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Database: UniProt
Entry: B0A7K4_9FIRM
LinkDB: B0A7K4_9FIRM
Original site: B0A7K4_9FIRM 
ID   B0A7K4_9FIRM            Unreviewed;       436 AA.
AC   B0A7K4;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=O-acetylhomoserine sulfhydrylase {ECO:0000313|EMBL:SKA60612.1};
GN   ORFNames=SAMN02745147_2578 {ECO:0000313|EMBL:SKA60612.1};
OS   Intestinibacter bartlettii DSM 16795.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Intestinibacter.
OX   NCBI_TaxID=445973 {ECO:0000313|EMBL:SKA60612.1, ECO:0000313|Proteomes:UP000190760};
RN   [1] {ECO:0000313|EMBL:SKA60612.1, ECO:0000313|Proteomes:UP000190760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16795 {ECO:0000313|EMBL:SKA60612.1,
RC   ECO:0000313|Proteomes:UP000190760};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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; FUXV01000007; SKA60612.1; -; Genomic_DNA.
DR   RefSeq; WP_007285725.1; NZ_FUXV01000007.1.
DR   AlphaFoldDB; B0A7K4; -.
DR   STRING; 261299.ERS852493_02171; -.
DR   eggNOG; COG2873; Bacteria.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000190760; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; 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}.
FT   MOD_RES         216
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   436 AA;  47644 MW;  3B9E19EAC1E82A9B CRC64;
     MANKISRKER NLKFETLQLH VGQETPDPVT DARAVPIYQT SSYVFKNCDH AAARFGLSDA
     GNIYGRLTNP TEDVFEQRMA ALEGGVAALA VASGAAALSY TFQNLAQSGD HIVAANNIYG
     GTYNYLEHTF PEYGVKTTFV DPSDLKSIED AIQENTKAVF IETLGNPNSD VVDIEAIAKI
     AHDNKIPLVI DNTFGTPYLI RPIEHGADIV VHSATKFIGG HGTTIGGVIV DGGKFDWEAS
     GKFPSLVEPN PSYHGVSFTK AAGPAAFVTK IRAILLRDTG ATLSPFHAFF FLQGLETLSL
     RVERHVENAL KVVEYLNNHP QVEKVHHPSI TDDPEQQRLY KKYFPNGAGS IFTFEIKGDA
     QKAKDFIDNL ELFSLLANVA DVKSLVIHPA STTHAQLNEE ELLACGIKPN TIRLSIGTEH
     IDDIIQDLEE AFKAVK
//
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