ID A0A0A2TK45_9FIRM Unreviewed; 429 AA.
AC A0A0A2TK45;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase {ECO:0000313|EMBL:KGP74793.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:KGP74793.1};
GN ORFNames=JT05_14435 {ECO:0000313|EMBL:KGP74793.1};
OS Desulfosporosinus sp. Tol-M.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1536651 {ECO:0000313|EMBL:KGP74793.1, ECO:0000313|Proteomes:UP000030439};
RN [1] {ECO:0000313|EMBL:KGP74793.1, ECO:0000313|Proteomes:UP000030439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Abu Laban N., Tan B., Dao A., Foght J.;
RT "Draft genome of Desulfosporosinus sp. Tol-M obtained by stable isotope
RT probing of toluene- degrading methanogenic culture enriched from oil sands
RT tailing of Alberta, Canada.";
RL Submitted (OCT-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:KGP74793.1}.
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DR EMBL; JQID01000203; KGP74793.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2TK45; -.
DR STRING; 1536651.JT05_14435; -.
DR Proteomes; UP000030439; Unassembled WGS sequence.
DR GO; GO:0003961; F:O-acetylhomoserine aminocarboxypropyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; 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 Reference proteome {ECO:0000313|Proteomes:UP000030439};
KW Transferase {ECO:0000313|EMBL:KGP74793.1}.
FT MOD_RES 210
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 429 AA; 46553 MW; 64EE466147226830 CRC64;
MANTNYKFET LQLHVGQEKP DSATDARAVP IYATTSYVFK DSAQAAGRFA LTEGGNIYTR
LMNPTSDVFE QRMAALEGGV AALATASGAA AITYAIQNIA KSGDHIVSAK TIYGGTYNFF
ANTLADTGIE TTFVDGSDVS NFVNTIKPNT KVIFIESFGN PNCDIIDIDA VADVAHKNGI
PLIIDNTFAT PYLLRPIEHG ADIVVHSATK FIGGHGTVLG GVIIDSGKFN WAQNDKFPGL
SKPNSSYHGI VFTEAVGNLA YIIKIRTTLM RDTGAIVSPF NSFLLLQGLE TLSLRVERHV
ENALKVVEYL KNHPQVEKVN HPLLSDHRGH ELYSKYFPNG AGSIFTFEIK GGSMAAKKFC
ENLELFSLLA NVADVKSLVI HPASTTHSQM SEEELLESGI KPNTIRLSIG TEHIDDIIDD
LKHGFESIK
//
