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
//