ID   I0R6K7_9FIRM            Unreviewed;       405 AA.
AC   I0R6K7;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE            EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN   ORFNames=HMPREF9970_0337 {ECO:0000313|EMBL:EIC95315.1};
OS   Lachnoanaerobaculum saburreum F0468.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Lachnoanaerobaculum.
OX   NCBI_TaxID=1095750 {ECO:0000313|EMBL:EIC95315.1, ECO:0000313|Proteomes:UP000005039};
RN   [1] {ECO:0000313|EMBL:EIC95315.1, ECO:0000313|Proteomes:UP000005039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0468 {ECO:0000313|EMBL:EIC95315.1,
RC   ECO:0000313|Proteomes:UP000005039};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (MAR-2012) 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:EIC95315.1}.
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DR   EMBL; AJGH01000087; EIC95315.1; -; Genomic_DNA.
DR   RefSeq; WP_008749943.1; NZ_AJGH01000087.1.
DR   AlphaFoldDB; I0R6K7; -.
DR   PATRIC; fig|1095750.3.peg.1895; -.
DR   eggNOG; COG1168; Bacteria.
DR   OrthoDB; 9802872at2; -.
DR   Proteomes; UP000005039; 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; 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   Lyase {ECO:0000313|EMBL:EIC95315.1}.
FT   DOMAIN          58..394
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   405 AA;  46850 MW;  8FF0236303EA4055 CRC64;
     MYNFDEIIDR RNTNCLNTDG FRGYIFHAEP EKKFPYKDEE FVRMWVADME FAVAAPILEA
     LRERIDRKIF GYTGVYDDSY YQSFKKWCED HYKWSFPKDE LCFSPGIIPA MYQLVETLLT
     KNEKVLVNTP SYGYFLHAAE YSGVEVLQSP LKKDKNGRFV LDYENFEKQC ADPACKLVFW
     CNPHNPTGRM WTEEELRRCG EIMMQYNLWV ISDEIHCDLI RQGKQHIPMA KVLDNYPKLI
     TCMAPSKTFN LAGLAFSNII IRDPQLREIF KNRDKLFGMV NPMSLVAAKA AYDRGGEWHE
     ELKIYLDKNF EFVKEYLSTN LPEAVMGISE ATYLAWVDLS AVLPDVKDLP GFFANNAGVL
     LEGGNSLFVG NADGYIRLNL AMPQAIIKTG LERICKSIEE YKNKI
//