ID D4K0F9_9FIRM Unreviewed; 429 AA.
AC D4K0F9;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE SubName: Full=O-acetylhomoserine sulfhydrolase {ECO:0000313|EMBL:CBK99758.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:CBK99758.1};
GN ORFNames=FP2_24380 {ECO:0000313|EMBL:CBK99758.1};
OS Faecalibacterium prausnitzii L2-6.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Faecalibacterium.
OX NCBI_TaxID=718252 {ECO:0000313|EMBL:CBK99758.1, ECO:0000313|Proteomes:UP000008804};
RN [1] {ECO:0000313|EMBL:CBK99758.1, ECO:0000313|Proteomes:UP000008804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-6 {ECO:0000313|Proteomes:UP000008804};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Faecalibacterium prausnitzii L2/6.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK99758.1, ECO:0000313|Proteomes:UP000008804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-6 {ECO:0000313|Proteomes:UP000008804};
RA Pajon A.;
RL Submitted (MAR-2010) 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; FP929045; CBK99758.1; -; Genomic_DNA.
DR AlphaFoldDB; D4K0F9; -.
DR STRING; 718252.FP2_24380; -.
DR KEGG; fpr:FP2_24380; -.
DR PATRIC; fig|718252.3.peg.624; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_0_9; -.
DR BioCyc; FPRA718252:G1375-2072-MONOMER; -.
DR Proteomes; UP000008804; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:CBK99758.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008804};
KW Transferase {ECO:0000313|EMBL:CBK99758.1}.
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 429 AA; 46377 MW; 1D7DC35E29DD1A7F CRC64;
MSNYKFETLQ LHVGQEQADP ATDSRAVPIY QTTSYVFRNS QHAADRFGLA DAGNIYGRLT
NSTQDVFEKR IAALEGGVAA LATASGAAAI TYTIEALAQA GDHIVAQKTI YGGSYNLLEH
TLTQFGVTTT FVDAHDLEEV ENAIQPNTKA VYLETLGNPN SDIPDIDAIA AIAHKHGLPL
VIDNTFGTPY LIRPIEHGAD IVVHSATKFI GGHGTTLGGI IVDSGKFDWK ASGKYGNIAA
PNPSYHGVSF ADAAGPAAFV TYIRAILLRD TGATISPFNA FLLLQGTETL SLRIERHVEN
TKKVVEFLAN HPQVEKVNHP SLPDHPDHAL YEKYFPNGGA SIFTFNIKGG REEAFKFIDN
LKIFSLLANV ADVKSLVIHP ASTTHSQLTD EELAEQQIYQ NTIRLSIGTE HIDDIIADLE
AGFAAVRGE
//