ID   D1PMM4_9FIRM            Unreviewed;       428 AA.
AC   D1PMM4;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase {ECO:0000313|EMBL:EFB75809.1};
GN   ORFNames=SUBVAR_05587 {ECO:0000313|EMBL:EFB75809.1};
OS   Subdoligranulum variabile DSM 15176.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Subdoligranulum.
OX   NCBI_TaxID=411471 {ECO:0000313|EMBL:EFB75809.1, ECO:0000313|Proteomes:UP000003438};
RN   [1] {ECO:0000313|EMBL:EFB75809.1, ECO:0000313|Proteomes:UP000003438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15176 {ECO:0000313|EMBL:EFB75809.1,
RC   ECO:0000313|Proteomes:UP000003438};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (DEC-2009) 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:EFB75809.1}.
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DR   EMBL; ACBY02000023; EFB75809.1; -; Genomic_DNA.
DR   RefSeq; WP_007046969.1; NZ_GG704769.1.
DR   AlphaFoldDB; D1PMM4; -.
DR   STRING; 411471.SUBVAR_05587; -.
DR   GeneID; 78305784; -.
DR   eggNOG; COG2873; Bacteria.
DR   HOGENOM; CLU_018986_4_2_9; -.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000003438; 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:SF3; O-ACETYLHOMOSERINE SULFHYDRYLASE; 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:UP000003438};
KW   Transferase {ECO:0000313|EMBL:EFB75809.1}.
FT   MOD_RES         208
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   428 AA;  45829 MW;  9DC7B2B599F193F1 CRC64;
     MSQNYSINTL CVQGGYHPGN GEPRQIPIVQ STTFKYDSSD EMGKLFDLEA SGYFYSRLQN
     PTCDTVAAKI TELEGGTAGM LTSSGQAANF FALFNLCNAG DHIVSSSSIY GGTFNLIAVT
     MAKMGITATF VSPDCTEEEL DAAFTPNTKV VFGETIANPA LTVLDIEKFA AAAHRHGVPL
     VVDNTFATPV NCRPLSWGAD IVTHSTTKYM DGHGGCVGGA IVDGGKFDWM AHADKFPGLT
     TPDESYHGIT YAERFGKEGA FITKATAQLM RDLGCVQSPM SAYMLNLGLE SLHVRMARHC
     ENGQAVAEFL ASHPKIAYVN YCGLPGDKYH ALAQKYLPNG SCGVVSFGVK GGREAAANFM
     AHLKVAAIET HVADARTCCL HPASSTHRQM NDEQLIAAGV QPDLVRMSCG LEDKRDLIAD
     IEQALAQI
//