ID   U2QGD0_9BACT            Unreviewed;       392 AA.
AC   U2QGD0;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE            EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN   ORFNames=HMPREF9135_2167 {ECO:0000313|EMBL:ERK40388.1};
OS   Segatella baroniae F0067.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Segatella.
OX   NCBI_TaxID=1115809 {ECO:0000313|EMBL:ERK40388.1, ECO:0000313|Proteomes:UP000016648};
RN   [1] {ECO:0000313|EMBL:ERK40388.1, ECO:0000313|Proteomes:UP000016648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0067 {ECO:0000313|EMBL:ERK40388.1,
RC   ECO:0000313|Proteomes:UP000016648};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (AUG-2013) 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:ERK40388.1}.
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DR   EMBL; AWEY01000006; ERK40388.1; -; Genomic_DNA.
DR   RefSeq; WP_021588617.1; NZ_AWEY01000006.1.
DR   AlphaFoldDB; U2QGD0; -.
DR   PATRIC; fig|1115809.3.peg.190; -.
DR   Proteomes; UP000016648; 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; 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:ERK40388.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016648}.
FT   DOMAIN          31..379
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   392 AA;  44152 MW;  762527E7DF081285 CRC64;
     MAKYDFDKLT ERRGTNSYKW DSPVDADVLP MWVADMDFEV APAITKALQE RVTQGIFGYT
     MVPDSYYEAI VDWFKRRHGW TLERDWILYT TGVVPAVSCA LKALTLPGEK VLVQTPAYNC
     FFSSIANSGC QLAENELIYE NGTYHIDFDD FERKCADEKT TVFLLCNPHN PAGRVWKREE
     LERMNAICLK HGVKVVSDEI HCELVMPGFR FVPFASVSAA CRDNCVVLNS PSKAFNIAGL
     QIANIICADA AVRRRIDRAV NINEVCDVNP FGVLALQAAY TAGEEWLDEL NAYIHGNYEL
     VKDFVAKEMP KLKVVRMEGT YLVWLDVMGL ESTSDELTDK LLKEAKVMVN SGTMYGRRAG
     EGFIRLNIAC PRARLLEGLK RMGRCLAEYN GG
//