ID A0A0Q3TYU1_9BACI Unreviewed; 430 AA.
AC A0A0Q3TYU1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase {ECO:0000313|EMBL:KQL37460.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:KQL37460.1};
GN ORFNames=AN959_05475 {ECO:0000313|EMBL:KQL37460.1};
OS Psychrobacillus sp. FJAT-21963.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX NCBI_TaxID=1712028 {ECO:0000313|EMBL:KQL37460.1, ECO:0000313|Proteomes:UP000051878};
RN [1] {ECO:0000313|EMBL:KQL37460.1, ECO:0000313|Proteomes:UP000051878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-21963 {ECO:0000313|EMBL:KQL37460.1,
RC ECO:0000313|Proteomes:UP000051878};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (SEP-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:KQL37460.1}.
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DR EMBL; LJIY01000001; KQL37460.1; -; Genomic_DNA.
DR RefSeq; WP_056828924.1; NZ_LJIY01000001.1.
DR AlphaFoldDB; A0A0Q3TYU1; -.
DR PATRIC; fig|1712028.3.peg.1233; -.
DR Proteomes; UP000051878; 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000051878};
KW Transferase {ECO:0000313|EMBL:KQL37460.1}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 207
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 430 AA; 46493 MW; 353E4D05978E6032 CRC64;
MTNFQPETLL LHGGQQPDPV TGSRAVPIHK TTSFVFRDTN HAQDLFALKE SGNIYSRITN
PTVDVFEQRV ALLEGGTAAV ALSSGMAAIA FSILNIAGAG DEIIAAENLY GGTFNLFAHT
LPRYGIHVKF VDSTDPENFR AAVTDKTKGF FAEIIGNPSL NVLDVEKVSA IANEVGVPLL
VDNTFASPYG ANPIKHGAHI VIHSATKWIG GHGTTIGGVV VDGGNFDWNS EKFPGFTEPD
VTYHGLRYGI DVPNVAFAIK LRVQLLRDFG PSLSPEAAFS FLQGLETLHL RVPKHNENAL
KIADYLSNHE GVEWVNYLGL ENHPSHELAH KYLHNGFGSI LTFGVKGGKE AGRHIIDNIE
IWSHVANVGD AKSLIIHPAS TTHQQLTPED LVKSGVTEDL IRLSVGLEAV EDLQNALDKV
LVGKTNVLSR
//
