ID A6L217_PHOV8 Unreviewed; 391 AA. AC A6L217; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 02-SEP-2026, entry version 79. DE RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224}; DE EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224}; GN OrderedLocusNames=BVU_2066 {ECO:0000313|EMBL:ABR39731.1}; OS Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / OS NBRC 14291 / NCTC 11154) (Bacteroides vulgatus). OC Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales; OC Bacteroidaceae; Phocaeicola. OX NCBI_TaxID=435590 {ECO:0000313|EMBL:ABR39731.1, ECO:0000313|Proteomes:UP000002861}; RN [1] {ECO:0000313|EMBL:ABR39731.1, ECO:0000313|Proteomes:UP000002861} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / RC NCTC 11154 {ECO:0000313|Proteomes:UP000002861}; RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156; RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C., RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H., RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K., RA Knight R.D., Gordon J.I.; RT "Evolution of symbiotic bacteria in the distal human intestine."; RL PLoS Biol. 5:1574-1586(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}. 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; CP000139; ABR39731.1; -; Genomic_DNA. DR RefSeq; WP_005842558.1; NC_009614.1. DR AlphaFoldDB; A6L217; -. DR STRING; 435590.BVU_2066; -. DR PaxDb; 435590-BVU_2066; -. DR GeneID; 5303031; -. DR KEGG; bvu:BVU_2066; -. DR eggNOG; COG1168; Bacteria. DR HOGENOM; CLU_017584_15_0_10; -. DR BioCyc; BVUL435590:G1G59-2159-MONOMER; -. DR Proteomes; UP000002861; 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; IPR027619; C-S_lyase_PatB-like. 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 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:ABR39731.1}; KW Lyase {ECO:0000256|ARBA:ARBA00023239}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}; KW Reference proteome {ECO:0000313|Proteomes:UP000002861}; KW Transferase {ECO:0000313|EMBL:ABR39731.1}. FT DOMAIN 30..370 FT /note="Aminotransferase class I/classII large" FT /evidence="ECO:0000259|Pfam:PF00155" SQ SEQUENCE 391 AA; 44768 MW; 473B89BA8F6ADC4E CRC64; MKYNFDKVID RSGTSAEKVE GLKHIWGRTD LIPLWVADMD FATAPFVTDA IRKRCENEVL GYTGKPDSYY NAIINWVKQR YDLIVTKEVI NFVPGIVPGI GMAMNCFTQK GDKVMIQPPV YHPFAWVTTR NERTLVINPL RWENGMYRMD LDAFREQIKG CKLFILCNPH NPGGVVWTEA ELRAIADICY DEKVLVFSDE IHADLTLPPH THRPFATVSE KARMNSVTFM SPSKAFNMPG LSASHALIFN EDLRKRFRIY MDAGELDMGH VFAFLSVEAA YSHGTEWLDQ CLAYIQGNID FVDEFLKKHA PKIKAIRPEA SYLVWLDCRE LELSQKDLNE FFVDKAHLAL NDGEMFGKEG IGFMRLNVAS PRCIIEKAMK QLADAYQLYI K //