ID   A7H8Y0_ANADF            Unreviewed;       438 AA.
AC   A7H8Y0;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=O-acetylhomoserine/O-acetylserine sulfhydrylase {ECO:0000313|EMBL:ABS25176.1};
DE            EC=2.5.1.49 {ECO:0000313|EMBL:ABS25176.1};
GN   OrderedLocusNames=Anae109_0967 {ECO:0000313|EMBL:ABS25176.1};
OS   Anaeromyxobacter sp. (strain Fw109-5).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=404589 {ECO:0000313|EMBL:ABS25176.1, ECO:0000313|Proteomes:UP000006382};
RN   [1] {ECO:0000313|EMBL:ABS25176.1, ECO:0000313|Proteomes:UP000006382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fw109-5 {ECO:0000313|EMBL:ABS25176.1,
RC   ECO:0000313|Proteomes:UP000006382};
RX   PubMed=25614562; DOI=10.1128/genomeA.01449-14;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA   Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA   Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA   Loeffler F.E., Fields M.W.;
RT   "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT   metal-reducing bacterium isolated from a contaminated subsurface
RT   environment.";
RL   Genome Announc. 3:0-0(2015).
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; CP000769; ABS25176.1; -; Genomic_DNA.
DR   RefSeq; WP_011985282.1; NC_009675.1.
DR   AlphaFoldDB; A7H8Y0; -.
DR   STRING; 404589.Anae109_0967; -.
DR   KEGG; afw:Anae109_0967; -.
DR   eggNOG; COG2873; Bacteria.
DR   HOGENOM; CLU_018986_4_0_7; -.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000006382; Chromosome.
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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006382}.
FT   MOD_RES         213
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   438 AA;  46964 MW;  F38D0DF6B69A19BA CRC64;
     MTIPPDRKLR FETLQVHAGQ EPAPGTNARA VPIYQTTSYT FDSAEHGANL FALKEFGNIY
     TRIMNPTTDV FEKRIAALEG GVAALATASG QAAQFLAIAN IAQAGDNVVS TSLLYGGTYN
     QFKVTLPRLG IGVKLVDGDD VAALRKAIDG KTKALYVESI GNPAGNVPDF EALARVAHEN
     GIPLIVDNTF GAGGYLVRPI EHGADVVVES ATKWIGGHGT SIGGVIVDSG KFDWAASGKF
     PVFTEPSPGY HGLVFNDVFG PKGPFGNIQF IIRARVEGLR DLGPALSPFN SFLLLQGLET
     LSLRVQRQVD NALALAQWLK AHRSVAWVNY TGLEEHPYHQ RARKYLRNGF GGVFTFGIKG
     GYEAGKTFID EVKLASHLAN VGDAKTLVIH PASTTHQQLS EAEQKSAGVT PDQIRVSAGI
     EHLDDIKEDF EAAFAAAR
//