ID D0R4Z0_LACJF Unreviewed; 388 AA. AC D0R4Z0; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 27-MAR-2024, entry version 50. DE RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224}; DE EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224}; GN Name=patB {ECO:0000313|EMBL:CAX67153.1}; GN OrderedLocusNames=FI9785_1293 {ECO:0000313|EMBL:CAX67153.1}; OS Lactobacillus johnsonii (strain FI9785). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=633699 {ECO:0000313|EMBL:CAX67153.1, ECO:0000313|Proteomes:UP000002627}; RN [1] {ECO:0000313|EMBL:CAX67153.1, ECO:0000313|Proteomes:UP000002627} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FI9785 {ECO:0000313|EMBL:CAX67153.1, RC ECO:0000313|Proteomes:UP000002627}; RX PubMed=19767436; DOI=10.1128/JB.01182-09; RA Wegmann U., Overweg K., Horn N., Goesmann A., Narbad A., Gasson M.J., RA Shearman C.; RT "Complete genome sequence of Lactobacillus johnsonii FI9785, a competitive RT exclusion agent against pathogens in poultry."; RL J. Bacteriol. 191:7142-7143(2009). 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 --------------------------------------------------------------------------- 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; FN298497; CAX67153.1; -; Genomic_DNA. DR RefSeq; WP_012846404.1; NC_013504.1. DR AlphaFoldDB; D0R4Z0; -. DR KEGG; ljf:FI9785_1293; -. DR HOGENOM; CLU_017584_15_0_9; -. DR Proteomes; UP000002627; Chromosome. 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:CAX67153.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002627}; KW Transferase {ECO:0000313|EMBL:CAX67153.1}. FT DOMAIN 27..377 FT /note="Aminotransferase class I/classII" FT /evidence="ECO:0000259|Pfam:PF00155" SQ SEQUENCE 388 AA; 43900 MW; 9024CD2B67721C1D CRC64; MKYDFKTVVN RRHTDSVKWN VKDNELPMSI ADMDFKTAPE IILAIKEKIK LGAFGYEEPG KDYFNSVSNW YELEHGAKAE PNWMIFATGV VPAISSIVRR VSHIGDNVLV QEPVYNIFYN SIENNGRHVL SNDLIYSNGK YEINWQDLEE KLANPLTTLM VFCNPHNPPG IVWKKREVER IASLCQENNV ILLSDEIHGD LVRNNVKYTP AFSVAKILRS NVISLVSPSK TFNVASLHAA TVIIPDNNLR DIINRGLNID ELAEPNLLAI PATIAAYTEG FNWLHELLAV IDNNFAYVEK KITSQLENVK IFSGPATYLM WLDVSKITHD SYKLAAYLRK ETGLIVSAGS IYRRNGNEFL RINLASPKSM VEDGISRLII GIKKYSKK //