ID   R6E6I3_9FIRM            Unreviewed;       427 AA.
AC   R6E6I3;
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 sulfhydrolase {ECO:0000313|EMBL:CDA92211.1};
GN   ORFNames=BN710_01565 {ECO:0000313|EMBL:CDA92211.1};
OS   Ruminococcus sp. CAG:563.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1262961 {ECO:0000313|EMBL:CDA92211.1, ECO:0000313|Proteomes:UP000018082};
RN   [1] {ECO:0000313|EMBL:CDA92211.1, ECO:0000313|Proteomes:UP000018082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:563 {ECO:0000313|Proteomes:UP000018082};
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:CDA92211.1}.
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DR   EMBL; CBCR010000102; CDA92211.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6E6I3; -.
DR   STRING; 1262961.BN710_01565; -.
DR   Proteomes; UP000018082; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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   Hydrolase {ECO:0000313|EMBL:CDA92211.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018082}.
FT   MOD_RES         208
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   427 AA;  46267 MW;  9560F973A449F9BF CRC64;
     MSDYKFETLQ LHVGQENPDP ATDSRAVPIY ATTSYVFKDS AQAAGRFGLT EGGNIYTRLM
     NPTSDVFEKR IAALEGGAAA LATASGSAAI SYAIQNIAIA GDHIVSSTNL YGGTHNLFAN
     TLKEQGLDTT FVDPSDPENF EKAIQPNTKL LYAESLGNPN SDVIDLEAIA DIAHKHGIPF
     IVDSTFATPY LLRPIEHGAD VVVHSATKFI GGHGTVMGGV VIDSGKFDWA QNDKFPGLSK
     PNPSYHGVVF TEACGNLAYI LKLRTTLMRD QGATISPFNS FLLLQGLETL SLRVERHVEN
     ALKVVDFLKN HPQVERVNHP SLATGKQKEL YDKYFKKGAA SIFTFEIKGD AETAKKFTES
     LKLFSLLANV ADVKSLVIHP ASTTHSQLSE EELLSCGIKP NTVRLSIGTE HIDDIIADLQ
     QGFDAVK
//