ID   V9WB03_9BACL            Unreviewed;       397 AA.
AC   V9WB03;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE            EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN   Name=malY {ECO:0000313|EMBL:AHD06895.1};
GN   ORFNames=ERIC2_c31440 {ECO:0000313|EMBL:AHD06895.1};
OS   Paenibacillus larvae subsp. larvae DSM 25430.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=697284 {ECO:0000313|EMBL:AHD06895.1, ECO:0000313|Proteomes:UP000029431};
RN   [1] {ECO:0000313|EMBL:AHD06895.1, ECO:0000313|Proteomes:UP000029431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25430 {ECO:0000313|EMBL:AHD06895.1,
RC   ECO:0000313|Proteomes:UP000029431};
RX   PubMed=24599066;
RA   Djukic M., Brzuszkiewicz E., Funfhaus A., Voss J., Gollnow K., Poppinga L.,
RA   Liesegang H., Garcia-Gonzalez E., Genersch E., Daniel R.;
RT   "How to Kill the Honey Bee Larva: Genomic Potential and Virulence
RT   Mechanisms of Paenibacillus larvae.";
RL   PLoS ONE 9:E90914-E90914(2014).
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; CP003355; AHD06895.1; -; Genomic_DNA.
DR   RefSeq; WP_024094949.1; NZ_CP019652.1.
DR   AlphaFoldDB; V9WB03; -.
DR   KEGG; plv:ERIC2_c31440; -.
DR   PATRIC; fig|697284.3.peg.2980; -.
DR   eggNOG; COG1168; Bacteria.
DR   HOGENOM; CLU_017584_15_0_9; -.
DR   Proteomes; UP000029431; Chromosome.
DR   GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:UniProtKB-EC.
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:AHD06895.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029431}.
FT   DOMAIN          30..385
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   397 AA;  45511 MW;  921362E111C8FF0C CRC64;
     MKTIFDKVVN RKGTFCTQWD YIEDRFGEKD LLPFSISDMD FRSPPEIIQA LEERLHHGVF
     GYTRWNHMEF KSAIQYWFRR RFACTVQADW IVYSPSVIYT VSRLIHQLTD PGDHIVIQTP
     AYDAFFKVIQ DNGRNMSCND LKIEQGRYTI DFDDLERKLA DPKAKLFLLC SPHNPTGRVW
     SQEELARMLD LCRAHRVFVV SDEIHMDIVH GPGSHIPVVK AAESTDHVCL CTSASKTFNT
     PGLGGSYAFI PNPSVREKFL LQLKNQDGLS SASIFGMLAT IRAYSACEEW ADQLRAYLYH
     NLRMVEQFLR QHLPDLSFTL PESTYLAWID VSDLGFSSEE LQEALVHKAK VAIMRGEVYG
     EAGRGFLRMN VGCPRVKVQE GLRRLKKAVD ELKGCSR
//