ID   A0A1H3W415_9FIRM        Unreviewed;       434 AA.
AC   A0A1H3W415;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=O-acetylhomoserine (Thiol)-lyase {ECO:0000313|EMBL:SDZ81581.1};
GN   ORFNames=SAMN02745687_00607 {ECO:0000313|EMBL:SDZ81581.1};
OS   Lachnospiraceae bacterium NK3A20.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=877406 {ECO:0000313|EMBL:SDZ81581.1, ECO:0000313|Proteomes:UP000199449};
RN   [1] {ECO:0000313|EMBL:SDZ81581.1, ECO:0000313|Proteomes:UP000199449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NK3A20 {ECO:0000313|EMBL:SDZ81581.1,
RC   ECO:0000313|Proteomes:UP000199449};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU362118};
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000256|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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DR   EMBL; FNQX01000008; SDZ81581.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3W415; -.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000199449; 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:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR   CDD; cd00614; CGS_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; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01326; OAH_OAS_sulfhy; 1.
DR   PANTHER; PTHR43797; HOMOCYSTEINE/CYSTEINE SYNTHASE; 1.
DR   PANTHER; PTHR43797:SF2; HOMOCYSTEINE_CYSTEINE SYNTHASE; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:SDZ81581.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199449}.
FT   MOD_RES         211
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   434 AA;  47425 MW;  5EC3F542E3EF804E CRC64;
     MSGEHKFGFN TLQLHVGQEA ADPATDARAV PIYATTSYVF HNAQHAADRF ALKDAGNIYG
     RLTNSTQEVL EKRIAALEGG VAALAVASGA AAVTYSITAL AGAGDHVVAQ KTIYGGSYNL
     LQHTLPQYGV ETTFVDTNNL AEIEAAIQPN TKLVYIETLT NPNADVPDIE EIAKIAHSHG
     LPLIVDNTFG TPYLIRPFEW GADIVVHSAT KFIGGHGTTL GGIIVDSGNF DWTKSDRYPQ
     FTQPNPSYHG ISFVQAAGSA AYVTYIRAII LRDEGAAISP FAAFLLLQGT ETLSLRLDRH
     WENTRRVLEF LRSEPLVKKI NHPYLEDHPN HKVYQKYFPN GGGSIFTFDI DGGQEEAFAF
     IDHLQIFSLL ANVADVKSLV VHPATTTHAE LSDEEAAEQD IYQSTIRLSI GTEDADDIIW
     DLQNGFDAVR ELEK
//