ID   A0PRS1_MYCUA            Unreviewed;       399 AA.
AC   A0PRS1;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   02-SEP-2026, entry version 86.
DE   RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE            EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN   OrderedLocusNames=MUL_2727 {ECO:0000313|EMBL:ABL05040.1};
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=362242 {ECO:0000313|EMBL:ABL05040.1, ECO:0000313|Proteomes:UP000000765};
RN   [1] {ECO:0000313|EMBL:ABL05040.1, ECO:0000313|Proteomes:UP000000765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99 {ECO:0000313|EMBL:ABL05040.1,
RC   ECO:0000313|Proteomes:UP000000765};
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D., Davies J.K., Jenkin G.A., Small P.L., Jones L.M., Tekaia F.,
RA   Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
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; CP000325; ABL05040.1; -; Genomic_DNA.
DR   RefSeq; WP_011740654.1; NC_008611.1.
DR   AlphaFoldDB; A0PRS1; -.
DR   KEGG; mul:MUL_2727; -.
DR   eggNOG; COG1168; Bacteria.
DR   HOGENOM; CLU_017584_15_2_11; -.
DR   Proteomes; UP000000765; Chromosome.
DR   GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; 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_large.
DR   InterPro; IPR051798; Class-II_PLP-Dep_Aminotrans.
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   Aminotransferase {ECO:0000313|EMBL:ABL05040.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000765};
KW   Transferase {ECO:0000313|EMBL:ABL05040.1}.
FT   DOMAIN          36..390
FT                   /note="Aminotransferase class I/classII large"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   399 AA;  43005 MW;  458A72A549EAD50D CRC64;
     MNPNPLEQLT LEQLRTRTSM KWRAHPADVL PLWVAEMDVN LAPTVAAALH RAVDNGDTGY
     PYGTAYAEAL AEFAALRWQW HDLEVGRTAI VPDVMMGIVE MLRLVTDRGD TVIVNSPVYA
     PFYAFVSHDG RRVVEAPLGT DGRINLDALE EAFAHARRAG GNVPYLLCNP HNPTGAAHSC
     DELRGVAERA RRYDVRVVSD EIHAPLVFSG ARFTPYLTVP GSENALSLTS ATKAWNLGGV
     KAALAVAGPE AAADLRRMPE EVSHGPSHLG IIAHTEAFRT GGDWLDALLA GLDANRTLSS
     DLVDAQLPGV RLRWPQGTYL AWLDCRDLGI SEQDASGLAV VSDLSGPASW FLDHARVALS
     SGHVFGTGGD GHVRMNFATS QAILTEAVTR MGKALGELR
//