ID   A0A396MQU2_9BACT        Unreviewed;       389 AA.
AC   A0A396MQU2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE            EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN   ORFNames=DWW79_07575 {ECO:0000313|EMBL:RHR63108.1};
OS   Alistipes sp. AF17-16.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=2292190 {ECO:0000313|EMBL:RHR63108.1, ECO:0000313|Proteomes:UP000265869};
RN   [1] {ECO:0000313|EMBL:RHR63108.1, ECO:0000313|Proteomes:UP000265869}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF17-16 {ECO:0000313|EMBL:RHR63108.1,
RC   ECO:0000313|Proteomes:UP000265869};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) 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:RHR63108.1}.
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DR   EMBL; QUGX01000004; RHR63108.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A396MQU2; -.
DR   Proteomes; UP000265869; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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   Aminotransferase {ECO:0000313|EMBL:RHR63108.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265869};
KW   Transferase {ECO:0000313|EMBL:RHR63108.1}.
FT   DOMAIN          34..370
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   389 AA;  44286 MW;  773C8E4BF3A7D8AD CRC64;
     MKYDFDTIIP RRGTNSYKWD TPEEEGVLPM WVADMDFRTA PAVIEALQRR VAHGIFGYTK
     VPQAYYDAVV RWFGNRHRWQ VDPRWIVYTS GVVPALSAII KALTVPGDRV IVQTPAYNCF
     YSSIRNDGCE MSANRLVYRD NRYTVDFDDL EAKAADPKAK LLLLCNPHNP VGRVWTPEEL
     RRIGDICLRH GVFVVADEIH CELTYEGHDY TPFASLSERF LMNSATCVSP SKAFNLAGLQ
     IADIVAADEQ VRRRIDRAVN INEVCDVNPF GVAATIAAYD ESGAWLDALR KYLWGNYEYL
     RRFFEERLPQ YPVLPLEGTY LVWIDCRATG IGSDDTALRL QKEQKLMVNS GTLYGPGGEG
     FIRLNIACPR TLLADGLERT VRVLERRRD
//