ID Q5LFN6_BACFN Unreviewed; 428 AA.
AC Q5LFN6; A0A380YWU2;
DT 21-JUN-2005, integrated into UniProtKB/TrEMBL.
DT 21-JUN-2005, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=O-acetylhomoserine sulfhydrylase {ECO:0000313|EMBL:CAH07057.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:CAH07057.1};
GN Name=metY {ECO:0000313|EMBL:CAH07057.1};
GN ORFNames=BF9343_1276 {ECO:0000313|EMBL:CAH07057.1};
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH07057.1, ECO:0000313|Proteomes:UP000006731};
RN [1] {ECO:0000313|EMBL:CAH07057.1, ECO:0000313|Proteomes:UP000006731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 /
RC Onslow {ECO:0000313|Proteomes:UP000006731};
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
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; CR626927; CAH07057.1; -; Genomic_DNA.
DR RefSeq; WP_010992441.1; NZ_UFTH01000001.1.
DR PaxDb; 272559-BF9343_1276; -.
DR KEGG; bfs:BF9343_1276; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_0_10; -.
DR BioCyc; BFRA272559:G1GHZ-1373-MONOMER; -.
DR Proteomes; UP000006731; Chromosome.
DR GO; GO:0018826; F:methionine gamma-lyase activity; IEA:UniProtKB-EC.
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:UP000006731};
KW Transferase {ECO:0000313|EMBL:CAH07057.1}.
FT MOD_RES 210
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 428 AA; 46089 MW; 23A3EC8E84552EA4 CRC64;
METKKLHFET LQLHVGQETP DPATDARAVP IYQTTSYVFR DSAHAAARFG LQDPGNIYGR
LTNSTQGVLE ERIAALEGGV GGLAVASGAA AVTYAIENIT RSGDHIVAAK TIYGGTYNLL
AHTLPAYGVT TTFVDPSDLF NFERAIRENT KAIFIETLGN PNSNIIDMDA VAAIAHKYRI
PLIVDNTFGT PYLIRPIEHG ADIVVHSATK FIGGHGSSLG GVIVDSGKFD WVASGKFPQL
TEPDASYHGV RFVDAAGAAA YIVRIRAVLL RDTGAAISPF NAFILLQGLE TLSLRVERHV
ANALKVIDFL VNHPKVAAVN HPSLPGHPDH AIYQRYFPGG AGSIFTFEVK GGTEEAQKFI
DSLQIFSLLA NVADVKSLVI HPGTTTHSQL NAQELEEQGI KPGTVRLSIG TEHIEDIIDD
LRQALEKI
//