ID   R7BEP2_9FIRM            Unreviewed;       428 AA.
AC   R7BEP2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=O-acetylhomoserine/O-acetylserine sulfhydrylase {ECO:0000313|EMBL:CDD63499.1};
GN   ORFNames=BN614_00261 {ECO:0000313|EMBL:CDD63499.1};
OS   Firmicutes bacterium CAG:341.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263019 {ECO:0000313|EMBL:CDD63499.1, ECO:0000313|Proteomes:UP000018400};
RN   [1] {ECO:0000313|EMBL:CDD63499.1, ECO:0000313|Proteomes:UP000018400}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:341 {ECO:0000313|Proteomes:UP000018400};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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}.
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:CDD63499.1}.
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DR   EMBL; CBHK010000049; CDD63499.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7BEP2; -.
DR   STRING; 1263019.BN614_00261; -.
DR   Proteomes; UP000018400; 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         210
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   428 AA;  46809 MW;  0330E0B51EED3E4E CRC64;
     MSEYKYHFET LQLHVGQEEP DPATDSRAVP IYQTTSYVFK NSDHAQARFG LADAGNIYGR
     LTNSTQDVFE QRVAALEGGV AALATASGAA ALAYTFQALA QAGDHIVSAK TIYGGTYNYL
     EHTFSQFGVT TTFVDPDNLA NFENAIQDNT KAIFIETLGN PNSNLIDIQK LADIAHSHNI
     PLVIDSTFAT PYLLRPIEYG ADIVVHSATK FIGGHGTTLG GVIVDSGNFD WKASGKYPQI
     SDPNPSYHGI SFQEAVGPAA FVTYIRAIIL RDTGATISPF NAFLLLQGLE TLSLRVERHV
     ENTKKVIEYL VNNPKVEKVN HPSIDPRYKE LYNKYFPNGA GSIFTFEIKG GEAEAKKFID
     SLKIFSILAN VADVKSLVIH PATTTHSQLS PEELAEQDIK PNTIRLSIGT EHIDDIIHDL
     DEAFAAID
//