL:EFO00998.1}.
FT   DOMAIN          41..381
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   388 AA;  44568 MW;  68E089BCA801AB96 CRC64;
     MGKYDFTSLP NRLGHHTYKW KEAETDSEVL PAWIADMDFV VLPEIRQAVQ TYADQLVYGY
     TYASDDLIKE VQKWEATQHG YHFDKEALVF IEGVVPAIST AIQAFTKEGE AVLINTPVYP
     PFARSVKLNN RRLITNSLVE KDGLFEIDFD QLEKDLVEED VKLYILCNPH NPGGRVWEKE
     VLEKIGQLCQ KHGVFLVSDE IHQDLALFGH KHQSFNTVNP DFKEFAIVLT SATKTFNIAG
     TKNSYAVIEN PKLRLAYQKR QLTNNQHEIS GLGYLATEAA YRYGKDWLEE LKQVFEDHIN
     YVVDLFGKET KIKVMKPQGT YLIWLDFSAY DLTDERLQEL LRNEAKVILN RGLDFGEEGS
     LHARLNVAMP KSLLQEVCQR IVTTFAKR
//