ID   A0A085F3I7_9BURK        Unreviewed;       412 AA.
AC   A0A085F3I7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=O-acetylhomoserine sulfhydrylase {ECO:0000313|EMBL:KFC66032.1};
GN   ORFNames=FG94_03590 {ECO:0000313|EMBL:KFC66032.1};
OS   Massilia sp. LC238.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1502852 {ECO:0000313|EMBL:KFC66032.1, ECO:0000313|Proteomes:UP000028601};
RN   [1] {ECO:0000313|EMBL:KFC66032.1, ECO:0000313|Proteomes:UP000028601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LC238 {ECO:0000313|EMBL:KFC66032.1,
RC   ECO:0000313|Proteomes:UP000028601};
RA   Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT   "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT   isolate.";
RL   Submitted (JUN-2014) 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}.
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:KFC66032.1}.
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DR   EMBL; JNNN01000065; KFC66032.1; -; Genomic_DNA.
DR   RefSeq; WP_036214334.1; NZ_JNNN01000065.1.
DR   AlphaFoldDB; A0A085F3I7; -.
DR   STRING; 1502852.FG94_03590; -.
DR   PATRIC; fig|1502852.3.peg.3539; -.
DR   eggNOG; COG2873; Bacteria.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000028601; Unassembled WGS sequence.
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   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   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.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   MOD_RES         208
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   412 AA;  44353 MW;  5DBBFE37CDA81738 CRC64;
     MSEQKYGFTT TILHNDRRKS IEQGSLHKPV HTSVAFGYND ARQLASVFQG KEPGFRYGRQ
     GNPTVAALED KISKMEDGVG TICFATGMGA IGALFQGLLR AGDHIVSSSF LFGNTNSLWQ
     TVAAQGVAVD FVDATDVANV EAVLRPDTRM VFVETIANPR TQVADLARIG QLCRERGILY
     VVDNTMTTPW LFRPKAVGAG LVVNSLTKSI GGHGIALGGA LTDTGLFDWS AYPHIAANFR
     KQPAANQGLA QLRAKALRDF GAALGPEAAH HIAVGAETLA LRMERTSANA LALAQMLEAD
     ERVAAVHYPG LASHPQNGIT KELFRAGGSL MSFELREDID CFDYLNRLKL GIPASNLGDT
     RTLVIPVAHT IFFEMGAERR ASMGIAESLI RVSVGIEDTE DLLADFRQAL EA
//