ID   A0A124IN97_9FIRM        Unreviewed;       430 AA.
AC   A0A124IN97;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase {ECO:0000313|EMBL:KUO71540.1};
GN   ORFNames=APF81_11235 {ECO:0000313|EMBL:KUO71540.1};
OS   Desulfosporosinus sp. BRH_c37.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=1734396 {ECO:0000313|EMBL:KUO71540.1, ECO:0000313|Proteomes:UP000053148};
RN   [1] {ECO:0000313|EMBL:KUO71540.1, ECO:0000313|Proteomes:UP000053148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c37 {ECO:0000313|EMBL:KUO71540.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) 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:KUO71540.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LOEW01000260; KUO71540.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A124IN97; -.
DR   Proteomes; UP000053148; 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   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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Transferase {ECO:0000313|EMBL:KUO71540.1}.
FT   MOD_RES         210
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   430 AA;  46663 MW;  B59F0A33E1C662AE CRC64;
     MTEQRQLGIE TISLHGGQSP DSATNARAVP IYQTSSFVFN DTDHAANLFA LKESGNIYTR
     IMNPTQDVFE QRIALLEGGV GALATASGQA AITYALLNIV QAGDEIVASS SLYGGTYTLF
     AYTFAKLGIK VHFVDVDKPE EFRSKITSQT KALYTETIGN PQINIADLER IAQIAHDNGL
     PLIVDNTFAS PYLCRPFEHG ADIVVHSATK FIGGHGTSIG GVIVDSGKFD WNNGKFLGLS
     QPDPSYHGIV FTEACGNAAY IIKARVSLLR DTGAALSPFN SFLFLQGLET LPLRMERHVA
     NAQKVAEFLD QHELVTWVNY PGLAKSPYHT LAKKYLPKGT GSIFTFGLKG GLNEGKKFIN
     NLKLFSHLAN VGDAKSLVIH PASTTHQQLD EESQRVAGVS PDMIRLSIGL ETIEDLLYDL
     DKALQTSQTA
//