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Database: UniProt
Entry: A0A1A3QL38_9MYCO
LinkDB: A0A1A3QL38_9MYCO
Original site: A0A1A3QL38_9MYCO 
ID   A0A1A3QL38_9MYCO        Unreviewed;       398 AA.
AC   A0A1A3QL38;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE            EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN   ORFNames=A5655_08970 {ECO:0000313|EMBL:OBK46815.1};
OS   Mycobacterium sp. 1081908.1.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834066 {ECO:0000313|EMBL:OBK46815.1, ECO:0000313|Proteomes:UP000092324};
RN   [1] {ECO:0000313|Proteomes:UP000092324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1081908.1 {ECO:0000313|Proteomes:UP000092324};
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Garcia-Basteiro A.,
RA   Lopez-Varela E., Palencia S.;
RL   Submitted (JUN-2016) 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:OBK46815.1}.
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DR   EMBL; LZLY01000104; OBK46815.1; -; Genomic_DNA.
DR   RefSeq; WP_067011883.1; NZ_LZLY01000104.1.
DR   AlphaFoldDB; A0A1A3QL38; -.
DR   STRING; 1834066.A5655_08970; -.
DR   OrthoDB; 3224382at2; -.
DR   Proteomes; UP000092324; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; PTHR43525:SF2; CYSTATHIONINE BETA-LYASE-RELATED; 1.
DR   PANTHER; PTHR43525; PROTEIN MALY; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:OBK46815.1}.
FT   DOMAIN          52..390
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   398 AA;  42790 MW;  62E5AAFD4FE5F5CE CRC64;
     MTFNPLEELT LQQLRARTSM KWRAHPADVV PLWVAEMDVQ LAPTIADALR AAIDIGDTGY
     PAGHAFAEAV GEFASRRWQW HDLEVGRTAT VPDVMLGIVE TLRLVTDRGD AVVVNSPVYA
     PFYAFVTHDG RRVIESPLDA EGRIDLGALE EAFARACTSG GQAAYLLCNP HNPTGAVHTF
     DELRGVAELA RRFGVRVVSD EIHAPVILPG ARFVPYLTVP GAENAFALTS ASKAWNLSGL
     KAALAIAGPE SAADLHRMPE EVGHGPSHLG IIAHAEAFRS GGEWLDALLA GLDANRALLG
     DLVAEHLPDV KYRRPQGTYL AWLDCRALGF DEEETGRLAV VADLSGPARW FLDHARVALS
     SGHVFGTGGA GHVRLNFATS QAILTEAVSR MGRALAQR
//
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