ID   A0A172ZKI5_9BACL        Unreviewed;       412 AA.
AC   A0A172ZKI5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE            EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN   ORFNames=AR543_20250 {ECO:0000313|EMBL:ANF98108.1};
OS   Paenibacillus bovis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1616788 {ECO:0000313|EMBL:ANF98108.1, ECO:0000313|Proteomes:UP000078148};
RN   [1] {ECO:0000313|Proteomes:UP000078148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BD3526 {ECO:0000313|Proteomes:UP000078148};
RA   Wu Z., Gao C., Liu Z., Zheng H.;
RT   "Genome of Paenibacillus bovis sp. nov.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ANF98108.1, ECO:0000313|Proteomes:UP000078148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BD3526 {ECO:0000313|EMBL:ANF98108.1,
RC   ECO:0000313|Proteomes:UP000078148};
RX   PubMed=26769366; DOI=10.1099/ijsem.0.000900;
RA   Gao C., Han J., Liu Z., Xu X., Hang F., Wu Z.;
RT   "Paenibacillus bovis sp. nov., isolated from raw yak (Bos grunniens)
RT   milk.";
RL   Int. J. Syst. Evol. Microbiol. 66:1413-1418(2016).
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; CP013023; ANF98108.1; -; Genomic_DNA.
DR   RefSeq; WP_060536190.1; NZ_CP013023.1.
DR   AlphaFoldDB; A0A172ZKI5; -.
DR   STRING; 1616788.AR543_20250; -.
DR   KEGG; pbv:AR543_20250; -.
DR   OrthoDB; 9802872at2; -.
DR   Proteomes; UP000078148; Chromosome.
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; 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   Lyase {ECO:0000313|EMBL:ANF98108.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078148}.
FT   DOMAIN          32..387
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   412 AA;  46790 MW;  8C7D98007B56E8B8 CRC64;
     MDYTQRFDHP PERINTNSAK WDQLQKLFGT EDVLPLWVAD MDFAAPESVQ HALKKSAEHG
     VVGYSFQSEA YYHALQEWMK NRHGWEIEKD WVVFTPGVVT ALNFAVQTFT EHGDQVVIQT
     PVYPPFYSVV TGHGREVVEN PLQQQENGDY AMDLEQLEQA LSGERVKLLI LCSPHNPIGR
     VWSREELERV DALCEKYNVI VVSDEIHGDL VFEPNQHIPY AMLSEQAKNR SIICTAPSKT
     FNIAGLNTSN VIIPNPELRD AFALKINNFG VGHISQFGAA ATEAAYTEGQ EWLEQCMQYI
     RANMEYVQQY ITEHLPEVSV NMPEATYLMW MDFRKLGMEQ ADLVSFLLHK ARIALNDGRA
     FGTAGEGYMR LNVACSRRLL EEAMERLRGA LEQWRTEGSP KAAEQVSSET NA
//