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Database: UniProt
Entry: A0A0M4GT00_9BACI
LinkDB: A0A0M4GT00_9BACI
Original site: A0A0M4GT00_9BACI 
ID   A0A0M4GT00_9BACI        Unreviewed;       441 AA.
AC   A0A0M4GT00;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase {ECO:0000313|EMBL:ALC92145.1};
DE            EC=2.5.1.49 {ECO:0000313|EMBL:ALC92145.1};
GN   ORFNames=AM500_21980 {ECO:0000313|EMBL:ALC92145.1};
OS   Bacillus sp. FJAT-18017.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1705566 {ECO:0000313|EMBL:ALC92145.1, ECO:0000313|Proteomes:UP000060713};
RN   [1] {ECO:0000313|EMBL:ALC92145.1, ECO:0000313|Proteomes:UP000060713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-18017 {ECO:0000313|EMBL:ALC92145.1,
RC   ECO:0000313|Proteomes:UP000060713};
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 (AUG-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}.
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DR   EMBL; CP012602; ALC92145.1; -; Genomic_DNA.
DR   RefSeq; WP_053601126.1; NZ_CP012602.1.
DR   AlphaFoldDB; A0A0M4GT00; -.
DR   STRING; 1705566.AM500_21980; -.
DR   PATRIC; fig|1705566.3.peg.4860; -.
DR   Proteomes; UP000060713; Chromosome.
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:UP000060713};
KW   Transferase {ECO:0000313|EMBL:ALC92145.1}.
FT   MOD_RES         211
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   441 AA;  47707 MW;  9094BF049E01096F CRC64;
     MTNQNENFGL ETLLLHGGQT PDPVTGSRAV PIYQTTSYVF KDTDHAQNLF SLAESGNIYT
     RIMNPTTDVL EKRIALLEGG AAALAVSSGM AAISLAIMNL AEAGDEIVAA ENLYGGTFNL
     FAVTLPKFGI NVRFVDSTNP ENFREAITPK TKVIFGEIIG NPSLNVLDVE AVADIAHENG
     IPLIIDNTFA SPYSCRPIEW GADIVVHSAT KWIGGHGTTI GGLIVDAGKF DWNSDKFPGF
     TEPDPSYNGL RFAQDVGPLA FITKLRVQLL RDFGSSLSPQ SAFLLLQGLE TLHLRIQKHN
     ENAIEIAQYL KDHPAVEWVS FPGLEEHPSH QLAKKYLGGG YGSIIVFGIK GGREAGKKVI
     DNIKLWSHVA NVGDAKSLII HPASTTHQQL SAEDLVKSGV TEELIRLSVG LETVKDLKED
     LDQAFLKAAS VSAAPEEQLN R
//
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