ID A0A1B6B9T5_9FIRM Unreviewed; 392 AA.
AC A0A1B6B9T5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=O-acetylhomoserine sulfhydrylase {ECO:0000313|EMBL:GAU76468.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:GAU76468.1};
GN ORFNames=F3D3_1065 {ECO:0000313|EMBL:GAU76468.1};
OS Fusibacter sp. 3D3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XII. Incertae Sedis; Fusibacter.
OX NCBI_TaxID=1048380 {ECO:0000313|EMBL:GAU76468.1, ECO:0000313|Proteomes:UP000095197};
RN [1] {ECO:0000313|EMBL:GAU76468.1, ECO:0000313|Proteomes:UP000095197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D3 {ECO:0000313|EMBL:GAU76468.1,
RC ECO:0000313|Proteomes:UP000095197};
RA Serrano A.E., Escudero L.V., Encalada O., Tebes C.J., Fernandez S.,
RA Demergasso C.S.;
RT "Draft genome sequence of Fusibacter ascotence 3D3 isolated from the high
RT arsenic level Ascotan salt flat in northern Chile.";
RL Submitted (SEP-2016) 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|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:GAU76468.1}.
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DR EMBL; BDHH01000003; GAU76468.1; -; Genomic_DNA.
DR RefSeq; WP_069871806.1; NZ_BDHH01000003.1.
DR AlphaFoldDB; A0A1B6B9T5; -.
DR STRING; 1048380.F3D3_1065; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000095197; Unassembled WGS sequence.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF90; CYSTATHIONINE GAMMA-LYASE; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 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:UP000095197};
KW Transferase {ECO:0000313|EMBL:GAU76468.1}.
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 392 AA; 43287 MW; 07577EBB610D5DD2 CRC64;
MEDKFMTQLT HLGAYKNIPT TSKPKVMPIY MSSAYSFEDS DICNDICYNR EDGYLYGSYG
NPTADALKEI LLAIEGAEAC DVYASGMAAI TMAILSQVKS GDHIIANSVI YGNVFKFLKT
ELGENLGVEV TFVDFKKVDL APYFKANTKM VYMETISNPM IEVIDIGKIA DVAHQHGAKL
IIDNTFATPI VCQPIKHGAD IVVYSATKFM NGHSDIMAGI VLGSKEVIDR VVDLSHTFGP
TISPFDVWLL MRSMRTLDLR VERHSHNAMK LATFLDNHPK TGKVYYPGLP SFPDHAEAKK
YFNKGLYGGM LAVDMGSYEH IAKFVEKAQL SEIVASLGTY TTSLCDTTIT HSGMTAAERK
EAGLPEGLMR ISTGLEHIED IIGEFERILD EL
//
