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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//